WO2023178182A1

WO2023178182A1 - Compositions and methods for detection and treatment of coronavirus infection

Info

Publication number: WO2023178182A1
Application number: PCT/US2023/064439
Authority: WO
Inventors: Wyatt James MCDONNELL
Original assignee: 10X Genomics, Inc.
Priority date: 2022-03-16
Filing date: 2023-03-15
Publication date: 2023-09-21

Abstract

The present disclosure relates generally to compositions comprising antigen-binding molecules that bind to a severe acute respiratory syndrome coronavirus (SARS-CoV), and/or comprising nucleic acids that encode such antigen-binding molecules, as well as therapeutic and diagnostic methods for using such compositions.

Description

COMPOSITIONS AND METHODS FOR DETECTION AND TREATMENT OF CORONAVIRUS INFECTION CROSS-REFERENCE TO RELATED APPLICATION [0001] This application claims the benefit of and priority to U.S. Provisional Patent Application Serial Nos.63/320,491, filed on March 16, 2022; 63/326,144, filed on March 31, 2022; and 63/377,521, filed on September 28, 2022. The disclosures of the above-referenced applications are herein expressly incorporated by reference it their entireties, including any drawings. FIELD [0002] The present disclosure relates generally to compositions comprising antigen- binding molecules that bind to a severe acute respiratory syndrome coronavirus (SARS-CoV), and/or comprising nucleic acids that encode such antigen-binding molecules, as well as therapeutic and diagnostic methods for using such compositions. INCORPORATION OF THE SEQUENCE LISTING [0003] This application contains a Sequence Listing, which is hereby incorporated herein by reference in its entirety. The accompanying Sequence Listing, named “057862-610001WO _SequenceListing_ST26.xml,” was created on March 7, 2023 and is 9.6 MB. BACKGROUND [0004] In the past decades, three novel coronaviruses (CoVs) have crossed from zoonotic hosts into humans and acquired the ability to spread by human-to-human transmission. Two of these pandemic CoVs, severe acute respiratory syndrome (SARS)-CoV in 2002 and Middle East respiratory syndrome (MERS)-CoV in 2012, caused relatively small outbreaks of human respiratory disease. The third, SARS-CoV-2 is a recently identified emerging coronavirus causing an acute respiratory distress syndrome known as COVID-19 that is similar to severe acute respiratory syndrome (SARS) caused by the closely related SARS-CoV. To date, SARS- CoV-2 is continuing its spread across the world with nearly 460 million confirmed cases in over 200 countries and more than six million deaths. While current vaccines still provide some protection against circulating SARS-CoV-2 variants, the ongoing emergence of increasingly diverse variants and the possibility of future spillovers of novel CoVs make pan-CoV vaccine development a public health issue of the highest priority. [0005] In view of the continuing threat to human health, there is an urgent need for preventive and therapeutic antiviral therapies for SARS-CoV-2 control. Because this virus uses its spike glycoprotein for interaction with the cellular receptor ACE2 and the serine protease TMPRSS2 for entry into a target cell, this spike (S) protein represents a target for antibody therapeutics. In particular, the immunogenic property of the S protein, including its ability to induce neutralizing antibodies and its essential role in viral attachment and fusion, make it a promising target for developing effective immunotherapy against SARS-CoV infection. For example, fully human antibodies that specifically bind to the SARS-CoV-2 spike protein with high affinity and that inhibit virus infectivity could be important in the prevention and treatment of coronavirus infection. [0006] It has been reported that during an outbreak, the SARS-CoV can mutate and exhibit antigenic variation. In fact, sequence analysis indicated that the clinical isolates could be divided into early, middle, and late isolates. The significance of this is demonstrated in the ability of later isolates to escape neutralization by a monoclonal antibody that effectively neutralized an earlier isolate. Therefore, it is important to produce neutralizing antibodies that are effective against a wide range of clinical isolates with antigenic diversity. Because of the potential evolution of antigenic variants, an effective passive therapy against SARS-CoV will likely contain a cocktail of neutralizing antibodies that target different epitopes and/or steps in the entry process, such as blocking receptor binding and fusion. [0007] Accordingly, there remains an urgent need for potent, broad-spectrum antibody therapeutics for use in preventing and/or treating SARS- CoV infection. In particular, there is a need for antibodies with specific binding affinity to the SARS-CoV-2 spike protein, including neutralizing therapeutic antibodies and their use for treating or preventing coronavirus infection. Furthermore, there is a continuing need for formulations and methods for delivering a functional antibody therapeutic or for expressing a functional form of an antibody therapeutic within a subject who suffers from coronavirus infection. The present disclosure addresses this need, in part, by providing anti-SARS-CoV-2 S antibodies and methods of using the same in the prevention, diagnosis, prognosis, monitoring, evaluation, and/or treatment of viral infections. SUMMARY [0008] This present disclosure relates generally to compositions, including without limitation lipid-based nanoparticle (LNP) formulations, comprising an antigen-binding molecule or a combination of two, three, four, or more antigen-binding molecules , e.g., antigen-binding polypeptides, antibodies, and antigen-binding fragments that specifically bind to a severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), nucleic acids encoding such antigen-binding molecules, and/or combinations thereof. Also provided are methods for manufacturing such LNP compositions, therapeutic and diagnostic methods using the compositions described herein, as well as kits for preventing, treating, diagnosing, or imaging a virus, a disease, a disorder, and/or a health condition using the compositions described herein. [0009] In one aspect of the disclosure, provided herein are compositions including a nucleic acid encoding an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), wherein the antigen- binding molecule or antigen-binding fragment thereof includes all six complementary determining regions (CDRs) from an antibody of the disclosure. In certain embodiments, the compositions of the invention are formulated in any formulation suitable for a therapeutic delivery of compositions comprising nucleic acids and/or proteins. In certain embodiments, the composition is formulated in a lipid-based nanoparticle (LNP). In some embodiments, the antigen-binding molecule, an antigen-binding fragment includes all six CDRs from an antibody identified in Tables 1A-1B. In some embodiments, the antigen-binding molecule or antigen- binding fragment is any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, and wherein optionally the composition is formulated in a lipid-based nanoparticle (LNP). [0010] In one aspect, provided herein are compositions including an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof includes all six CDRs from an antibody of the disclosure. In certain embodiments, the compositions of the invention are formulated in any formulation suitable for a therapeutic delivery of compositions comprising nucleic acids and/or proteins. In certain embodiments, the composition is formulated in a lipid- based nanoparticle (LNP). In some embodiments, the antigen-binding molecule, an antigen- binding fragment includes all six CDRs from an antibody identified in Tables 1A-1B. In some embodiments, the antigen-binding molecule, an antigen-binding fragment is any one of TXG- 0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, and wherein optionally the composition is formulated in a lipid-based nanoparticle (LNP). [0011] Non-limiting exemplary embodiments of the compositions the disclosure can include one or more of the following features. In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof includes all six complementary determining regions (CDRs) from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG- 0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203. In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for a spike (S) protein of SARS-CoV-2. [0012] In some embodiments, the nucleic acid encoding an antigen-binding molecule, or an antigen-binding fragment thereof, is a DNA molecule or an RNA molecule. In some embodiments, the RNA molecule is a messenger RNA (mRNA) molecule. In some embodiments, the nucleic acid includes one or more modified nucleosides. In some embodiments, the one or more modified nucleosides includes pyridin-4-one ribonucleoside, 5- aza-uridine, 2-thio- 5-aza-uridine, 2-thiouridine, 4-thio-pseudouridine, 2-thio-pseudouridine, 5- hydroxyuridine, 3-methyluridine, 5-carboxymethyl-uridine, 1-carboxymethyl- pseudouridine, 5- propynyl-uridine, 1-propynyl-pseudouridine, 5-taurinomethyluridine, 1- taurinomethyl- pseudouridine, 5-taurinomethyl-2-thio-uridine, 1 -taurinomethyl-4-thio- uridine, 5-methyl- uridine, 1-methyl-pseudouridine, 4-thio-l-methyl-pseudouridine, 2- thio- 1 -methyl- pseudouridine, 1 -methyl- 1 -deaza-pseudouridine, 2-thio- 1 -methyl- 1 -deaza- pseudouridine, dihydrouridine, dihydropseudouridine, 2-thio-dihydrouridine, 2-thio- dihydropseudouridine, 2- methoxyuridine, 2-methoxy-4-thio-uridine, 4-methoxy- pseudouridine, 4-methoxy-2-thio- pseudouridine, 5-aza-cytidine, pseudoisocytidine, 3- methyl-cytidine, N4-acetylcytidine, 5- formylcytidine, N4-methylcytidine, 5- hydroxymethylcytidine, 1 -methyl-pseudoisocytidine, pyrrolo-cytidine, pyrrolo- pseudoisocytidine, 2-thio-cytidine, 2-thio-5-methyl-cytidine, 4-thio- pseudoisocytidine, 4- thio- 1 -methyl-pseudoisocytidine, 4-thio- 1 -methyl- 1 -deaza- pseudoisocytidine, 1 -methyl- 1 -deaza-pseudoisocytidine, zebularine, 5-aza-zebularine, 5- methyl-zebularine, 5-aza-2- thio-zebularine, 2-thio-zebularine, 2-methoxy-cytidine, 2-methoxy- 5-methyl-cytidine, 4- methoxy-pseudoisocytidine, 4-methoxy- 1 -methyl-pseudoisocytidine, 2- aminopurine, 2, 6-diaminopurine, 7-deaza-adenine, 7-deaza-8-aza-adenine, 7-deaza-2- aminopurine, 7- deaza-8-aza-2-aminopurine, 7-deaza-2,6-diaminopurine, 7-deaza-8-aza-2,6- diaminopurine, 1 -methyladenosine, N6-methyladenosine, N6-isopentenyladenosine, N6- (cis- hydroxyisopentenyl)adenosine, 2-methylthio-N6-(cis-hydroxyisopentenyl) adenosine, N6- glycinylcarbamoyladenosine, N6-threonylcarbamoyladenosine, 2- methylthio-N6-threonyl carbamoyladenosine, N6,N6-dimethyladenosine, 7- methyladenine, 2-methylthio-adenine, and 2- methoxy-adenine, inosine, 1 -methyl-inosine, wyosine, wybutosine, 7-deaza-guanosine, 7-deaza- 8-aza-guanosine, 6-thio-guanosine, 6- thio-7-deaza-guanosine, 6-thio-7-deaza-8-aza-guanosine, 7-methyl-guanosine, 6-thio-7- methyl-guanosine, 7-methylinosine, 6-methoxy-guanosine, 1 - methylguanosine, N2- methylguanosine, N2,N2-dimethylguanosine, 8-oxo-guanosine, 7-methyl- 8-oxo- guanosine, l-methyl-6-thio-guanosine, N2-methyl-6-thio-guanosine, and N2,N2- dimethyl-6-thio-guanosine, and combinations thereof. [0013] In some embodiments, the lipid nanoparticle includes an ionizable cationic lipid, a cationic lipid, an anionic lipid, a neutral lipid, a sterol, a PEG-modified lipid, or a combination of any thereof. In some embodiments, the lipid nanoparticle further includes phosphatidyl choline. In some embodiments, the sterol is cholesterol. In some embodiments, the mean ratio of lipid to nucleic acid (wt/wt) ranges from about 2:1 to about 100:1. In some embodiments, the LNP has a mean diameter ranging from about 10 nm to about 200 nm. [0014] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike (S) protein of two, three, four, five or more variants of SARS- CoV-2. In some embodiments, the SARS-CoV-2 variants are any one of alpha, beta, delta, gamma, kappa, omicron, or a combination thereof. In some embodiments, at least one of the SARS-CoV-2 variants is omicron. In some embodiments, the antigen-binding molecule or antigen-binding fragment further has a binding affinity for one or more human coronaviruses (HCoVs) that is any one of HCoV-229E, HCoV-OC43, HCoV-HKU1, or a combination thereof, or a variant of any thereof. In some embodiments, the one or more HCoVs is HCoV-229E, HCoV-OC43, or a combination thereof. [0015] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a sub-nanomolar binding affinity for a spike (S) protein of SARS-CoV-2, a fragment thereof, or a multimeric form thereof. In some embodiments, the antigen-binding molecule or antigen- binding fragment has a sub-picomolar binding affinity for a SARS-CoV-2 S protein, a fragment thereof, or a multimeric form thereof. In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for S1 subunit of the SARS-CoV-2 S protein. In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for a receptor binding domain (RBD) and/or a N-terminal domain (NTD) of the S1 subunit. In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity to the NTD of the S1 subunit. In some embodiments, the antigen- binding molecule or antigen-binding fragment thereof has binding affinity for a trimeric form of the SARS-CoV-2 S protein. [0016] In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof comprises all framework regions (FWRs) from the antibody being any one identified in Tables 1A-1B. In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof includes all FWRs from the antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0017] In some embodiments, the antigen-binding molecule or antigen-binding fragment further includes a heavy chain constant region. In some embodiments, the heavy chain constant region is an IgA, IgD, IgE, IgG, or IgM heavy chain constant region. In some embodiments, the heavy chain constant region is of the same isotype and subclass as the antibody identified in Tables 1A-1B. In some embodiments, the heavy chain constant region is of the same isotype and subclass as the antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG- 0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. In some embodiments, the antigen-binding molecule or antigen-binding fragment further includes a light chain constant region. In some embodiments, the light chain constant region is a kappa type or lambda type light chain constant region. In some embodiments, the light chain constant region is the same light chain constant region of the antibody identified in Tables 1A-1B. In some embodiments, the light chain constant region is the same light chain constant region of the antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG- 0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0018] In one aspect, provided herein are methods for reducing binding of a spike (S) protein of a coronavirus (CoV-S) to a cell in a subject and/or reducing entry of the coronavirus into a cell of a subject, wherein the methods include administering (e.g., therapeutically or prophylactically) to the subject: (a) an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike (S) protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof includes all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, and wherein optionally the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the spike (S) protein of two, three, four, five or more variants of SARS-CoV-2, and/or for one or more human coronaviruses (HCoVs) that is any one of HCoV-229E, HCoV-OC43, HCoV-HKU1, or a combination thereof, or a variant of any thereof; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof of (a). In some embodiments, the one or more HCoVs is HCoV-229E, HCoV-OC43, or a combination thereof. [0019] In another aspect, provided herein are methods for inducing an immune response in a subject, wherein the methods include administering (e.g., therapeutically or prophylactically) to the subject a composition as disclosed herein. [0020] In another aspect, provided herein are methods for aiding in the neutralization of two, three, four, five or more variants of SARS-CoV-2, wherein said aiding includes providing: (a) an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike (S) protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof includes all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen- binding fragment thereof of (a). [0021] In another aspect, provided herein are methods for aiding in the neutralization of two, three, four, five or more variants of SARS-CoV-2, wherein said aiding includes providing a composition comprising a nucleic acid encoding an antigen-binding molecule, or an antigen- binding fragment thereof, that binds to a severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), wherein the antigen-binding molecule is any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0022] In yet another aspect, provided herein are methods for reducing a viral load of two, three, four, five or more variants of SARS-CoV-2, wherein the method includes providing: (a) an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike (S) protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof includes all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen- binding fragment thereof of (a). [0023] In another aspect, provided herein are methods for aiding in the neutralization of two, three, four, five or more variants of SARS-CoV-2, wherein said aiding includes providing a composition as disclosed herein. In another aspect, provided herein are methods for reducing the viral load of two, three, four, five or more variants of SARS-CoV-2, wherein the method includes providing a composition as disclosed herein. [0024] Non-limiting exemplary embodiments of the methods as described herein can include one or more of the following features. In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof includes all six complementary determining regions (CDRs) from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG- 0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203. In some embodiments, the subject is suspected of being infected with a coronavirus, has been diagnosed of having or at risk of having a coronavirus infection, has been infected with a coronavirus, has been vaccinated, or has been recovered from a coronavirus infection. In some embodiments, the subject is an immunocompromised subject or has been previously treated for coronavirus infection. In some embodiments, the subject is a mammalian subject. In some embodiments, the mammalian subject is a human subject. In some embodiments, the coronavirus belongs to a genus being any one of alphacoronavirus, betacoronavirus, gammacoronavirus, or deltacoronavirus. In some embodiments, the coronavirus belongs to a betacoronavirus lineage is any one of lineage A, lineage B, lineage C, or lineage D. In some embodiments, the coronavirus is human coronavirus 229E, OC43, HKU1, NL63, SARS- CoV-1, SARS-CoV-2, MERS-CoV, or a variant of any thereof. In some embodiments, the coronavirus is SARS-CoV-2 or a variant thereof being any one of alpha, beta, delta, gamma, kappa, omicron, or a combination thereof. In some embodiments, one of the two, three, four, five or more variants of SARS-CoV-2 is omicron. In some embodiments, one of the one or more of the HCoVs is HCoV-229E or HCoV-OC43; and HCoV-HKU1 is HCoV-229E or HCoV-OC43. [0025] In some embodiments of the methods disclosed herein, the composition is therapeutically or prophylactically administered at a total dose of about 0.1 mg/kg to about 40 mg/kg. Dosing can be single dosage or cumulative (serial dosing), and can be readily determined by one skilled in the art. For example, treatment of a viral infection can comprise a one-time administration of an effective dose of a pharmaceutical composition disclosed herein. Alternatively, treatment of viral infection may include multiple administrations of an effective dose of a pharmaceutical composition carried out over a range of time periods, such as, e.g., once daily, twice daily, trice daily, once every few days, or once weekly. The timing of administration can vary from individual to individual, depending upon such factors as the severity of an individual's symptoms and/or viral load. For example, an effective dose of a pharmaceutical composition disclosed herein can be administered to an individual once daily for an indefinite period of time, or until the individual no longer requires therapy. A person of ordinary skill in the art will recognize that the condition of the individual can be monitored throughout the course of treatment and that the effective amount of a pharmaceutical composition disclosed herein that is administered can be adjusted accordingly. [0026] In some embodiments, the composition is therapeutically or prophylactically administered on a defined schedule such as three time a day, twice a day, once a day, every other day, every third day, weekly, biweekly, every three weeks, every four weeks, and monthly. In some embodiments, the total dose is administered by multiple administrations. In some embodiments, the multiple administrations occur on a defined schedule such as three times a day, twice a day, once a day, every other day, every third day, weekly, biweekly, every three weeks, every four weekly, and monthly. The compositions of the disclosure may be administered parenterally. The compositions may be administered directly into the blood stream, into tissue, into muscle, or into an internal organ. In some embodiments, administration may be systemic, e.g., to injection or infusion. In some embodiments, administration may be local. Suitable means for administration include intravenous, intraarterial, intrathecal, intraventricular, intraurethral, intrasternal, intracranial, subretinal, intravitreal, intra-anterior chamber, intramuscular, intrasynovial and subcutaneous. Suitable devices for administration include needle (including microneedle) injectors, needle-free injectors and infusion techniques. In some embodiments, the composition is administered by intradermal, intravenous, intramuscular, subcutaneous injection, and/or local administration. In some embodiments, the composition is administered intradermal or intramuscular injection. [0027] In some embodiments, the administered composition reduces binding of the CoV-S protein to and/or reduces coronavirus entry into a cell of the subject. In some embodiments, the administered composition neutralizes against the coronavirus. In some embodiments, the administered composition treats, prevents, or ameliorates a heath condition associate with a coronavirus infection in the subject. In some embodiments, the administered composition reduces the viral load in the subject as compared to a reference subject who has not been administered with the composition. In some embodiments, the methods further include administering to the subject an additional therapy. In some embodiments, the additional therapy includes an anti-viral agent being any one of interferon, Remdesivir, Baricitinib, Azithromycin, Nirmatrelvir, Ritonavir, Molnupiravir, Casirivimab, Imdevimab, Bamlanivimab, Etesevimab, Sotrovimab, Cilgavimab, Bebtelovimab, Tocilizumab, Tixagevimab, or a combination thereof. [0028] In another aspect, provided herein are methods for detecting the presence of SARS- CoV-2 S protein and/or SARS-CoV-2 in a biological sample, the method comprising contacting a biological sample with an antigen-binding molecule having an amino acid sequence being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, or an antigen-binding fragment of any thereof, wherein optionally the antigen-binding molecule or antigen-binding fragment has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof. In some embodiments, the antigen- binding molecule or antigen-binding fragment thereof includes all six complementary determining regions (CDRs) from an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203. [0029] Non-limiting exemplary embodiments of the detection methods as described herein can include one or more of the following features. In some embodiments, the biological sample is from a subject suspected of being infected with a coronavirus, has been diagnosed of having or at risk of having a coronavirus infection, has been infected with a coronavirus, has been vaccinated, or has been recovered from a coronavirus infection. In some embodiments, the methods further include detecting a complex formed between the antigen-binding molecule or antigen-binding fragment thereof with a SARS-CoV-2 S antigen. In some embodiments, said detecting includes visualizing the complex by using an enzyme, a secondary antibody, a colored dye, a fluorescent dye, a chemiluminescent molecule, a molecule containing a radioactive atom, or a molecule containing a heavy metal. [0030] In another aspect, provided herein are methods for aiding in the diagnosis, prognosis, monitoring, and/or evaluation of a coronavirus infection and/or treatment thereof in a subject, wherein said aiding includes providing: (a) an antigen-binding molecule having an amino acid sequence being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG- 0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, or an antigen-binding fragment of any thereof, wherein optionally the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more common HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof. [0031] In another aspect, provided herein are kits for preventing, treating, diagnosing, or imaging a virus, a disease, a disorder, and/or health condition, the kits include (a) an antigen- binding molecule, or an antigen-binding fragment of any thereof, including all 6 CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG- 0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, wherein optionally the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more common HCoVs that is 229E, OC43, HKU1, or a combination thereof; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof of (a); and instructions for performing a method of preventing, treating, diagnosing, or imaging a virus, a disease, a disorder, and/or health condition as disclosed herein. [0032] In another aspect, provided herein are methods of manufacturing a pharmaceutical composition, the methods including: (a) admixing a lipid solution with an aqueous buffer solution including a buffer agent thereby forming a lipid nanoparticle solution including a lipid nanoparticle (LNP); and (b) adding to the lipid nanoparticle: (i) an antigen-binding molecule, or an antigen-binding fragment include any thereof, including all 6 CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, wherein optionally the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more common HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof; and/or (ii) a nucleic acid encoding the antigen-binding molecule or antigen- binding fragment thereof of (a), thereby forming a LNP formulation including the LNP associated with the antigen-binding molecule or antigen-binding fragment thereof, and/or with the nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof. [0033] The foregoing summary is illustrative only and is not intended to be in any way limiting. In addition to the illustrative embodiments and features described herein, further aspects, embodiments, objects and features of the disclosure will become fully apparent from the drawings and the detailed description and the claims. BRIEF DESCRIPTION OF THE DRAWINGS [0034] FIG.1 shows an exemplary scheme for antigen-specific enrichment of B cells by using fluorescence-activated cell sorting (FACS) technique. In these experiments, cells were initially gated on being single, live (7AAD^negative) and PE-Cy7-CD19+ and then sorted on their PE and/or APC status directly into master mix and water. In this figure, Y axis represents PE signal (pre-fusion trimerized SARS-2 glycoprotein S antigen+ and/or HSA+ control antigen- binding cells). X axis represents APC signal (trimerized SARS-2 S glycoprotein D614G antigen+ and/or HSA+ control antigen-binding cells). Numbers adjacent to each gate name represent the fraction of events relative to the parent population (single, live, CD19+ cells) for that gate. [0035] FIG.2 schematically illustrates that the new scoring system described herein allowed for determining relative K_D values which in turn facilitate identification of binding antibodies with good dynamic range of reporter oligonucleotides. [0036] FIGS.3A-3B schematically depict the results of representative analysis performed to illustrate that the new scoring system described herein allow for selection of high-affinity antibodies with a data set. In this analysis, BEAM scores are approximately normally distributed, increase exponentially as target antigen-binding relative to expressed antibody and control antigen increases, are correlated with generation probability of the HCDR3 junction, e.g., following the known general relationship of somatic hypermutation (SHM) and increasing affinity, and also reveal that class switching increases predicted relative affinity in concordance with the literature. [0037] FIG.4 schematically summarizes the results of representative analysis performed to illustrate clonotype enrichment based on relative KD. BEAM scores were found to be also generally higher within sublineages that contain more daughter antibodies than narrow sublineages. [0038] FIG.5 shows an exemplary microfluidic channel structure for partitioning individual biological particles in accordance with some embodiments of the disclosure. [0039] FIG.6 shows an exemplary microfluidic channel structure for the controlled partitioning of beads into discrete droplets. [0040] FIG.7 shows an exemplary barcode carrying bead. [0041] FIG.8 illustrates another example of a barcode carrying bead. [0042] FIG.9 schematically illustrates an example microwell array. [0043] FIG.10 schematically illustrates an example workflow for processing nucleic acid molecules. [0044] FIG.11 schematically illustrates examples of labelling agents. [0045] FIG.12 depicts an example of a barcode carrying bead. [0046] FIGS.13A, 13B and 13C schematically depict an example workflow for processing nucleic acid molecules. [0047] FIG.14 shows an exemplary microfluidic channel structure for delivering barcode carrying beads to droplets. [0048] FIGS.15A and 15B depict the amino acid sequences of a wild-type SARS-CoV spike protein (FIG.15A) and a variant SARS-CoV spike protein (FIG.15B). Various mutations have been introduced and indicated by the original amino acids above the mutated amino acids. These mutations fall in 3 classes: 1) proline stabilization/S2P mutations (F817P, A892P, A899P, A942P, K986P, V987P), 2) alanine stabilization mutations (R683A, R685A), and 3) viral variant mutations (D614G). The asterisks in the sequences indicate the start and end of the sequences used to produce the antigens used in the experiments described in the Examples below. The C- terminal end of the antigens (ending at the 2nd asterisk) is fused to the T4 trimerization domain and the His tag. [0049] FIGS.16A-16B schematically summarize the results of representative SPR analyses performed to evaluate binding affinity of exemplary antibodies of the disclosure to the following antigens: (1) a trimerized wild-type SARS-CoV-2 S protein (FIG.16A), (2) a SARS- CoV-2 S protein variant with D614G substitution (FIG.16B). [0050] FIG.17A summarizes the results of experiments performed to assess RBD binding kinetics. A triple mutant RBD containing triple amino acid substitutions K417N, E484K, and N501Y was used. FIG.17B: RBD kinetics in comparison to FDA-approved therapeutic antibodies. [0051] FIG.18A depicts binding kinetics of hypothetical antibodies having the same KD value 10 nM, with varying kon and koff rates. Red and yellow curves depict optimal binding kinetics of antibodies having high therapeutic potential due to binding stability, while green and blue curves depict less optimal binding kinetics. [0052] FIG.18B depicts binding kinetics of exemplary TXG antibodies and FDA- approved or late clinical development stage spike antibodies (data from each antibody shown in triplicate). Antibodies having optimal binding kinetics are depicted in FIG.18B as boxes with asterisk symbols (*). Antibodies having less optimal binding kinetics are depicted in FIG.18B as boxes with solid circle (●). FDA-approved or late clinical development stage spike antibodies used as positive controls are depicted as boxes with solid triangle (▲). [0053] FIG.18C depicts the relationship between Koff of a given TXG antibody to the pre-fusion trimeric spike and its binding kinetics. Koff is shown here for the purpose of brevity as half-life and mean-life kinetics of a receptor-ligand pair are determined by the Koff of the interaction and not the Kon or the ratio of Koff to Kon (KD). Box plots are shown for each kinetic profile described above and shown in FIG.18C. Twenty-seven (27) antibodies are shown as having a Koff rate of 1e-05, indicating they have surpassed the lower limit of detection from the SPR data and therefore have lower estimated KD values than those reported in the provided data. [0054] FIG.18D depicts the relationship between Koff and Kon of given TBS-antibodies to the pre-fusion trimeric spike, color coded by kinetic profile. [0055] FIG.19 schematically depicts binding affinity of exemplary antibodies to wild-type SARS-CoV-2 S protein, illustrating that the majority of tested antibodies could bind to wild-type S protein in picomolar and nanomolar range. Remarkably, several antibodies described herein were found to have binding affinities as good as or superior to FDA-approved antibodies or antibodies in late clinical development. [0056] FIG.20 schematically depicts the general procedure of live virus neutralization assay employed to determine the anti-SARS-CoV-2 activity of various antibodies described herein. [0057] FIG.21 depicts representative raw data from neutralization assay described in FIG. 20. CTRL-0004: Casirivimab; CTRL-0006: Bamlanivimab; CTRL-0007: Etesevimab; CTRL- 0008: Sotrovimab; CS478 pi_vac_pf1, positive plasma control of Pfizer vaccine. [0058] FIG.22 depicts representative neutralization percentage from neutralization assay described in FIG.20. CTRL-0004: Casirivimab; CTRL-0006: Bamlanivimab; CTRL-0007: Etesevimab; CTRL-0008: Sotrovimab; CS478 pi_vac_pf1, positive plasma control of Pfizer vaccine. [0059] FIG.23 schematically depicts representative neutralization curves (ID50) of four FDA-approved antibodies or antibodies in late clinical development (controls). CTRL-0004: Casirivimab; CTRL-0006: Bamlanivimab; CTRL-0007: Etesevimab; CTRL-0008: Sotrovimab; CS478 pi_vac_pf1, positive plasma control of Pfizer vaccine. [0060] FIG.24 schematically depicts representative neutralization curves (ID50) of six exemplary antibodies in accordance with some embodiments of the disclosure. [0061] FIG.25 schematically depicts an UpSet plot wherein antibodies are binned into antigen bins based on two rounds of SPR binding affinity data. For an antibody to be placed into a bin a detectable kinetic fit at all concentrations of antigen was required from at least one of the SPR experiments described in Examples 9 and 12, or orthogonal neutralization data. [0062] FIG.26 schematically depicts an UpSet plot of antibodies identified as having neutralization activity against live SARS-COV-2, wherein the antibodies are binned into antigen bins as described in FIG.25. [0063] FIGS.27A and 27B depict UpSet plots of the potently (IC50 <= 1000 ng / ml) neutralizing antibodies retrieved in this BEAM-seq workflow. FIG.27A is an Upset plot of the potently neutralizing antibodies selected from 239 antibodies identified in Example 6. FIG.27B is an Upset plot of the potently neutralizing antibodies selected from the antibodies of Table 4. In these figures, rows represent the binding of these neutralizing antibodies to pre-fusion spike trimers from major SARS-CoV-2 variants of concern, and the endemic HKU1 coronavirus spike protein as well as the SARS-CoV-2 N terminal domain. [0064] FIG.28 schematically summarizes of the neutralization potency of the antibodies described in Table 10 as determined in testing against SARS-CoV-2. The neutralization potency of an antibody is generally quantified by the inhibitory concentration (IC) values (e.g., IC₅₀) in live SARS-CoV-2 assays (see also, Table 11) [0065] FIG.29 is a heat map summarizing results of the epitope binning assays described in Example 14, wherein antibodies were tested against one another in a pairwise and combinatorial fashion for binding to a specific target antigen, i.e., pre-fusion trimerized spike protein from SARS-CoV-2 USA-WA1/2020 isolate. [0066] FIG.30 is a heat map summarizing results of the epitope binning assays described in Example 14, wherein antibodies were tested against one another in a pairwise and combinatorial fashion for binding to spike protein from SARS-CoV-2 delta variant. [0067] FIG.31 schematically depicts an UpSet plot wherein antibodies are binned into antigen bins based on multiple rounds of SPR binding affinity data. For an antibody to be placed into a bin a detectable kinetic fit at all concentrations of antigen was required from at least one of the SPR experiments described in Examples 9 and 12. As illustrated in FIG.31, the recovered antibodies have a range of binding breadths including binding to multiple endemic coronaviruses and SARS-CoV-2 variants, and that most of the antibodies recovered successfully bind multiple SARS-CoV-2 variants. [0068] FIGS.32A-32D summarize the results of experiments demonstrating that TXG- 0078 is an NTD supersite-targeting mAb that can bind alpha- and betacoronaviruses. FIG.32A: 3.9Å cryo-electron microscopy image of the digested Fab of TXG-0078 in complex with the spike trimer from the SARS-CoV-2 Wuhan entry strain (WT). FIG.32B: 4A8 sequence threading into the TXG-0078:spike structure, revealing that TXG-0078 targets the NTD supersite as has been described for other antibodies. FIG.32C: the N3 and N5 loops comprise the epitope of TXG-0078; the longer CDRH3 of TXG-0078 reaches into a pocket in the N5 loop and the light chain is only minimally engaged in binding. FIG.32D: A 3Å negative stain EM image of TXG-0078 in complex with the Wuhan spike trimer. [0069] FIGS.33A-33B summarize the results of experiments illustrating that TXG-0078 protects transgenic ACE2 mice from live SARS-CoV-2 challenge. FIG.33A: Mice were administered 20 μg of (i) TXG-0078, (ii) a reference RBD-targeting antibody, or (iii) Control 1 (antibody targeting Zika virus (ZIKV)). Mean percent change in baseline weight is shown for each group ± SEM. FIG.33A: Percent baseline weight at Day 5 is shown for all mice (n=15), with mean and SEM shown for each group. DETAILED DESCRIPTION OF THE DISCLOSURE [0070] In the following detailed description, reference is made to the accompanying drawings, which form a part hereof. In the drawings, similar symbols generally identify similar components, unless context dictates otherwise. The illustrative alternatives described in the detailed description, drawings, and claims are not meant to be limiting. Other alternatives may be used and other changes may be made without departing from the spirit or scope of the subject matter presented here. It will be readily understood that the aspects, as generally described herein, and illustrated in the Figures, can be arranged, substituted, combined, and designed in a wide variety of different configurations, all of which are explicitly contemplated and make part of this application. [0071] Unless otherwise defined, all terms of art, notations, and other scientific terms or terminology used herein are intended to have the meanings commonly understood by those of skill in the art to which this application pertains. In some cases, terms with commonly understood meanings are defined herein for clarity and/or for ready reference, and the inclusion of such definitions herein should not necessarily be construed to represent a substantial difference over what is generally understood in the art. Many of the techniques and procedures described or referenced herein are well understood and commonly employed using conventional methodology by those skilled in the art. D^EFINITIONS [0072] Unless otherwise defined, all terms of art, notations and other scientific terms or terminology used herein are intended to have the meanings commonly understood by those of skill in the art to which this disclosure pertains. In some cases, terms with commonly understood meanings are defined herein for clarity and/or for ready reference, and the inclusion of such definitions herein should not necessarily be construed to represent a substantial difference over what is generally understood in the art. Many of the techniques and procedures described or referenced herein are well understood and commonly employed using conventional methodology by those skilled in the art. [0073] The singular form “a,” “an,” and “the” include plural references unless the context clearly dictates otherwise. For example, the term “a cell” includes one or more cells, including mixtures thereof. “A and/or B” is used herein to include all of the following alternatives: “A,” “B,” “A or B,” and “A and B.” [0074] As used herein, a “subject” or an “individual” includes animals, such as human (e.g., human individuals) and non-human animals. The term “non-human animals” includes all vertebrates, e.g., mammals, e.g., rodents, e.g., mice, non-human primates, and other mammals, such as e.g., rat, mouse, cat, dog, cow, pig, sheep, horse, goat, rabbit; and non-mammals, such as amphibians, reptiles, etc. A subject can be a mammal, preferably a human or humanized animal, e.g., an animal with humanized or human VDJC loci. The subject may be a non-human animal (e.g., a non-human mammal) with human VDJ loci and non-human C loci. The subject may be non-human animals with humanized or human VDJC loci and knockouts of a target of interest. The subject may be in need of prevention and/or treatment of a disease or disorder such as viral infection or cancer. The subject may have a viral infection, e.g., a coronavirus infection, or be predisposed to developing an infection. Subjects predisposed to developing an infection, or subjects who may be at elevated risk for contracting an infection (e.g., of coronavirus), include subjects with compromised immune systems because of autoimmune disease, subjects receiving immunosuppressive therapy (for example, following organ transplant), subjects afflicted with human immunodeficiency syndrome (HIV) or acquired immune deficiency syndrome (AIDS), subjects with forms of anemia that deplete or destroy white blood cells, subjects receiving radiation or chemotherapy, or subjects afflicted with an inflammatory disorder. Additionally, subjects of very young (e.g., 5 years of age or younger) or old age (e.g., 65 years of age or older) are at increased risk. Moreover, a subject may be at risk of contracting a viral infection due to proximity to an outbreak of the disease, e.g., subject resides in a densely-populated city or in close proximity to subjects having confirmed or suspected infections of a virus, or choice of employment, e.g. hospital worker, pharmaceutical researcher, traveler to infected area, or frequent flier. In some embodiments, a “subject” or “individual” is a patient under the care of a physician. [0075] The term “viral load,” “viral burden” or “viral titer” refers to a numerical expression of the quantity of virus in a given volume of body fluid, usually blood plasma. It is often expressed as viral particles, or infectious particles per mL depending on the type of assay. A higher viral burden, titer, or viral load often correlates with the severity of an active viral infection. [0076] Where a range of values is provided, it is understood that each intervening value, to the tenth of the unit of the lower limit unless the context clearly dictates otherwise, between the upper and lower limit of that range and any other stated or intervening value in that stated range, is encompassed within the disclosure. The upper and lower limits of these smaller ranges may independently be included in the smaller ranges, and are also encompassed within the disclosure, subject to any specifically excluded limit in the stated range. Where the stated range includes one or both of the limits, ranges excluding either or both of those included limits are also included in the disclosure. [0077] Certain ranges are presented herein with numerical values being preceded by the term “about.” The term “about” is used herein to provide literal support for the exact number that it precedes, as well as a number that is near to or approximately the number that the term precedes. In determining whether a number is near to or approximately a specifically recited number, the near or approximating unrecited number may be a number which, in the context in which it is presented, provides the substantial equivalent of the specifically recited number. If the degree of approximation is not otherwise clear from the context, “about” means either within plus or minus 10% of the provided value, or rounded to the nearest significant figure, in all cases inclusive of the provided value. In some embodiments, the term “about” indicates the designated value ± up to 10%, up to ± 5%, or up to ± 1%. [0078] It is appreciated that certain features of the disclosure, which are, for clarity, described in the context of separate embodiments, may also be provided in combination in a single embodiment. Conversely, various features of the disclosure, which are, for brevity, described in the context of a single embodiment, may also be provided separately or in any suitable sub-combination. All combinations of the embodiments pertaining to the disclosure are specifically embraced by the present disclosure and are disclosed herein just as if each and every combination was individually and explicitly disclosed. In addition, all sub-combinations of the various embodiments and elements thereof are also specifically embraced by the present disclosure and are disclosed herein just as if each and every such sub- combination was individually and explicitly disclosed herein. CORONAVIRUSES [0079] Coronaviruses are a family of large, enveloped, positive-sense single-stranded RNA viruses. They infect humans, other mammals and avian species, including livestock and companion animals (such as dogs, cats, chicken, cattle, pigs, and birds), and are therefore not only a challenge for public health but also a veterinary and economic concern. Coronaviruses include the genera of alphacoronaviruses, betacoronaviruses, gammacoronaviruses, and deltacoronaviruses. Whereas alphacoronaviruses and betacoronaviruses exclusively infect mammalian species, gammacoronaviruses and deltacoronaviruses have a wider host range that includes avian species. Coronaviruses cause respiratory, gastrointestinal, and neurological disease. The most common coronaviruses in clinical practice are 229E, OC43, NL63, and HKU1, which typically cause common cold symptoms in immunocompetent individuals. Other coronaviruses include severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV-2, which have emerged in the human population over the past 20 years and are highly pathogenic. [0080] The initial steps of coronavirus infection involve the specific binding of the coronavirus spike (S) protein to the cellular entry receptors, which have been identified for several coronaviruses and include human aminopeptidase N (APN; HCoV-229E), angiotensin- converting enzyme 2 (ACE2; HCoV-NL63, SARS-CoV and SARS-CoV-2) and dipeptidyl peptidase 4 (DPP4; MERS-CoV). [0081] The sites of receptor binding domains (RBD) within the S1 region (often referred to as S1 subunit) of a coronavirus S protein vary depending on the virus, with some having the RBD at the C-terminus of S1. The S-protein/receptor interaction is the primary determinant for a coronavirus to infect a host species and also governs the tissue tropism of the virus. Additional information regarding coronavirus biology, pathophysiology, diagnosis, and treatment can be found in recent reviews by V’kovski P. et al. (Nature Rev. Microbiol. Oct.28, 2020) and Wiersinga WJ et al. (JAMA.2020;324(8):782-793). [0082] Coronavirus spike (S) proteins are class I fusion glycoproteins which assemble into trimers that constitute the spikes or peplomers on the surface of the enveloped coronavirus particle. The proteins are divided into two parts (region or subunit) with distinct functions, host receptor binding and membrane fusion, which are attributed to the N-terminal (S1) and C- terminal (S2) halves of the S proteins. The surface-exposed S1 includes the NTD and RBD that specifically engages the host cell receptor, thereby determining virus cell tropism and pathogenicity. The transmembrane S2 domain contains heptad repeat regions, e.g., heptad repeat 1 (HR1) and heptad repeat 2 (HR2), central helix (CH), connector domain (CD), transmembrane domain (TM), and cytoplasmic tail (CT), the fusion peptide (FP), which mediate the fusion of viral and cellular membranes upon extensive conformational rearrangements. The function of S2 subunit is to fuse the membranes of viruses and host cells. The cleavage site at the border between the S1 and S2 subunits is called S1/S2 protease cleavage site. For all the coronaviruses, host proteases cleave the spike glycoprotein at the S2’ cleavage site to activate the proteins which allows subsequent fusion of the membranes of viruses and host cells through irreversible conformational changes. CoV-S binds to its cognate receptor, angiotensin-converting enzyme 2 (ACE2), via a receptor binding domain (RBD) present in the S1 subunit. [0083] The amino acid sequence of full-length SARS-CoV-2 spike protein is exemplified by the amino acid sequence provided in SEQ ID NO: 3045and FIG.15A. The term “CoV-S” as used herein includes protein variants of CoV spike protein isolated from different CoV isolates as well as recombinant CoV spike protein or a fragment thereof. CoV spike protein variants include CoV spike proteins with one or more substitutions, as exemplified by the amino acid sequence provided in SEQ ID NO: 3046and FIG.15B. C^{OMPOSITIONS OF THE DISCLOSURE} [0084] As described in greater detail below, one aspect of the present disclosure relates to compositions including (a) antigen-binding molecules, e.g., antibodies and antigen-binding fragments that bind to a SARS-CoV-2; and/or (b) nucleic acids encoding the antigen-binding molecules (e.g., antibodies and antigen-binding fragments) of (a), wherein the composition is formulated in a lipid-based nanoparticle (LNP). Compositions of the disclosure are useful for preventing, treating, diagnosing, or imaging a virus (e.g., coronavirus), a disease, a disorder, and/or a health condition associated with virus infection. Compositions of the disclosure are also useful for methods of aiding the detection and/or treatment of a disease, a disorder, and/or a health condition associated with virus infection, such as a coronavirus infection. As used herein, a “method of aiding” generally refers to methods of assisting in performing or practicing a method disclosed herein, for example, methods of assisting in (i) performing, (ii) practicing, and/or (iii) making a determination concerning the detection, classification, treatment regiment, or nature, of a virus infection (e.g., a coronavirus infection), a disease, a disorder, and/or a health condition. Antigen-binding molecules [0085] Generally, the antigen-binding molecules, e.g., antigen-binding polypeptides, antibodies, and antigen-binding fragments, that are formulated into LNP compositions of the disclosure, have a binding affinity for an epitope in the spike (S) protein of a coronavirus. [0086] An antibody is generally understood by the skilled artisan in the art to refer to immunoglobulin molecules including four polypeptide chains, two heavy chains (HCs) and two light chains (LCs) inter-connected by disulfide bonds (i.e., “full antibody molecules”), as well as multimers thereof (e.g., IgM). Exemplary antibodies include, for example, those listed in Tables 1A-1B and the Sequence Listing. Each heavy chain includes a heavy chain variable region (“HCVR” or “VH”) and a heavy chain constant region (which is comprised of domains CH1, CH2 and CH3). Each light chain is comprised of a light chain variable region (“LCVR or “VL”) and a light chain constant region (CL). The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDR), interspersed with regions that are more conserved, termed framework regions (FWR). Each VH and VL includes three CDRs and four FWRs, arranged from amino-terminus to carboxy-terminus in the following order: FWR1, CDR1, FWR2, CDR2, FWR3, CDR3, and FWR4. Heavy chain CDRs can also be referred to as HCDRs, and numbered as described above (e.g., HCDR1, HCDR2, and HCDR3). Likewise, light chain CDRs can be referred to as LCDRs, and numbered LCDR1, LCDR2, and LCDR3. In some embodiments of the disclosure, the FWRs of the antibodies or antigen-binding fragments thereof are identical to the human germline sequences, or are naturally or artificially modified. Thus, the present disclosure provides LNP compositions comprising anti-CoV-S antibodies or antigen-binding fragments thereof (e.g., anti-SARS-CoV-2- S antibodies or antigen-binding fragments thereof) including HCDR and LCDR sequences of Tables 1A-1B as well as those identified as such in the Sequence Listing within a variable heavy chain or light chain region of human germline immunoglobulin sequences. [0087] In some embodiments, the assignment of amino acids to each domain is in accordance with the definitions of Sequences of Proteins of Immunological Interest, Kabat, et al.; National Institutes of Health, Bethesda, Md.; 5th ed.; NIH Publ. No.91-3242 (1991). The amino acid sequence boundaries of an antibody CDR can also be determined by one of skill in the art using any of a number of numbering schemes, including those described by Kabat (1978) Adv. Prot. Chem.32:1-75; Kabat, et al., (1977) J. Biol. Chem.252:6609-6616 (“Kabat” numbering scheme, which derives CDR definitions and a residue numbering scheme based purely on antibody sequence information); Chothia, et al., (1987) J Mol. Biol.196:901-917, Chothia, et al., (1989) Nature 342:878-883, or Al-Lazikani et al., 1997, J. Mol. Biol., 273:927- 948 (“Chothia” numbering scheme, which defines defined CDRs from the earliest structures of antibodies); MacCallum et al., 1996, J. Mol. Biol.262:732-745 (“Contact” numbering scheme); Lefranc et al., Dev. Comp. Immunol., 2003, 27:55-77 (“IMGT” numbering scheme); and Honegge and Plückthun, J. Mol. Biol., 2001, 309:657-70 (“AHo” numbering scheme). In addition or alternatively, the amino acid sequence boundaries of an antibody CDR can also be determined by one of skill in the art using an “enhanced Chothia” scheme as described previously in, e.g., Abhinandan KR and Martin AC, Mol Immunol 2008 Aug;45(14):3832-9; or using a more recent methodology of distance-function clustering of antibody CDR loop conformations based on directional statistics and clustering algorithm using affinity propagation (see, e.g., North B. et al. J Mol Biol.2011 Feb 18; 406(2): 228–256. [0088] In some embodiments, CDR and FWR regions are determined using evolutionarily conserved motifs. See, e.g., PCT Application No. PCT/US2022/015986, which is hereby incorporated by reference in its entirety. T^ABLES 1A and 1B: Exemplary antigen-binding polypeptides, e.g., antibodies, and clonotypes of the disclosure. HCVR(1) and LCVR(1) correspond to the sequences of heavy chain variable region and light chain variable regions, respectively, without a leader peptide sequence. HCVR(2) and LCVR(2) correspond to the sequences of heavy chain variable region and light chain variable regions, respectively, including a leader peptide sequence. TABLE 1A

TABLE 1B

[0089] The term “antigen-binding fragment” of an antibody or antigen-binding polypeptide, as used herein, include any naturally occurring, enzymatically obtainable, synthetic, or genetically engineered polypeptide or glycoprotein that specifically binds an antigen to form a complex. Non-limiting examples of antigen-binding fragments include (i) Fab fragments; (ii) F(ab′)2 fragments; (iii) Fd fragments; (iv) Fv fragments; (v) single-chain Fv (scFv) molecules; (vi) dAb fragments; and (vii) minimal recognition units consisting of the amino acid residues that mimic the hypervariable region of an antibody (e.g., an isolated complementarity determining region (CDR) such as a CDR3 peptide), or a constrained FWR3-CDR3-FWR4 peptide. Other engineered molecules, such as domain-specific antibodies, single domain antibodies, chimeric antibodies, CDR-grafted antibodies, diabodies, triabodies, tetrabodies, minibodies, nanobodies (e.g., monovalent nanobodies, bivalent nanobodies, etc.), small modular immunopharmaceuticals (SMIPs), and shark variable IgNAR domains, are also encompassed within the expression “antigen-binding fragment,” as used herein. In some embodiments of the disclosure, the antigen- binding fragment includes three or more CDRs of an antibody of Tables 1A-1B or of an antibody described in the Sequence Listing (e.g., HCDR1, HCDR2 and HCDR3; or LCDR1, CDR2 and LCDR3). [0090] An antigen-binding fragment of an antibody, in some embodiment of the disclosure, include at least one variable domain. The variable domain can be of any size or amino acid composition and will generally include at least one CDR, which is adjacent to or in frame with one or more framework sequences. In antigen-binding fragments having a VH domain associated with a VL domain, the VH and VL domains can be situated relative to one another in any suitable arrangement. For example, the variable region can be dimeric and contain VH-VH, VH- VL or VL-VL dimers. Alternatively, the antigen-binding fragment of an antibody can contain a monomeric VH or VL domain. [0091] In some embodiments, an antigen-binding fragment of an antibody can contain at least one variable domain covalently linked to at least one constant domain. Non-limiting, exemplary configurations of variable and constant domains that can be found within an antigen- binding fragment of an antibody of the present disclosure include (i) V_H-C_H1; (ii) V_H-C_H2; (iii) VH-CH3; (iv) VH-CH1-CH2; (v) VH-CH1-CH2-CH3; (vi) VH-CH2-CH3; (vii) VH-CL; (viii) VL-CH1; (ix) VL-CH2; (x) VL-CH3; (xi) VL-CH1-CH2; (xii) VL-CH1-CH2-CH3; (xiii) VL-CH2-CH3; and (xiv) V_L-C_L. In any configuration of variable and constant domains, including any of the exemplary configurations listed above, the variable and constant domains can be either directly linked to one another or may be linked by a full or partial hinge or linker region. A hinge region may consist of at least 2 (e.g., 5, 10, 15, 20, 40, 60 or more) amino acids, which result in a flexible or semi-flexible linkage between adjacent variable and/or constant domains in a single polypeptide molecule. Moreover, an antigen-binding fragment of an antibody of the present disclosure may include a homo-dimer or hetero-dimer (or other multimer) of any of the variable and constant domain configurations listed above in non-covalent association with one another and/or with one or more monomeric VH or VL domain (e.g., by disulfide bond(s)). Antigen-binding proteins (e.g., antibodies and antigen-binding fragments) can be mono-specific or multi-specific (e.g., bi- specific). [0092] In some embodiments, the compositions of the disclosure include a nucleic acid encoding an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a SARS-CoV-2. In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof comprises all six complementary determining regions (CDRs) from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, and wherein optionally the composition is formulated in an LNP. [0093] In some embodiments, the compositions of the disclosure include a nucleic acid encoding an antigen-binding molecule, or an antigen-binding fragment thereof, that includes all six CDRs from TXG-0048. In some embodiments, the compositions of the disclosure include a nucleic acid encoding an antigen-binding molecule, or an antigen-binding fragment thereof, that includes all six CDRs from TXG-0070. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0087. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0114. In some embodiments, the antigen-binding molecule or an antigen- binding fragment thereof includes all six CDRs from TXG-0175. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0192. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0203. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0001. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0002. In some embodiments, the antigen-binding molecule or an antigen- binding fragment thereof includes all six CDRs from TXG-0004. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0005. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0006. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0008. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0009. In some embodiments, the antigen-binding molecule or an antigen- binding fragment thereof includes all six CDRs from TXG-0009. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0081 In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0115. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0154. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0174. In some embodiments, the antigen-binding molecule or an antigen- binding fragment thereof includes all six CDRs from TXG-0180. [0094] In some embodiments, the compositions of the disclosure include an antigen- binding molecule, or an antigen-binding fragment thereof, that binds to a SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof includes all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG- 0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, and wherein optionally the composition is formulated in an LNP. [0095] In some embodiments, the compositions of the disclosure include an antigen- binding molecule, or an antigen-binding fragment thereof, that includes all six CDRs from TXG- 0048. In some embodiments, the compositions of the disclosure include an antigen-binding molecule, or an antigen-binding fragment thereof, that includes all six CDRs from TXG-0070. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0087. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0114. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0175. In some embodiments, the antigen-binding molecule or an antigen- binding fragment thereof includes all six CDRs from TXG-0192. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0203. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0001. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0002. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0004. In some embodiments, the antigen-binding molecule or an antigen- binding fragment thereof includes all six CDRs from TXG-0005. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0006. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0008. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0009. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0009. In some embodiments, the antigen-binding molecule or an antigen- binding fragment thereof includes all six CDRs from TXG-0081 In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0115. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0154. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0174. In some embodiments, the antigen-binding molecule or an antigen-binding fragment thereof includes all six CDRs from TXG-0180. [0096] In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include the heavy chain CDRs (HCDR1, HCDR2, and HCDR3) from the antibodies belonging to the same clonotype family, for example, from any one of the following clonotype families: A, A1, B, B1, C, C1, D, E, F, G, H, I, J, K, L, and M. In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include the heavy chain CDRs (HCDR1, HCDR2, and HCDR3) from the antibodies belonging to the same clonotype family that is clonotype family A or C1 (see, e.g., Tables 1A and 1B). In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include the heavy chain CDRs (HCDR1, HCDR2, and HCDR3) from an antibody belonging to clonotype family A. In some embodiments, the antibody is TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG- 0008, or TXG-0009. [0097] In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include the heavy chain CDRs (HCDR1, HCDR2, and HCDR3) from an antibody belonging to clonotype family C1. In some embodiments, the antibody is TXG-0228 or TXG- 0230. [0098] In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include the light chain CDRs (LCDR1, LCDR2, and LCDR3) from the antibodies belonging to the same clonotype family, for example, from any one of the following clonotype families A, A1, B, B1, C, C1, D, E, F, G, H, I, J, K, L, and M. In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include the light chain CDRs (LCDR1, LCDR2, and LCDR3) from the antibodies belonging to the same clonotype family that is any one of clonotype families A or C1. In some embodiments, the antibodies and antigen- binding fragments thereof of the disclosure include the CDRs (LCDR1, LCDR2, and LCDR3) from an antibody belonging to clonotype family A. In some embodiments, the antibody is TXG- 0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, or TXG-0009. In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include the CDRs (LCDR1, LCDR2, and LCDR3) from an antibody belonging to clonotype family C1. In some embodiments, the antibody is TXG-0228 or TXG-0230. [0099] In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include (a) the heavy chain CDRs (HCDR1, HCDR2, and HCDR3), and (b) the light chain CDRs (LCDR1, LCDR2, and LCDR3) from the antibodies belonging to the same clonotype family, for example, from a clonotype family being any one of the clonotype families A, A1, B, B1, C, C1, D, E, F, G, H, I, J, K, L, or M. In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include (a) the heavy chain CDRs (HCDR1, HCDR2, and HCDR3), and (b) the light chain CDRs (LCDR1, LCDR2, and LCDR3) from the antibodies belonging to the same clonotype family selected from the group consisting of clonotype families A and C1. In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include (a) the heavy chain CDRs (HCDR1, HCDR2, and HCDR3), and (b) the light chain CDRs (LCDR1, LCDR2, and LCDR3) from an antibody belonging to clonotype family A. In some embodiments, the antibody is TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, or TXG-0009. In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure include (a) the heavy chain CDRs (HCDR1, HCDR2, and HCDR3), and (b) the light chain CDRs (LCDR1, LCDR2, and LCDR3) from an antibody belonging to clonotype family C1. In some embodiments, the antibody is TXG-0228 or TXG-0230. [0100] Non-limiting exemplary embodiments of the antibodies and antigen-binding fragments thereof of the disclosure can include one or more of the following features. In some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure can include a polypeptide including an amino acid sequence that is set forth herein except for one or more (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10) mutations such as, for example, missense mutations (e.g., conservative substitutions), non-sense mutations, deletions, or insertions. For example, the present disclosure includes antigen-binding polypeptides which include an immunoglobulin light chain variant comprising an LCVR amino acid sequence set forth in Tables 1A-1B and Sequence Listing but having one or more of such mutations and/or an immunoglobulin heavy chain variant comprising an HCVR amino acid sequence set forth in Tables 1A-1B and Sequence Listing but having one or more of such mutations. As described in greater detail below, in some embodiments, an antigen-binding molecule or antigen-binding fragment of the disclosure can include an immunoglobulin light chain variant comprising LCDR1, LCDR2 and LCDR3 wherein one or more (e.g., 1 or 2 or 3) of such CDRs has one or more of such mutations (e.g., conservative substitutions) and/or an immunoglobulin heavy chain variant comprising HCDR1, HCDR2 and HCDR3 wherein one or more (e.g., 1 or 2 or 3) of such CDRs has one or more of such mutations (e.g., conservative substitutions). Such substitutions can be in a CDR, framework, and/or constant region of an antibody or antigen-binding fragment. [0101] Accordingly, in some embodiments, the antibodies and antigen-binding fragments thereof of the disclosure can include one or more variant CDRs (e.g., any one or more of HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and/or LCDR3) that are set forth herein with at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, sequence identity to, e.g., the heavy chain and light chain CDRs of the Sequence Listing. [0102] In some embodiments, the HCDR1 amino acid sequence is at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to an HCDR1 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the HCDR1 amino acid sequence is at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to the HCDR1 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0103] In some embodiments, the HCDR1 includes an amino acid sequence identical to an HCDR1 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing, and further wherein one, two, or three amino acids in the amino acid sequence is substituted by a different amino acid. In some embodiments, the HCDR1 includes an amino acid sequence identical to the HCDR1 of an antibody any one of TXG-0001, TXG-0002, TXG-0004, TXG- 0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG- 0230; and further wherein one, two, or three amino acids in the amino acid sequence is substituted by a different amino acid. [0104] In some embodiments, the HCDR1 amino acid sequence is 100% identical to an amino acid sequence identical to an HCDR1 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the HCDR1 amino acid sequence is 100% identical to an amino acid sequence identical to the HCDR1 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0105] In some embodiments, the HCDR2 amino acid sequence is at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to an HCDR2 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the HCDR2 amino acid sequence is at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to the HCDR2 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0106] In some embodiments, the HCDR2 includes an amino acid sequence identical to an HCDR2 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing, and further wherein one, two, or three amino acids in the amino acid sequence is substituted by a different amino acid. In some embodiments, the HCDR2 includes an amino acid sequence identical to the HCDR2 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG- 0230; and further wherein one, two, or three amino acids in the amino acid sequence is substituted by a different amino acid. [0107] In some embodiments, the HCDR2 amino acid sequence is 100% identical to an amino acid sequence identical to an HCDR2 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the HCDR2 amino acid sequence is 100% identical to an amino acid sequence identical to the HCDR2 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0108] In some embodiments, the LCDR1 amino acid sequence is at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to an LCDR1 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the LCDR1 amino acid sequence is at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to the LCDR1 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0109] In some embodiments, the LCDR1 includes an amino acid sequence identical to an LCDR1 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing, and further wherein one, two, or three amino acids in the amino acid sequence is substituted by a different amino acid. In some embodiments, the LCDR1 includes an amino acid sequence identical to the LCDR1 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG- 0230; and further wherein one, two, or three amino acids in the amino acid sequence is substituted by a different amino acid. [0110] In some embodiments, the LCDR1 amino acid sequence is 100% identical to an amino acid sequence identical to an LCDR1 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the LCDR1 amino acid sequence is 100% identical to an amino acid sequence identical to the LCDR1 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0111] In some embodiments, the LCDR2 amino acid sequence is at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to an LCDR2 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the LCDR2 amino acid sequence is at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to the LCDR2 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0112] In some embodiments, the LCDR2 includes an amino acid sequence identical to an LCDR2 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing, and further wherein one, two, or three amino acids in the amino acid sequence is substituted by a different amino acid. In some embodiments, the LCDR2 includes an amino acid sequence identical to the LCDR2 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG- 0230; and further wherein one, two, or three amino acids in the amino acid sequence is substituted by a different amino acid. [0113] In some embodiments, the LCDR2 amino acid sequence is 100% identical to an amino acid sequence identical to an LCDR2 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the LCDR2amino acid sequence is 100% identical to an amino acid sequence identical to the LCDR2 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0114] In some embodiments, an antibody or antigen-binding fragment of the disclosure includes: (a) a HCDR1 comprising an amino acid sequence having 100% sequence identity to an HCDR1 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing; (b) a HCDR2 comprising an amino acid sequence having 100% sequence identity to an HCDR2 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing; c) a HCDR3 comprising an amino acid sequence having 100% sequence identity to an HCDR3 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing; (d) a LCDR1 comprising an amino acid sequence having 100% sequence identity to an LCDR1 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing; (e) a LCDR2 comprising an amino acid sequence having 100% sequence identity to an LCDR2 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing; and (f) a LCDR3 comprising an amino acid sequence having 100% sequence identity to an LCDR3 amino acid sequence identified as such in Tables 1A-1B and Sequence Listing. [0115] In some embodiments, the antibody or antigen-binding fragment of the disclosure includes three heavy chain CDRs (HCDR1, HCDR2 and HCDR3), and three light chain CDRs (LCDR1, LCDR2 and LCDR3), wherein the heavy chain CDRs and light chain CDRs are independently selected from the HCDRs and LCDRs of the antibodies belonging to a clonotype family. One skilled in the art will appreciate that when an antibody is said to include a plurality of HCDRs and/or LCDRs that “are independently selected from a group of antibodies,” this can mean that each of the HCDRs and/or LCDRs of the antibody or antigen-binding fragment can be independently selected from the HCDRs and LCDRs of the antibodies belonging to said group of antibodies. As such, in some embodiments, an antibody or antigen-binding fragment as disclosed herein can include three HCDRs and three LCDRs each of which can be independently selected from the HCDRs and LCDRs of different antibodies belonging to the same group of antibodies. As such, in some embodiments, an antibody or antigen-binding fragment as disclosed herein can include the three HCDRs and three LCDRs of any one of the antibodies of the group. [0116] Some embodiments of the disclosure provide an antibody or antigen-binding fragment including three HCDRs and three LCDRs each of which are independently selected from the HCDRs and LCDRs of the antibodies belonging to a clonotype family. In some embodiments, an antibody or antigen-binding fragment as disclosed herein can include three HCDRs and three LCDRs each of which can be independently selected from the HCDRs and LCDRs of different antibodies belonging to the same clonotype family. In some embodiments, an antibody or antigen-binding fragment as disclosed herein can include the three HCDRs and the three LCDRs of a selected antibody of a clonotype family. As described in greater detail in Examples 6-7 below, antibodies and antigen-binding fragments exhibiting a binding affinity to a target antigen above a cut-off threshold were selected for further analysis using 10x Genomics “Enclone” (available at https://bit.ly/enclone), which is a computational tool developed for clonal grouping to study the adaptive immune system. In this computational tool, the 10x Genomics Chromium Single Cell V(D)J data containing B cell receptor (BCR) and T cell receptor (TCR) RNA sequences are entered as input data to Enclone. Based on the input, Enclone finds and organizes cells arising from the same progenitors into groups (e.g., clonotype families) and compactly displays each clonotype along with its salient features, including mutated amino acids. In some embodiments, the antibodies belong to clonotype family A or clonotype family C1. In some embodiments, the antibody or antigen-binding fragment of the disclosure includes three heavy chain CDRs (HCDR1, HCDR2 and HCDR3), and three light chain CDRs (LCDR1, LCDR2 and LCDR3), wherein the heavy chain CDRs and light chain CDRs are independently selected from the HCDRs and LCDRs of the following clonotype family of antibodies: (a) clonotype family A: or (b) clonotype family C1. [0117] In some embodiments, the antibody or antigen-binding fragment of the disclosure includes three heavy chain CDRs (HCDR1, HCDR2 and HCDR3), and three light chain CDRs (LCDR1, LCDR2 and LCDR3), wherein the heavy chain CDRs and light chain CDRs are independently selected from the HCDRs and LCDRs of the antibodies belonging to a clonotype family A as identified in Tables 1A and 1B. [0118] In some embodiments, the antibody or antigen-binding fragment of the disclosure includes three heavy chain CDRs (HCDR1, HCDR2 and HCDR3), and three light chain CDRs (LCDR1, LCDR2 and LCDR3), wherein the heavy chain CDRs and light chain CDRs are independently selected from the HCDRs and LCDRs of the antibodies belonging to a clonotype family C1 as identified in Tables 1A and 1B. [0119] Variations in amino acid sequences of the CoV-S antibodies and antigen-binding fragments described herein may be naturally occurring, such as splicing variants or allelic variants. In addition or alternatively, variations in amino acid sequences of the CoV-S antibodies and antigen-binding fragments may be introduced by substitution, deletion or insertion of one or more codons into the nucleic acid sequences encoding the antibodies that results in a change in the amino acid sequences of the antibodies. Optionally, the variation may be resulted from substitution of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids with any other amino acid in the antibodies. Amino acid substitutions in variants of CoV-S antibodies and antigen-binding fragments may be conservative or non-conservative. Those of skill in the art will understand that a “non-conservative substitution,” when used in reference to a polypeptide, refers to a substitution of an amino acid in a polypeptide with an amino acid with significantly differing side chain properties. Non-conservative substitutions may use amino acids between, rather than within, the defined groups and affects (a) the structure of the peptide backbone in the area of the substitution (e.g., serine for glycine), (b) the charge or hydrophobicity, or (c) the bulk of the side chain. A non-limiting exemplary non-conservative substitution can be an acidic amino acid substituted with a basic or aliphatic amino acid; an aromatic amino acid substituted with a small amino acid; and a hydrophilic amino acid substituted with a hydrophobic amino acid. [0120] Conservatively modified variant anti-CoV-S antibodies and antigen-binding fragments thereof are also contemplated as part of the present disclosure. A “conservatively modified variant” or a “conservative substitution” refers to a variant wherein there is one or more substitutions of amino acids in a polypeptide with other amino acids having similar characteristics (e.g. charge, side-chain size, hydrophobicity/hydrophilicity, backbone conformation and rigidity, etc.). Such changes can frequently be made without significantly disrupting the biological activity of the antibody or fragment. Those of skill in this art recognize that, in general, single amino acid substitutions in non-essential regions of a polypeptide do not substantially alter biological activity. In addition, substitutions of structurally or functionally similar amino acids are less likely to significantly disrupt biological activity. [0121] Examples of groups of amino acids that have side chains with similar chemical properties include 1) aliphatic side chains: glycine, alanine, valine, leucine and isoleucine; 2) aliphatic-hydroxyl side chains: serine and threonine; 3) amide-containing side chains: asparagine and glutamine; 4) aromatic side chains: phenylalanine, tyrosine, and tryptophan; 5) basic side chains: lysine, arginine, and histidine; 6) acidic side chains: aspartate and glutamate, and 7) sulfur-containing side chains: cysteine and methionine. Exemplary conservative amino acids substitution groups include valine-leucine-isoleucine, phenylalanine-tyrosine, lysine-arginine, alanine-valine, glutamate-aspartate, and asparagine-glutamine. Alternatively, a conservative replacement is any change having a positive value in the PAM250 log-likelihood matrix as disclosed in Gonnet et al. (1992) Science 256: 144345. [0122] In some embodiments, the antibody or antigen-binding fragment of the disclosure includes a framework region having at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, sequence identity to the amino acid sequence of a framework region (FWR) identified as such in Tables 2A-2B and Sequence Listing. [0123] In some embodiments, the antibody or antigen-binding fragment of the disclosure includes: (a) a heavy chain framework region 1 (HFWR1) comprising an amino acid sequence selected from the HFWR1 sequences identified as such in Tables 2A-2B and Sequence Listing; (b) a heavy chain framework region 2 (HFWR2) comprising an amino acid sequence selected from the HFWR2 sequences identified as such in Tables 2A-2B and Sequence Listing; (c) a heavy chain framework region 3 (HFWR3) comprising an amino acid sequence selected from the HFWR3 sequences identified as such in Tables 2A-2B and Sequence Listing; and (d) a heavy chain framework region 4 (HFWR4) comprising an amino acid sequence selected from the HFWR4 sequences identified as such in Tables 2A-2B and Sequence Listing. [0124] In some embodiments, the antibody or antigen-binding fragment of the disclosure includes: (a) a light chain framework region 1 (LFWR1) comprising an amino acid sequence selected from the LFWR1 sequences of the Sequence Listing; (b) a light chain framework region 2 (LFWR2) comprising an amino acid sequence selected from the LFWR2 sequences of the Sequence Listing; (c) a light chain framework region 3 (LFWR3) comprising an amino acid sequence selected from the LFWR3 sequences of the Sequence Listing; and (d) a light chain framework region 4 (LFWR4) comprising an amino acid sequence selected from the LFWR4 sequences of the Sequence Listing. [0125] In some embodiments, the antibody or antigen-binding fragment of the disclosure includes the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2, and LCDR3 of an antibody of Tables 1A 1B. In some embodiments, the antibody or antigen-binding fragment of the disclosure further includes the heavy chain framework regions HFWR1, HFWR2, HFWR3, and HFWR4 of the same antibody or antigen-binding fragment of Tables 1A 1B and as set forth in the Sequence Listing. In some embodiments, the antibody or antigen-binding fragment of the disclosure further includes the light chain framework regions LFWR1, LFWR2, LFWR3, and LFWR4 of the same antibody or antigen-binding fragment as set forth in Table 2 and the Sequence Listing. TABLE 2A: Exemplary antibodies of the disclosure and corresponding framework regions.

TABLE 2B: Exemplary antibodies of the disclosure and corresponding framework regions.

[0126] In some embodiments, the antibody or antigen-binding fragment includes a heavy chain variable region (HCVR) comprising an amino acid sequence having at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, sequence identity to an HCVR identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the antibody or antigen-binding fragment includes a HCVR comprising an amino acid sequence having at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, sequence identity to the HCVR of an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0127] In some embodiments, the antibody or antigen-binding fragment includes a light chain variable region (LCVR) comprising an amino acid sequence having at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, sequence identity to an LCVR identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the antibody or antigen-binding fragment includes a LCVR comprising an amino acid sequence having at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, sequence identity to the HCVR of an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0128] In some embodiments, the antibody or antigen-binding fragment of the disclosure includes: (a) a HCVR comprising an amino acid sequence having at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, sequence identity to an HCVR identified as such in Tables 1A-1B and Sequence Listing; and b) a LCVR comprising an amino acid sequence having at least 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, sequence identity to an LCVR identified as such in Tables 1A-1B and Sequence Listing. In some embodiments, the antibody or antigen-binding fragment includes: a HCVR and a LCVR which respectively are 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to the HCVR and LCVR of an antibody of Table 1A or Table 1B. In some embodiments, the antibody or antigen-binding fragment includes: a HCVR and a LCVR which respectively are 90%, e.g., at least 91%, at least 92%, at least 93%, at least 93%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to the HCVR and LCVR of an antibody selected from the group consisting of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0129] In some embodiments, the antibody or antigen-binding fragment includes the HCVR and LCVR of an antibody of Table 1A or Table 1B. In some embodiments, the antibody or antigen-binding fragment includes the HCVR and LCVR of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. In some embodiments, the antibody or antigen-binding fragment of the disclosure is selected from Table 1A or Table 1B. In some embodiments, the antibody or antigen-binding fragment is being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG- 0230. [0130] In some embodiments, the antibody or antigen-binding fragment of the disclosure further includes a constant region (e.g., an Fc region). In some embodiments, the constant region is an IgA, IgD, IgE, IgG, or IgM heavy chain constant region. In some embodiments, the heavy chain constant region is of the same isotype and subclass as the antibody identified in Tables 1A- 1B. In some embodiments, the antibody or antigen-binding fragment of the disclosure includes a constant region of the type IgA (e.g., IgA1 or IgA2), IgD, IgE, IgG (e.g., IgG1, IgG2, IgG3 and IgG4) or IgM. In some embodiments, the constant region is an IgG constant region. [0131] In some embodiments, the antibody or antigen-binding fragment of the disclosure further includes a kappa type light chain constant region. In some embodiments, the antibody or antigen-binding fragment of the disclosure further includes a lambda type light chain constant region. [0132] In some embodiments, the antibody or antigen-binding fragment of the disclosure comprises a hinge domain. In some embodiments, the hinge domain comprises a stabilizing mutation. [0133] In some embodiments, the antibody or antigen-binding fragment of the disclosure comprises a variant Fc region. The variant Fc region may comprise one or more amino acid modifications that reduce the affinity of the variant Fc Region for an FcγR receptor. Exemplary amino acid modifications that reduce the affinity of the variant Fc Region for an FcγR receptor include L234A; L235A; or L234A and L235A, according to Kabat (EU index) numbering system. The variant Fc region may comprise one or more amino acid modifications that enhance the serum half-life of the variant Fc region. Exemplary amino acid modifications that enhance the serum half-life of the variant Fc region include M252Y; M252Y and S254T; M252Y and T256E; M252Y, S254T and T256E; or K288D and H435K, according to Kabat (EU index) numbering system. [0134] In some embodiments, the antibody or antigen-binding fragment of the disclosure is a human antibody or antigen-binding fragment. One of ordinary skill in the art will understand that the term “human” antibody includes antibodies having variable and constant regions derived from human germline immunoglobulin sequences whether in a human cell or grafted into a non- human cell, e.g., a mouse cell. The human antibodies of the disclosure can include amino acid residues not encoded by human germline immunoglobulin sequences (e.g., mutations introduced by random or site-specific mutagenesis in vitro or by somatic mutation in vivo), for example in the CDRs, such as CDR3. However, the term “human antibody,” as used herein, is not intended to include antibodies in which CDR sequences derived from the germline of another mammalian species (e.g., mouse) have been grafted onto human FWR sequences. The term includes antibodies recombinantly produced in a non-human mammal or in cells of a non-human mammal. [0135] In some embodiments, the antibody or antigen-binding fragment is a humanized antibody, a chimeric antibody, or a hybrid antibody, or an antigen-binding fragment of any thereof. The term “humanized antibody” as used herein encompasses antibodies comprising heavy and light chain variable region sequences from a non-human species (e.g., a mouse) but in which at least a portion of the VH and/or VL sequence has been altered to be more “human- like,” i.e., more similar to human germline variable sequences. One type of humanized antibody is a CDR-grafted antibody in which human CDR sequences are introduced into non-human VH and VL sequences to replace the corresponding non-human CDR sequences. Another type of humanized antibody is a FWR-grafted antibody in which human FWR sequences are introduced into non-human VH and VL sequences to replace corresponding non-human FWR sequences. In some embodiments, the antibodies or antigen-binding fragments of the disclosure include a murine antibody, phage display antibody, or nanobody / VHH containing the frameworks and/or CDRs described in this disclosure (e.g., in Tables 1A-1B, A-2B, and Sequence Listing). As used herein, the term “chimeric antibody” encompasses antibodies having the variable domain from a first antibody and the constant domain from a second antibody, wherein the first and second antibodies are from different species. As used herein, the term “hybrid antibody” encompasses antibodies having the variable domain from a first antibody and the constant domain from a second antibody, wherein the first and second antibodies are from different animals, or wherein the variable domain, but not the constant region, is from a first animal. For example, a variable domain can be taken from an antibody isolated from a human and expressed with a fixed constant region not isolated from that antibody. Hybrid antibodies are synthetic and non- naturally occurring because the variable and constant regions they contain are not isolated from a single natural source. In some embodiments, the hybrid antibodies of the disclosure includes a light chain from a first antibody and a heavy chain from a second antibody, wherein the first and second antibodies are from different species. In some embodiments, the chimeric antibodies of the disclosure includes a non-human light chain which is combined with a heavy chain or set of heavy chain CDRs disclosed in this application. [0136] In some embodiments, the antibody is a monoclonal antibody. In some embodiments, the antibody or antigen-binding fragment is an engineered antibody or engineered antibody fragment. Non-limiting examples of engineered antibody fragment include a single- chain variable fragment (scFv), a nanobody, a diabody, a triabody, a minibody, an F(ab’)2 fragment, an F(ab) fragment, a VH domain, a VL domain, a single chain variable fragment (scFv), a single domain antibody (sdAb), a VNAR domain, and a VHH domain. In some embodiments, the antibody or antigen-binding fragment of the disclosure is a single-chain antibody fragment (scFv), a F(ab) fragment, a F(ab') fragment, a Fab'-SH, a F(ab')2 fragment, or a Fv fragment. [0137] In some embodiments, the antibody or antigen-binding fragment has a binding affinity (e.g., ability to bind, with varying degrees of specificity) to an epitope in a subunit of the SARS-CoV-2 S protein. One skilled in the art will understand that the term “epitope” refers to an antigenic determinant (e.g., a CoV-S polypeptide) that interacts with a specific antigen-binding site of an antigen-binding polypeptide, e.g., a variable region of an antibody molecule, known as a paratope. A single antigen can have more than one epitope. Thus, different antibodies may bind to different areas on an antigen and may have different biological effects. The term “epitope” also refers to a site on an antigen to which B and/or T cells respond. It also refers to a region of an antigen that is bound by an antibody. Epitopes can be defined as structural or functional. Functional epitopes are generally a subset of the structural epitopes and have those residues that directly contribute to the affinity of the interaction. Epitopes can be linear or conformational, that is, composed of non-linear amino acids. In some embodiments, epitopes can include determinants that are chemically active surface groupings of molecules such as amino acids, sugar side chains, phosphoryl groups, or sulfonyl groups, and, in some embodiments, can have specific three-dimensional structural characteristics, and/or specific charge characteristics. [0138] Methods for determining the epitope of an antigen-binding polypeptide, e.g., antibody or antigen-binding fragment or polypeptide, include alanine scanning mutational analysis, peptide blot analysis, peptide cleavage analysis, crystallographic studies and NMR analysis. In addition, methods such as epitope excision, epitope extraction and chemical modification of antigens can be employed. Another method that can be used to identify the amino acids within a polypeptide with which an antigen-binding polypeptide (e.g., antibody or fragment or polypeptide) interacts is hydrogen/deuterium exchange detected by mass spectrometry. [0139] As described in greater detail below, the vast majority of known antibodies against SARS-CoV-2 recognize one of three major epitope regions of the spike protein: the RBD of the S1 subunit, the NTD of the S1 subunit, and the S2 subunit. In particular, neutralizing antibodies (nAbs) against each of these epitope regions have been identified and reported, with the broadest nAbs targeting epitopes in the S2 subunit or the RBD of the S1 subunit. In contrast, antibodies specific for the NTD of the S1 subunit primarily target a single supersite, have a limited genetic vocabulary and, because the NTD is not particularly well conserved across CoVs, are generally understood to be of limited breadth (Suryadevara et al., J. Clin. Invest. Jun 1;132(11), 2022). Recently, NTD-specific antibodies targeting a moderately conserved epitope outside the NTD supersite neutralized several SARS-CoV-2 variants of concern (VoCs) have been reported, but their breadth did not extend beyond SARS-CoV-2 to other human CoVs (Wang et al., BioRxiv. Preprint.2022 Feb 1; doi: 10.1101/2022.02.01.478695). [0140] In some embodiments of the present disclosure, the antibody or antigen-binding fragment has a binding affinity to an epitope the S1 subunit of the SARS-CoV-2 S protein. In some embodiments, the antibody or antigen-binding fragment has a binding affinity to a RBD of the S1 subunit. In some embodiments, the subunit of the S protein of SARS-CoV-2 is the S2 subunit. In some embodiments, the antibody or antigen-binding fragment has a binding affinity to a NTD of the S1 subunit. [0141] In some embodiments, the SARS-CoV-2 S protein may include one or more amino acid substitutions. In some embodiments, the SARS-CoV-2 S protein includes one or more of the following Proline substitutions: F817P, A892P, A899P, A942P, K986P, and V987P. In some embodiments, the SARS-CoV-2 S protein includes one or more of the following Alanine substitutions: R683A and R685A. In some embodiments, the one or more amino acid substitutions includes D614G substitution. In some embodiments, the SARS-CoV-2 S protein has the amino acid sequence provided in FIG.15A. In some embodiments, the S protein of SARS-CoV-2 has the amino acid sequence provided in FIG.15B. [0142] In some embodiments, the SARS-CoV-2 S protein includes one or more amino acid substitutions at a position being any one of K417, L452, E484, N501, D614, or a combination thereof. In some embodiments, the SARS-CoV-2 S protein includes an amino acid substitution at position K417. In some embodiments, the K417 amino acid substitution is a conservative amino acid substitution. In some embodiments, the amino acid substitution at position K417 is K417T or K417N. In some embodiments, the K417 amino acid substitution is a non-conservative amino acid substitution. In some embodiments, the L452 amino acid substitution is a conservative amino acid substitution. In some embodiments, the amino acid substitution at position L452 is L452R. In some embodiments, the L452 amino acid substitution is a non-conservative amino acid substitution. In some embodiments, the SARS-CoV-2 S protein includes an amino acid substitution at position E484. In some embodiments, the E484 amino acid substitution is a conservative amino acid substitution. In some embodiments, the E484 amino acid substitution is a non-conservative amino acid substitution. In some embodiments, the amino acid substitution at position E484 is E484K or E484Q. In some embodiments, the SARS-CoV-2 S protein includes an amino acid substitution at position N501. In some embodiments, the N501 amino acid substitution is a conservative amino acid substitution. In some embodiments, the N501 amino acid substitution is a non-conservative amino acid substitution. In some embodiments, the amino acid substitution at position N501 is N501Y. In some embodiments, the SARS-CoV-2 S protein includes an amino acid substitution at position D614. In some embodiments, the D614 amino acid substitution is a conservative amino acid substitution. In some embodiments, the D614 amino acid substitution is a non-conservative amino acid substitution. In some embodiments, the amino acid substitution at position D614 is D614G. [0143] In some embodiments, the SARS-CoV-2 S protein includes one or more amino acid substitutions that is any one of K417T, K417N, L452R, E484K, E484Q, N501Y, D614G, or a combination thereof. In some embodiments, the SARS-CoV-2 S protein includes a combination of the following amino acid substitutions: K417N, E484K, and N501Y. In some embodiments, the SARS-CoV-2 S protein includes a combination of the following amino acid substitutions: K417T, E484K, and N501Y. In some embodiments, the SARS-CoV-2 S protein includes a combination of the following amino acid substitutions: L452R and E484Q. In some embodiments, the antibody or antigen-binding fragment has binding affinity for a trimeric form of the CoV-S protein. In some embodiments, the antibody or antigen-binding fragment has binding affinity for a pre-fusion trimeric form of the CoV-S protein. In some embodiments, the antibody or antigen-binding fragment has binding affinity for a stabilized prefusion spike protein (e.g., an S2P-stabilized pre-fusion spike protein) in monomeric or multimeric (e.g., trimeric) form. In some embodiments, the antibody or antigen-binding fragment has binding affinity for a non-prefusion spike protein in monomeric or multimeric (e.g., trimeric) form. In some embodiments, the antibody or antigen-binding fragment has binding affinity for a non-S2P- stabilized pre-fusion spike protein in monomeric or multimeric (e.g., trimeric) form. Pre-fusion and non-prefusion conformations of the spike protein are described in, e.g., Cai Y. et al. Science Vol.369, Issue 6511, pp.1586-1592, 2020; Xu C. et al. Science Advances, Vol.7, no.1, Jan 2021; Wrobel AG et al. Nat Comms 11, 5337, 2020; and Zhang J. et al. Science March 16, 2021; all of which are hereby incorporated by reference in their entirety. [0144] Generally, binding affinity of an antigen-binding molecule (e.g., antibody) or antigen-binding fragment to its target antigen can be used as a measure of the strength of a non- covalent interaction between two molecules, e.g., an antibody or antigen-binding fragment thereof and an antigen (e.g., coronavirus S protein antigen). In some cases, binding affinity can be used to describe monovalent interactions (intrinsic activity). Binding affinity between two molecules can be quantified by determination of the equilibrium dissociation constant (K_D). In turn, K_D can be determined by measurement of the kinetics of complex formation and dissociation using, e.g., the surface plasmon resonance (SPR) method (Biacore). The rate constants corresponding to the association and the dissociation of a monovalent complex are referred to as the association rate constants k_a (or k_on) and dissociation rate constant k_d (or k_off), respectively. KD is related to ka and kd through the equation KD = kd / ka. The value of the dissociation constant can be determined directly by various methods, and can be computed even for complex mixtures by methods such as those set forth in Caceci et al. (1984, Byte 9: 340-362). For example, the K_D can be established using a double-filter nitrocellulose filter binding assay such as that disclosed by Wong & Lohman (1993, Proc. Natl. Acad. Sci. USA 90: 5428- 5432). As shown in Examples 9 and 12 below, binding affinity of the antibodies and fragments described herein can also be assayed using a Carterra LSA SPR biosensor equipped with a HC30M chip. [0145] Other assays to evaluate the binding ability (e.g., binding affinity and/or specificity) of the antigen-binding molecules (e.g., antibodies) and antigen-binding fragments of the present disclosure towards target antigens include, for example, ELISAs, Western blots, RIAs, and flow cytometry analysis. The binding kinetics and binding affinity of the antibody also can be assessed by standard assays known in the art, such as Surface Plasmon Resonance (SPR), e.g. by using a Biacore™ system, or KinExA. In some embodiments, the binding affinity of an antibody or an antigen-binding fragment for a target antigen (e.g., coronavirus S protein antigen) can be calculated by the Scatchard method described by Frankel et al., Mol. Immunol, 16: 101- 106, 1979. It will be understood that the binding affinity of an antibody or antigen-binding fragment for a target antigen is the strength of interaction between the antibody or antigen- binding fragment with the target antigen, whereas the binding specificity of an antibody or antigen-binding fragment for a target antigen relates to the affinity to the target antigen relative to other antigens. It will also be understood that an antibody or antigen-binding fragment that “specifically binds” a target antigen (such as S protein) is an antigen-binding fragment that binds the target antigen but does not significantly bind other antigens. In some embodiments, the antibody or antigen-binding fragment “specifically binds” a target antigen if it does not significantly bind other antigens but binds the target antigen with high affinity, e.g., with an equilibrium dissociation constant (KD) of 100 nM or less, such as 60 nM or less, for example, 30 nM or less, such as, 15 nM or less, or 10 nM or less, or 5 nM or less, or 1 nM or less, or 500 pM or less, or 400 pM or less, or 300 pM or less, or 200 pM or less, or 100 pM or less. In some embodiments, the antibody or antigen-binding fragment binds a target antigen with high affinity, e.g., with a KD of less than 1 µM. In some embodiments, the antibodies or antigen-binding fragments of the disclosure that specifically bind a target antigen, such as a CoV-S protein (e.g., SARS-CoV-2 S protein), have a binding affinity to the target antigen expressed as KD, of at least about 10⁻⁸ M, as measured by real-time, label free bio-layer interferometry assay, for example, at 25° C. or 37°C, e.g., an Octet® HTX biosensor, or by surface plasmon resonance, e.g., BIACORE™, or by solution-affinity ELISA. In some embodiments, the antibody or antigen- binding fragment has a measurable binding affinity and/or binding specificity, e.g., with an equilibrium dissociation constant (KD) value of less than 1 mM, less than 100 µM, less than 10 µM , less than 1 µM, less than 900 nM, less than 800 nM, less than 700 nM, less than 600 nM, less than 500 nM, for example, less than 400 nM, less than 300 nM, less than 200 nM, less than 150 nM, less than 120 nM, less than 100 nM, less than 90 nM, less than 80 nM, less than 70 nM, less than 60 nM, less than 50 nM, less than 40 nM, less than 20 nM, less than 15 nM, less than 10 nM, less than 5 nM, less than 5 nM, or less than 1 nM. [0146] In some embodiments, the binding affinity and/or binding specificity of an antigen- binding molecule (e.g., antibody or antigen-binding fragment) to a CoV-S target antigen is determined based on a quantity/number of target and optionally non-target antigen sequence reads and/or unique molecular identifiers (UMIs) associated with the antigen binding molecule via a process termed “barcode-enabled antigen mapping by sequencing” (BEAM-seq) (see, e.g., Examples 6 and 7 and FIGS.2, 3, and 4 below. Antigen sequence reads and/or UMIs can be associated bioinformatically with antigen binding molecule sequences via shared partition barcode sequences. For example, binding affinity and/or binding specificity of an antigen binding molecule to the CoV-S antigen can be determined based on independent observations of quantity/number of UMIs associated with the CoV-S antigen and optionally non-target antigen from one or more partitions, wherein each of the one or more partitions comprise a cell expressing the same antigen-binding molecule. For other example, binding affinity and/or binding specificity of an antigen binding molecule to the CoV-S antigen can be determined based on independent observations of quantity/number of UMIs associated with the antigen from one or more partitions, wherein each of the one or more partitions comprise a cell expressing an antigen-binding molecule belonging to the same clonotype group. For example, high (e.g., over 40) target antigen UMI counts can be used to predict high binding affinity. As demonstrated in the Examples below, an antibody can be predicted to have specific binding affinity for the target CoV-S antigen if it is associated with high target antigen counts and low non-target antigen counts. [0147] In some embodiments, the antibody or antigen-binding fragment has a binding affinity and/or binding specificity with an equilibrium dissociation constant (KD) value of less than 500 nM, for example, less than 400 nM, less than 300 nM, less than 200 nM, less than 150 nM, less than 120 nM, less than 100 nM, less than 90 nM, less than 80 nM, less than 70 nM, less than 60 nM, less than 50 nM, less than 40 nM, less than 20 nM, less than 15 nM, less than 10 nM, less than 5 nM, less than 5 nM, or less than 1 nM. [0148] In some embodiments, the antibody or antigen-binding fragment has a binding affinity with a K_D value lower than the binding affinity between a SARS-CoV-2 S protein and its receptor ACE2, which has been previously estimated to have a KD value of about 120 nM. Accordingly, in some embodiment of the disclosure, the antibody or antigen-binding fragment has a binding affinity with a K_D value of less than 120 nM. In some embodiments, the antibody or antigen-binding fragment has a KD value of less than 120 nM and includes three heavy chain CDRs (HCDR1, HCDR2 and HCDR3), and three light chain CDRs (LCDR1, LCDR2 and LCDR3), wherein the heavy chain CDRs and light chain CDRs are independently selected from the HCDRs and LCDRs of the antibodies of Table 4. [0149] In some embodiments, the antibody or antigen-binding fragment has a binding affinity with an equilibrium dissociation constant (K_D) value of less than 120 nM and includes three heavy chain CDRs (HCDR1, HCDR2 and HCDR3), and three light chain CDRs (LCDR1, LCDR2 and LCDR3), wherein the heavy chain CDRs and light chain CDRs are independently selected from the HCDRs and LCDRs of the following group of antibodies: TXG-0072, TXG- 0098, TXG-0112, TXG-0115, TXG-0136, TXG-0153, TXG-0154, TXG-0173, TXG-0174, TXG-0192, TXG-0228, and TXG-0230. [0150] In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity to the HCVR of an antibody of Table 4. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of an antibody being any one of TXG-0072, TXG-0098, TXG-0112, TXG-0115, TXG-0136, TXG-0153, TXG-0154, TXG-0173, TXG-0174, TXG-0192, TXG-0228, or TXG- 0230. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0072. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0098. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0112. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0115. [0151] In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0136. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0153. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0154. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0173. In some embodiments, the antibody or antigen- binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0174. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0192. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0228. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the HCVR of TXG-0230. [0152] In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of an antibody being any one of TXG-0072, TXG-0098, TXG-0112, TXG-0115, TXG-0136, TXG- 0153, TXG-0154, TXG-0173, TXG-0174, TXG-0192, TXG-0228, or TXG-0230. [0153] In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0072. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0098. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0112. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0115. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0136. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0153. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0154. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0173. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0174. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0192. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0228. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the HCVR of TXG-0230. [0154] In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of an antibody being any one of TXG-0072, TXG-0098, TXG-0112, TXG-0115, TXG- 0136, TXG-0153, TXG-0154, TXG-0173, TXG-0174, TXG-0192, TXG-0228, or TXG-0230. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0072. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0098. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0112. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0115. [0155] In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0136. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0153. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0154. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0173. In some embodiments, the antibody or antigen- binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0174. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0192. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0228. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 90% sequence identity, for example, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the LCVR of TXG-0230. [0156] In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of an antibody being any one of TXG-0072, TXG-0098, TXG-0112, TXG-0115, TXG-0136, TXG- 0153, TXG-0154, TXG-0173, TXG-0174, TXG-0192, TXG-0228, or TXG-0230. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0072. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0098. In some embodiments, the antibody or antigen-binding fragment includes a HCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0112. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0115. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0136. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0153. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0154. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0173. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0174. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0192. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0228. In some embodiments, the antibody or antigen-binding fragment includes a LCVR which includes an amino acid sequence having at least 100% sequence identity to the LCVR of TXG-0230. [0157] In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof includes all framework regions (FWR) from the antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. In some embodiments, the antigen-binding molecule or antigen- binding fragment further includes a heavy chain constant region. In some embodiments, the heavy chain constant region is an IgA, IgD, IgE, IgG, or IgM heavy chain constant region. In some embodiments, the heavy chain constant region is of the same isotype and subclass as the antibody identified in Tables 1A-1B. In some embodiments, the heavy chain constant region is of the same isotype and subclass as the antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0158] In some embodiments, the antibody or antigen-binding fragment further includes a light chain constant region. In some embodiments, the light chain constant region is a kappa type or lambda type light chain constant region. In some embodiments, the light chain constant region is the same light chain constant region of the antibody identified in Tables 1A-1B. In some embodiments, the light chain constant region is the same light chain constant region of the antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG- 0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. [0159] As illustrated in Tables 7-8 and FIG.31, in some embodiments of the disclosure, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike (S) protein of two, three, four, five or more variants of SARS-CoV-2. Non-limiting examples of SARS-CoV-2 variants include alpha, beta, delta, gamma, kappa, and omicron. In some embodiments, at least one of the SARS-CoV-2 variants is omicron. In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike protein of the beta and gamma variants. Exemplary antibodies with binding affinity for the spike protein of the beta and gamma variants include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG- 0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0070, TXG-0072, TXG-0078, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0192, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0160] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike protein of the beta and kappa variants. Exemplary antibodies with binding affinity for the spike protein of the beta and kappa variants include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0070, TXG-0072, TXG-0078, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0136, TXG-0141, TXG-0144, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0192, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0161] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike protein of the beta and omicron variants. Exemplary antibodies with binding affinity for the spike protein of the beta and omicron variants include TXG-0057, TXG-0063, TXG-0070, TXG-0072, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0141, TXG-0144, TXG-0153, TXG-0174, TXG-0180, TXG-0183, TXG-0187, TXG-0192, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG- 0230. [0162] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike protein of the gamma and kappa variants. Exemplary antibodies with binding affinity for the spike protein of the gamma and kappa variants include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0163] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike protein of the gamma and omicron variants. Exemplary antibodies with binding affinity for the spike protein of the gamma and omicron variants include TXG-0057, TXG-0063, TXG-0070, TXG-0072, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0153, TXG-0174, TXG-0180, TXG-0183, TXG-0187, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0164] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike protein of the kappa and omicron variants. Exemplary antibodies with binding affinity for the spike protein of the kappa and omicron variants include TXG-0057, TXG-0063, TXG-0070, TXG-0072, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0174, TXG-0180, TXG-0183, TXG-0187, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG- 0230. [0165] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike protein of the beta, gamma, and omicron variants. Exemplary antibodies with binding affinity for the spike protein of the beta, gamma, and omicron variants include TXG-0057, TXG-0063, TXG-0070, TXG-0072, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0141, TXG-0144, TXG-0153, TXG-0174, TXG-0180, TXG-0183, TXG-0187, TXG-0192, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0166] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike protein of the beta, kappa, and omicron variants. Exemplary antibodies with binding affinity for the spike protein of the beta, kappa, and omicron variants include TXG-0057, TXG-0063, TXG-0070, TXG-0072, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0141, TXG-0144, TXG-0174, TXG-0180, TXG-0183, TXG-0187, TXG-0192, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0167] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike protein of the gamma, kappa, and omicron variants. Exemplary antibodies with binding affinity for the spike protein of the gamma, kappa, and omicron variants include TXG-0057, TXG-0063, TXG-0070, TXG-0072, TXG-0091, TXG- 0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0174, TXG-0180, TXG-0183, TXG-0187, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0168] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for the WT spike and all four beta, gamma, kappa, and omicron variants. Exemplary antibodies with binding affinity for the WT spike and all four beta, gamma, kappa, and omicron variants include TXG-0057, TXG-0063, TXG-0070, TXG-0072, TXG-0091, TXG- 0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0141, TXG-0144, TXG-0174, TXG-0180, TXG-0183, TXG-0187, TXG-0192, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0169] It is understood that coronavirus infection and vaccination induce antibody- mediated and T cell-mediated immunity, which can beneficially reduce disease severity and transmission. Such immunity can be embodied in polyclonal populations of naive immune cells as well as recalled antigen-experienced immune cells which can target new, previously seen, or evolutionarily-related antigens by searching an immensely diverse antibody repertoire space. Thus, broad and neutralizing antibodies are typically quite rare and their discovery often requires very deep sampling of the pathogen-specific antibody response. However, once identified, broadly neutralizing antibodies are vitally important, as they can inform the design of rational vaccine immunogens that focus the immune response toward highly conserved regions of viral vulnerability, and can represent a significant advance in the development of prophylactic and therapeutic antibodies that can maintain their efficacy in the face of rapidly evolving SARS- CoV2 mutants. As described in greater detail below, several antibodies described herein are pan- coronavirus antibodies that bind with high affinity to the NTD of SARS-CoV-2 S protein and to a spike protein of one or more SARS-CoV variants (e.g.., beta, gamma, kappa, and omicron), endemic human coronaviruses (HCoVs), and variants of thereof (e.g., HCoV-229E, HCoV- OC43, and HCoV-HKU1). These broadly protective antibodies against the NTD of the S1 subunit can be a particularly valuable addition to potential therapeutic antibody cocktails comprising anti-SARS-CoV-2 antibodies targeting other epitope regions of the SARS-CoV2 spike protein, such as the S2 subunit or the RBD of the S1 subunit, as increased epitope diversity from such a cocktail can provide added protection against viral escape. Accordingly, without being bound to any particular theory, broad and potently neutralizing NTD-targeting antibodies, such as those disclosed herein, could be particularly useful in therapeutic combination against SARS-CoV-2 and other coronaviruses and in combination with RBD-binding antibodies or non- S1 binding therapeutic antibodies (e.g., S2-targeting antibodies). [0170] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a high affinity to N-terminal domain of SARS-CoV-2 S protein (NTD) and/or to a spike protein of the omicron variant. Exemplary antibodies having these binding characteristics include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. Of these antibodies, at least five antibodies were found to have a high affinity to both (i) N-terminal domain of SARS-CoV-2 S protein (NTD) and (ii) a spike protein of the omicron variant. Exemplary antibodies having these binding characteristics include TXG-0072, TXG-0099, TXG-0114, TXG-0203, and TXG-0230. [0171] In some embodiments, the antigen-binding molecule or antigen-binding fragment has a binding affinity for one or more endemic human coronaviruses (HCoVs), or a variant of any thereof. Non-limiting examples of endemic HCoVs include HCoV-229E, HCoV-OC43, and HCoV-HKU1. Exemplary antibodies with binding affinity for HCoV-229E include TXG-0078, TXG-0112, TXG-0114, TXG-0136, TXG-0192, TXG-0203, TXG-0228, and TXG-0230. As shown in Table 9, all of these eight antibodies exhibit high affinity for HCoV-229E. [0172] Examples of antibodies exhibiting affinity for HCoV-OC43 include TXG-0006, TXG-0048, TXG-0070, TXG-0078, TXG-0100, TXG-0114, TXG-0136, TXG-0154, TXG-0192, and TXG-0203. Of these antibodies, at least four were found to have high affinity for the endemic human coronavirus HCoV-OC43 (see, e.g., TXG-0100, TXG-0114, TXG-0136, TXG- 0192, and TXG-0203 of Table 9) [0173] In some embodiments, the antigen-binding molecule or antigen-binding fragment has binding affinity for HCoV-OC43, HCoV-229E, SARS-CoV-2 omicron and the N-terminal domain of SARS-CoV-2. Exemplary antibodies having this ultra-broad binding affinity include TXG-0114, TXG-0192, and TXG-0203. In some embodiments, the antigen-binding molecule or antigen-binding fragment binds HCoV-OC43, HCoV-229E, SARS-CoV-2 omicron and the N- terminal domain of SARS-CoV-2 with high affinity. Examples of antibodies having this property include TXG-0114 and TXG-0203. [0174] In some embodiments, the antigen-binding molecule or antigen-binding fragment of the disclosure has binding affinity for the WT spike, all four variants (i.e., beta, gamma, kappa, and omicron) as well as the endemic coronaviruses HCoV-OC43 and HCoV-229E. Exemplary antibodies having this ultra-broad binding affinity include TXG-0114, TXG-0192, and TXG-0203. [0175] In some embodiments, the antibody or antigen-binding fragment has a high binding affinity (nM) for the endemic HKU1 coronavirus spike protein. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0078, TXG-0112, TXG-0114, TXG-0136, TXG-0187, TXG-0192, TXG-0203, TXG-0228, or TXG-0230. [0176] In some embodiments, the antibody or antigen-binding fragment has a sub- nanomolar binding affinity for a SARS-CoV-2 S protein, a fragment thereof, or a multimeric form thereof. For example, in some embodiments of the disclosure, the antibody or antigen- binding fragment has a binding affinity with a K_D value of less than 500 pM, for example, less than 100 pM, less than 50 pM, less than 10 pM, or less than 5 pM. In some embodiments, the antibody or antigen-binding fragment with sub-nanomolar binding affinity for a SARS-CoV-2 S protein is any one of TXG-0072, TXG-0098, TXG-0112, TXG-0115, TXG-0136, TXG-0153, TXG-0154, TXG-0173, TXG-0174, TXG-0192, TXG-0228, or TXG-0230. One skilled in the art will appreciate that when an antibody is said to “be any one of” or “be selected from a group,” this can mean that the antibody comprises all six CDRs from any one of the antibodies selected from the group. In some embodiments, the antibody can comprise the HCVR and LCVR from any one of the antibodies selected from the group. In some embodiments, the antibody can be any one of the antibodies in the group. [0177] In some embodiments, the antibody or antigen-binding fragment has a sub- nanomolar binding affinity for HCOV and/or for a SARS-CoV-2 S variant being any one of beta, gamma, delta, or kappa. In some embodiments, the antibody or antigen-binding fragment has a sub-picomolar binding affinity for HCOV and/or for a SARS-CoV-2 S variant being any one of beta, gamma, delta, or kappa. [0178] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and has binding affinity to the trimeric forms of wild-type SARS- CoV-2 S and beta, gamma, kappa variants. Exemplary antibodies having these binding affinity properties include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0057, TTXG-0094, TXG-0109, TXG-0115, TXG-0120, TXG-0141, TXG- 0144, TXG-0154, TXG-0180, TXG-0181, TXG-0183, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, and TXG-0210. In some embodiments, such antibodies also have binding affinity for the SARS-CoV-2 delta variant. [0179] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2, and has binding affinity to the N-terminal domain (NTD) of the S1 subunit. The neutralization potency of an antibody is generally quantified by the inhibitory concentration (IC) values (e.g., IC50) in live SARS-CoV-2 assays. Generally, an antibody is determined to potently neutralize SARS-CoV 2 when its IC50 is less than 1,000 nM/mL (see also, Table 11). As discussed in greater detail below, broadly protective antibodies against the NTD of the S1 subunit can be a particularly valuable addition to potential therapeutic antibody cocktails comprising anti-SARS-CoV-2 antibodies targeting either the S2 subunit or the RBD of the S1 subunit. In some embodiments, the antibody or antigen-binding fragment of the present disclosure potently neutralizes live SARS-CoV 2, and has binding affinity to the NTD of the S1 subunit and to the trimeric forms of wild-type SARS-CoV-2 S, as well as to trimeric forms of the gamma and kappa variants. Exemplary antibodies having these binding affinity properties include TXG-0076, TXG-0104, TXG-0170, and TXG-0173. In some embodiments, such antibodies also have binding affinity for the SARS-CoV-2 delta variant. [0180] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2, and has binding affinity to the N-terminal domain of the S1 subunit and to the trimeric form of wild-type SARS-CoV-2 S, as well as to trimeric forms of the beta, gamma, and kappa variants. Exemplary antibodies having these binding affinity properties include TXG-0063 and TXG-0099. In some embodiments, such antibodies also have binding affinity for the SARS-CoV-2 delta variant. [0181] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2, and has binding affinity to the N-terminal domain (NTD) of the S1 subunit and to the trimeric form of wild-type SARS-CoV-2 S, as well as to the trimeric form of the kappa variant. Exemplary antibodies having these binding affinity properties include TXG-0066. [0182] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2, and has binding affinity to the trimeric form of wild-type SARS- CoV-2 S, as well as to the trimeric forms of the gamma and kappa variants. Exemplary antibodies having these binding affinity properties include TXG-0129 and TXG-0197. [0183] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and has binding affinity to the trimeric form of wild-type SARS- CoV-2 S, as well as to the trimeric forms of the beta and gamma variants. Exemplary antibodies having these binding affinity properties include TXG-0088. [0184] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and does not have binding affinity to the N-terminal domain of the S1 subunit, but has binding affinity to the trimeric form of wild-type SARS-CoV-2 S protein, as well as to trimeric forms of HCOV, the beta, gamma, and kappa variants. Exemplary antibodies having these binding affinity properties include is TXG-0091. [0185] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and has binding affinity to the N-terminal domain of the S1 subunit and to the trimeric form of wild-type SARS-CoV-2 S, as well as to trimeric forms of the HCOV, beta, gamma, and kappa variants. Exemplary antibodies having these binding affinity properties include TXG-0078. [0186] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and has binding affinity to wild-type SARS-CoV-2 S protein. Exemplary antibodies having these binding affinity properties include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0057, TXG-0063, TXG-0066, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0094, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0170, TXG-0180, TXG-0181, TXG-0183, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, and TXG-0210. [0187] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and has binding affinity to the N-terminal domain of the S1 subunit. Exemplary antibodies having these binding affinity properties include TXG-0063, TXG- 0066, TXG-0076, TXG-0078, TXG-0099, TXG-0104, TXG-0170, TXG-0173, and TXG-0174. [0188] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and has binding affinity to the beta variant. Exemplary antibodies having these binding affinity properties include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0057, TXG-0063, TXG-0078, TXG-0088, TXG-0091, TXG-0094, TXG-0099, TXG-0109, TXG-0115, TXG-0120, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0174, TXG-0180, TXG-0181, TXG-0183, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, and TXG-0210. [0189] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and has binding affinity to the gamma variant. Exemplary antibodies having these binding affinity properties include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0057, TXG-0063, TXG-0076, TXG-0078, TXG-0088, TXG-0091, TXG-0094, TXG-0099, TXG-0104, TXG-0109, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0180, TXG-0181, TXG-0183, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, and TXG-0210. [0190] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and has binding affinity to the kappa variant. Exemplary antibodies having these properties include T TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0057, TXG-0063, TXG-0066, TXG-0076, TXG-0078, TXG-0091, TXG-0094, TXG-0099, TXG-0104, TXG-0109, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0180, TXG-0181, TXG-0183, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, and TXG- 0210. In some embodiments, such antibodies potently neutralize live SARS-CoV 2 and have binding affinity to the delta variant. [0191] In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV 2 and has binding affinity to HCoV-HKU1 (isolate N5) S1 protein. Exemplary antibodies having these properties include TXG-0078 and TXG-0091. [0192] In some embodiments, the antibodies and antigen-binding fragments of the disclosure bind to a target antigen, such as a CoV-S protein (e.g., SARS-CoV-2 S protein), and compete for binding with another antigen-binding polypeptide (e.g., antibody or antigen-binding fragment thereof) to the target antigen. Accordingly, also provided herein are antibodies or antigen-binding fragments thereof that compete for binding with an antibody disclosed herein, e.g., in Table 1A or Table 1B. [0193] The term “competes” as used herein, refers to an antibody or antigen-binding fragment that binds to a target antigen, and inhibits or blocks the binding of another antigen- binding polypeptide (e.g., antibody or antigen-binding fragment thereof) to the target antigen. The term also includes competition between two antigen-binding polypeptides e.g., antibodies, in both orientations, i.e., a first antibody that binds and blocks binding of second antibody and vice versa. In some embodiments, the first antigen-binding polypeptide (e.g., antibody or antigen- binding fragment) and second antigen-binding polypeptide (e.g., antibody or antigen-binding fragment thereof) may bind to the same epitope. Alternatively, the first and second antigen- binding polypeptides (e.g., antibodies or antigen-binding fragments) may bind to different, but, for example, overlapping epitopes, wherein binding of one inhibits or blocks the binding of the second antibody, e.g., via steric hindrance. Competition between antigen-binding polypeptides (e.g., antibodies or antigen-binding fragments) may be measured by methods known in the art, for example, by a real-time, label-free bio-layer interferometry assay. Epitope mapping (e.g., via alanine scanning or hydrogen-deuterium exchange (HDX)) can be used to determine whether two or more antibodies are non-competing (.e.g. on a spike protein RBD monomer), competing for the same epitope, or competing but with diverse micro-epitopes (e.g., identified through HDX). In some embodiments, competition between a first and second anti-CoV-S antigen- binding polypeptide (e.g., antibody or antigen-binding fragment thereof) is determined by measuring the ability of an immobilized first anti-CoV-S antigen-binding polypeptide (e.g., antibody) (not initially complexed with CoV-S protein) to bind to soluble CoV-S protein complexed with a second anti-CoV-S antigen-binding polypeptide (e.g., antibody or antigen- binding fragment thereof). A reduction in the ability of the first anti-CoV-S antigen-binding polypeptide (e.g., antibody or antigen-binding fragment thereof) to bind to the complexed CoV-S protein, relative to uncomplexed CoV-S protein, indicates that the first and second anti-CoV-S antigen-binding polypeptides (e.g., antibodies or antigen-binding fragments thereof) compete. The degree of competition can be expressed as a percentage of the reduction in binding. Such competition can be measured using a real time, label-free bio-layer interferometry assay, e.g., on an Octet RED384 biosensor (Pall ForteBio Corp.), ELISA (enzyme-linked immunosorbent assays) or SPR (surface plasmon resonance). [0194] In some embodiments, the antibodies and antigen-binding fragments of the disclosure have a neutralizing activity (e.g., antagonistic activity) against SARS-CoV-2, e.g., able to bind to and neutralize the activity of SARS-CoV-S, as determined by in vitro or in vivo assays. The ability of the antibodies of the disclosure to bind to, block and/or neutralize the activity of SARS-CoV-2 may be measured using any standard method known to those skilled in the art, including binding assays, or activity assays, as described herein. For example, the binding affinity and dissociation constants of anti-SARS-CoV-2 antigen-binding polypeptides for SARS-CoV-2 can be determined by surface plasmon resonance (SPR) assay. Alternatively, neutralization assays were used to determine infectivity of SARS-CoV-2 S protein-containing virus-like particles. One of ordinary skill in the art will understand that a neutralizing or antagonistic CoV-S antigen-binding polypeptide, e.g., antibody or antigen-binding fragment, generally refers to a molecule that inhibits an activity of CoV-S to any detectable degree, e.g., inhibits or reduces the ability of CoV-S to bind to a receptor such as ACE2, to be cleaved by a protease such as TMPRSS2, or to mediate viral entry into a host cell or mediate viral reproduction in a host cell. In some embodiments, the antibodies and antigen-binding fragments of the disclosure have a neutralization activity IC₅₀ value of less than 150 ng/ml for viral neutralization, as determined by a quantitative focus reduction neutralization test (FRNT) described previously by Zost et al. (Nature, 584:443–449, 2020). In some embodiments, the antibodies and antigen-binding fragments of the disclosure have blocking activity IC50 value of less than 150 ng/ml for blocking ACE2. In some embodiments, the antibodies and antigen- binding fragments of the disclosure have blocking activity IC50 value of less than 10 ng/ml for S2P ectodomain binding. In some embodiments, the antibodies and antigen-binding fragments of the disclosure have blocking activity IC₅₀ value of less than 10 ng/ml for RBD ectodomain binding. In some embodiments, the antibody or antigen-binding fragment neutralizes at least 50% of 200 times the tissue culture infectious dose (200×TCID50) of the coronavirus at an antibody concentration of 12.5 μg/ml or less. Here, TCID50 represents the viral load at which 50% of cells are infected when a solution containing the virus is added to cell culture. In some embodiments, neutralizing antibodies are effective at antibody concentrations of <3.125 μg/ml, <.8 μg/ml, <.2 μg/ml, or <.l μg/ml. [0195] In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC50 value below 1 µg/mL, below 200 ng/mL, or below 40 ng/mL. In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC50 value ranging from 200 ng/mL to 1,000 ng/mL. In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC50 value ranging from 40 ng/mL to 200 ng/mL. In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC₅₀ value ranging from 8 ng/mL to 40 ng/mL. [0196] In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC50 value that is 1 µg/mL or less. In some embodiments, the antibody or antigen-binding fragment having a neutralizing activity against SARS-CoV-2 with an IC₅₀ value of 1 µg/mL or less is any one of TXG-0001, TXG-0002, TXG-0004, TXG- 0005, TXG-0006, TXG-0008, TXG-0009, TXG-0057, TXG-0063, TXG-0066, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0094, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0180, TXG-0181, TXG-0183, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, or TXG- 0210. [0197] In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC50 value that is from 200 ng/mL to 1 µg/mL. In some embodiments, the antibody or antigen-binding fragment having a neutralizing activity against SARS-CoV-2 with an IC₅₀ value ranging from 200 ng/mL to 1 µg/mL is any one of TXG-0005, TXG-0008, TXG-0057, TXG-0066, TXG-0076, TXG-0091, TXG-0094, TXG-0099, TXG-0104, TXG-0141, TXG-0144, TXG-0170, TXG-0180, TXG-0183, TXG-0198, or TXG-0201 [0198] In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC50 value that is from 40 ng/mL to 200 ng/mL. In some embodiments, the antibody or antigen-binding fragment having a neutralizing activity against SARS-CoV-2 with an IC₅₀ value ranging from 40 ng/mL to 200 ng/mL is any one of TXG-0001, TXG-0002, TXG-0004, TXG-0009, TXG-0063, TXG-0078, TXG-0080, TXG-0081, TXG-0088, TXG-0100, TXG-0115, TXG-0181, TXG-0189, TXG-0197, TXG-0200, TXG-0202, TXG-0204, TXG-0209, or TXG-0210. [0199] In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC50 value that is 200 ng/mL or less. In some embodiments, the antibody or antigen-binding fragment having a neutralizing activity against SARS-CoV-2 with an IC50 value of 200 ng/mL or less is any one of TXG-0078, TXG-0080, TXG-0081, TXG-0088, TXG-0100, TXG-0109, TXG-0115, TXG-0120, TXG-0126, TXG-0128, TXG-0129, TXG-0154, TXG-0181, TXG-0189, TXG-0197, TXG-0200, TXG-0202, TXG-0204, TXG-0209, or TXG-0210. [0200] In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC₅₀ value that is 100 ng/mL or less. In some embodiments, the antibody or antigen-binding fragment having a neutralizing activity against SARS-CoV-2 with an IC50 value of 100 ng/mL or less is any one of TXG-0001, TXG-0004, TXG-0006, TXG-0009, TXG-0063, TXG-0080, TXG-0088, TXG-0109, TXG-0120, TXG-0129, TXG-0154, TXG-0189, TXG-0197, TXG-0200, TXG-0202, TXG-0204, TXG-0209, or TXG- 0210. [0201] In some embodiments, the antibody or antigen-binding fragment has a neutralizing activity against SARS-CoV-2 with an IC50 value that is 40 ng/mL or less. In some embodiments, the antibody or antigen-binding fragment having a neutralizing activity against SARS-CoV-2 with an IC₅₀ value of 40 ng/mL or less is any one of TXG-0006, TXG-0109, TXG-0120, TXG- 0126, TXG-0129, or TXG-0154. [0202] Some embodiments of the disclosure provide antibodies or antigen-binding fragments thereof that have a binding affinity to the NTD of a SARS-CoV-2 S protein and potently neutralizes live SARS-CoV-2. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0066, TXG-0072, TXG-0078, TXG-0104, TXG-0116, TXG-0136, TXG-0170, TXG-0173, or TXG-0174. In some embodiments, the antibody or antigen-binding fragment is selected from the group consisting of TXG-0173 and TXG-0174. In some embodiments, the antibody or antigen-binding fragment is TXG-0174. In some embodiments, the antibody or antigen-binding has a binding affinity to the NTD of an S protein from a SARS- CoV-2 delta variant. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0072, TXG-0078, TXG-0091, TXG-0099, TXG-0116, TXG-0137, TXG-0170, or TXG- 0174. [0203] Some embodiments of the disclosure provide antibodies or antigen-binding fragments thereof that have a binding affinity primarily to the RBD of a SARS-CoV-2 S protein and potently neutralizes live SARS-CoV-2. In some embodiments, such antibody or antigen- binding fragment is any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0063, TXG-0094, TXG-0100, TXG-0115, TXG-0120, TXG-0126, TXG-0128, TXG-0129, TXG-0141, TXG-0153, TXG-0154, TXG-0180, TXG-0181, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, or TXG-0210. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0057, TXG-0063, TXG-0091, TXG-0094, TXG-0109, TXG-0115, TXG-0120, TXG-0128, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0180, TXG-0181, TXG-0183, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0207, TXG-0209, or TXG-0210. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0057, TXG-0063, TXG-0091, TXG-0094, TXG-0120, TXG-0181, or TXG-0183. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0109, TXG-0128, TXG-0141, TXG- 0144, TXG-0180, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0207, TXG-0209, or TXG-0210. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0080, TXG-0081, TXG-0088, TXG-0100, TXG-0126, TXG-0129, or TXG- 0189. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0115, TXG-0153, or TXG-0154. In some embodiments, the antibody or antigen-binding fragment is TXG-0153. In some embodiments, the antibody or antigen-binding fragment is TXG-0115 or TXG-0154. [0204] In some embodiments, the antibody or antigen-binding fragment has a binding affinity primarily to the RBD of an S protein from a SARS-CoV-2 delta variant and potently neutralizes live SARS-CoV-2. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG- 0009, TXG-0063, TXG-0094, TXG-0100, TXG-0120, TXG-0126, TXG-0128, TXG-0129, TXG-0141, TXG-0180, TXG-0181, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, or TXG-0210. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0063, TXG-0094, TXG-0120, TXG-0128, TXG-0180, TXG-0181, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, or TXG-0209. In some embodiments, the antibody or antigen-binding fragment is TXG-0154. In some embodiments, the antibody or antigen-binding fragment has a binding affinity for a SARS-CoV-2 S protein and is any one of TXG-0112, TXG-0192, TXG-0228, or TXG-0230. [0205] In some embodiments, the antibody or antigen-binding fragment has a binding affinity primarily to the RBD of an S protein from a SARS-CoV-2 delta variant. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0063, TXG-0094, TXG-0120, or TXG-0181. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0128, TXG-0180, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, or TXG-0209. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0100, TXG-0126, TXG-0129, TXG-0141, or TXG-0210. In some embodiments, the antibody or antigen-binding fragment has a binding affinity for an S protein of a SARS-CoV-2 delta variant and is any one of TXG-0115, TXG-0136, TXG-0192, or TXG-0230. In some embodiments, such antibodies and antigen-binding fragments have a neutralizing activity against live SARS-CoV-2. In some embodiments, the antibody or antigen-binding fragment is TXG- 0115. [0206] In some embodiments, the antibody or antigen-binding fragment has a binding affinity for an S protein from a SARS-CoV-2 delta variant and is any one of TXG-0112, TXG- 0173, or TXG-0228. In some embodiments, such antibody or antigen-binding fragment potently neutralizes live SARS-CoV-2. In some embodiments, the antibody or antigen-binding fragment is TXG-0173. [0207] In some embodiments, the antibody or antigen-binding fragment has a binding affinity for a SARS-CoV-2 S protein and targets a distinct epitope from FDA approved antibodies such as Casirivimab, Imdevimab, Bamlanivimab, Etesevimab, and Sotrovimab. In some embodiments, such antibody or antigen binding-fragment. In some embodiments, such antibody or antigen-binding fragment is any one of TXG-0076, TXG-0099, TXG-0114, TXG- 0187, or TXG-0203. In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV-2 and is TXG-0076 or TXG-0099. In some embodiments, the antibody or antigen-binding fragment has a high binding affinity (nM) for an S protein from a wild-type SARS-CoV-2 or from the gamma, kappa, and beta variants. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0053, TXG-0099, TXG-0114, TXG- 0187, or TXG-0203. In some embodiments, the antibody or antigen-binding fragment has a high binding affinity (nM) for an NTD of a SARS-CoV-2 S protein. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0064, TXG-0076, TXG-0099, or TXG- 0146. In some embodiments, the antibody or antigen-binding fragment has a high binding affinity (nM) for the endemic HKU1 coronavirus spike protein. In some embodiments, the antibody or antigen-binding fragment is any one of TXG-0053, TXG-0114, TXG-0187, and TXG-0203. [0208] Some embodiments of the disclosure provide antibodies or antigen-binding fragments thereof that have a binding affinity for a spike protein of a SARS-CoV-2 delta variant and targets a distinct delta variant epitope from FDA approved antibodies such as Casirivimab, Imdevimab, Bamlanivimab, Etesevimab, and Sotrovimab. In some embodiments, such antibody or antigen-binding fragment is any one of TXG-0080, TXG-0175, or TXG-0232. In some embodiments, the antibody or antigen-binding fragment potently neutralizes live SARS-CoV-2 and is TXG-0080 or TXG-0175. In some embodiments, the antibody or antigen-binding fragment has a high binding affinity (nM) for an S protein from a wild-type SARS-CoV-2 or for an S protein from the gamma, kappa, and beta variants. In some embodiments, the antibody or antigen-binding fragment having a high binding affinity (nM) for an S protein from a wild-type SARS-CoV-2 or from the gamma, kappa, and beta variants is any one of TXG-0099, TXG-0114, TXG-0187, or TXG-0203. In some embodiments, the antibody or antigen-binding fragment has a binding affinity for a S protein from a SARS-CoV-2 delta variant and is any one of TXG-0057, TXG-0076, TXG-0081, TXG-0088, TXG-0104, TXG-0109, TXG-0114, TXG-0144, TXG-0183, TXG-0187, TXG-0189, or TXG-0203. In some embodiments, the antibody or antigen-binding fragment having has a binding affinity for a SARS-CoV-2 S protein potently neutralizes live SARS-CoV-2. In some embodiments, the antibody or antigen-binding fragment having a binding affinity for a SARS-CoV-2 S protein and potently neutralizing live SARS-CoV-2 is any one of TXG-0057, TXG-0076, TXG-0081, TXG-0088, TXG-0104, TXG-0109, TXG-0144, TXG-0183, or TXG-0189. In some embodiments, the antibody or antigen-binding fragment has a high binding affinity (nM) for an S protein from a wild-type SARS-CoV-2 or for an S protein from the gamma and kappa variants. In some embodiments, the antibody or antigen-binding fragment having a high binding affinity (nM) for an S protein from a wild-type SARS-CoV-2 or from the gamma and kappa variants is any one of TXG-0057, TXG-0076, TXG-0104, TXG-0109, TXG- 0114, TXG-0144, TXG-0183, TXG-0187, or TXG-0203. In some embodiments, the antibody or antigen-binding fragment has a high binding affinity (nM) for an S protein from a wild-type SARS-CoV-2 or from the beta, gamma, and kappa variants. In some embodiments, the antibody or antigen-binding fragment having a high binding affinity (nM) for an S protein from a wild- type SARS-CoV-2 or from the beta, gamma, and kappa variants is any one of TXG-0057, TXG- 0109, TXG-0114, TXG-0144, TXG-0183, TXG-0187, TXG-0203. [0209] In some embodiments, the isolated antibodies or antigen-binding fragments as described herein are recombinant antibodies and antigen-binding fragments. In some embodiments, the antibodies or antigen-binding fragments as described herein are isolated (e.g., purified) antibodies and antigen-binding fragments. As described above, when referring to polypeptides, e.g., antigen-binding polypeptides, antibodies, and antigen-binding fragments, one skilled in the art will understand that the term “isolated protein”, “isolated polypeptide” or “isolated antibody” is a protein, polypeptide or antibody that by virtue of its origin or source of derivation (1) is not associated with naturally associated components that accompany it in its native state, (2) is substantially free of other proteins from the same species, (3) is expressed by a recombinant cell from a different species, or (4) does not occur in nature. Thus, a polypeptide that is chemically synthesized or biosynthesized in a recombinant cellular system different from the cell from which it naturally originates can be “isolated” from its naturally associated components. A protein may also be rendered substantially free of naturally-associated components by isolation or purification, using one or more protein purification techniques. [0210] Examples of isolated antibodies include anti- SARS-CoV S protein antibodies that have been purified using SARS-CoV S protein or a portion thereof, anti- SARS-CoV S protein antibodies that have been synthesized by a hybridoma or other recombinant cell line in vitro, and a human anti-SARS-CoV S protein antibody derived from a transgenic mouse. Examples of purification techniques suitable for the purification of the antibodies and antigen-binding fragments disclosed herein include affinity chromatography, anion exchange chromatography (AEX), cation exchange chromatography (CEX), hydroxyapatite chromatography, size exclusion chromatography (SEC), hydrophobic interaction chromatography (HIC), metal affinity chromatography, mixed mode chromatography (MMC), centrifugation, diafiltration, and ultrafiltration. [0211] Generally, a polypeptide (e.g., antibody or antigen-binding fragment) is “substantially pure,” “substantially homogeneous,” or “substantially purified” when at least about 60 to 75% of a sample exhibits a single species of polypeptide. The polypeptide may be monomeric or multimeric. A substantially pure polypeptide generally includes about 50%, 60%, 70%, 80% or 90% W/W of a protein sample, more usually about 95%, 96%, 97%, 98%, or in some embodiments, over 99% pure. Protein purity or homogeneity may be indicated by a number of means available in the art, such as polyacrylamide gel electrophoresis of a protein sample, followed by visualizing a single polypeptide band upon staining the gel with a suitable stain available in the art. For certain purposes, higher resolution may be provided by using HPLC or other means available in the art for purification. Accordingly, in some embodiments, the isolated antibodies and antigen-binding fragments of the disclosure have a purity of greater than 80% such as, for example, a purity of greater than 85%, 90%, 95%, 96%, 97%, 98%, or 99%. [0212] In some embodiments, an anti-SARS-CoV-S antigen-binding polypeptide (e.g., antibody or antigen-binding fragment) described herein is not an antibody or antigen-binding fragment described in the following patent publications CN111620946A, CN111690059A, US10787501, and WO2015179535. In some embodiments, the an anti-SARS-CoV-S antigen- binding polypeptide (e.g., antibody or antigen-binding fragment) described herein is not an antibody or antigen-binding fragment described in the following documents Jakob Kreye et al., 2020; Seth Zost et al., (Nature Medicine, July 10, 2020); Xiaojian Han et al., (BioRxiv, Aug 21, 2020); Tal Noy-Porat et al., (Nature Comm., Aug.27, 2020); Edurne Rujas et al. (BioRxiv, Oct 16, 2020), 2020; Renhong Yan et al., (BioRxiv, 2020); Christoph Kreer et al., (Cell, Aug 20, 2020; Vol.182, Issue 4, pp.843-854); Yunlong Cao et al., (Cell, July 9, Vol.182, Issue 1, 2020); and Thomas Rogers et al., (Science Aug 21, 2020: Vol.369, Issue 6506, pp.956-963) . Nucleic acids [0213] The term “nucleic acid,” in its broadest sense, includes any compound and/or substance that comprise a polymer of nucleotides linked via a phosphodiester bond. These polymers are often referred to as oligonucleotides. Exemplary nucleic acids include ribonucleic acids (RNAs), deoxyribonucleic acids (DNAs), threose nucleic acids (TNAs), glycol nucleic acids (GNAs), peptide nucleic acids (PNAs), locked nucleic acids (LNAs) or hybrids thereof. They may also include RNAi-inducing agents, RNAi agents, siRNAs, shRNAs, miRNAs, antisense RNAs, ribozymes, catalytic DNA, tRNA, RNAs that induce triple helix formation, aptamers, vectors, etc. [0214] As discussed in greater detail below, the nucleic acids of the disclosure may encode any one of the antigen-binding molecules or antigen-binding fragment described herein. In some embodiments, the nucleic acids disclosed herein encode an amino acid sequence comprising the VL and/or an amino acid sequence comprising the VH of an antibody described herein (e.g., the light and/or heavy chains of the antibody). In some embodiments, the nucleic acids encode three or more CDRs of an antibody described in Tables 1A-1B and Sequence Listing (e.g., HCDR1, HCDR2 and HCDR3; or LCDR1, CDR2 and LCDR3). In some embodiments, the nucleic acids may encode the HCDR1, HCDR2, and HCDR3 of an antibody of Table 1A or Table 1B. In some embodiments, the nucleic acids may encode the HCDR1, HCDR2, and HCDR3 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG- 0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203. In some embodiments, the nucleic acids may encode the LCDR1, LCDR2, and LCDR3 of an antibody of Table 1A or Table 1B. In some embodiments, the nucleic acids may encode the LCDR1, LCDR2, and LCDR3 of an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203. [0215] In some embodiments, the nucleic acids may encode all six CDRs (e.g., HCDR1, HCDR2, HCDR3, LCDR1, LCDR2, and LCDR3) of an antibody of Table 1A or Table 1B. In some embodiments, the nucleic acids may encode all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG- 0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. In some embodiments, the nucleic acids may encode all six complementary determining regions (CDRs) from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203. [0216] In some embodiments, the nucleic acids may further encode the heavy chain framework regions HFWR1, HFWR2, HFWR3, and HFWR4 of the same antibody or antigen- binding fragment as set forth in Tables 2A-2B and Sequence Listing. In some embodiments, the nucleic acids may further encode the light chain framework regions LFWR1, LFWR2, LFWR3, and LFWR4 of the same antibody or antigen-binding fragment as set forth in Tables 2A-2B and Sequence Listing. [0217] As discussed above, the nucleic acids encoding the antigen-binding molecules or antigen-binding fragments may be DNA molecules or RNA molecules. [0218] The nucleic acid molecules provided can contain naturally occurring sequences, or sequences that differ from those that occur naturally, but, due to the degeneracy of the genetic code, encode the same polypeptide, e.g., antibody. For example, just as polypeptide variants can be described in terms of their identity with a referenced amino acid sequence, the nucleic acid molecules encoding the polypeptide variants can have a certain identity with those that encode the referenced amino acid sequence. For example, nucleic acid molecule variants encoding an antibody of the disclosure, a variant thereof, or an antigen-fragment thereof can be at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, preferably at least 75%, at least 80%, more preferably at least 85%, at least 90%, and most preferably at least 95% (e.g., 96%, 97%, 98%, or 99%) identical to the nucleic acid encoding a referenced antibody or an antigen-fragment thereof. Thus, in some embodiments, the nucleic acid molecule encoding an antibody of the disclosure, a variant thereof, or an antigen-fragment thereof can be at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, preferably at least 75%, at least 80%, more preferably at least 85%, at least 90%, and most preferably at least 95% (e.g., 96%, 97%, 98%, or 99%) identical to the nucleic acid encoding an antibody or antigen-binding fragment thereof having an amino acid sequence set forth in the Sequence Listing. [0219] In some embodiments, the nucleic acids include a nucleotide sequence encoding an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, preferably at least 75%, at least 80%, more preferably at least 85%, at least 90%, and most preferably at least 95% (e.g., 96%, 97%, 98%, or 99%) sequence identity to a HCVR of an antibody of the disclosure or an antigen-binding fragment thereof. Non-limiting examples of such nucleic acid sequences are listed in SEQ ID NOS: 3085-3888 and 6181-6580 of the Sequence Listing. In some embodiments, the nucleic acid molecule includes a nucleotide sequence encoding an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, preferably at least 75%, at least 80%, more preferably at least 85%, at least 90%, and most preferably at least 95% (e.g., 96%, 97%, 98%, or 99%) sequence identity to an LCVR of an antibody of the disclosure or an antigen-binding fragment thereof. Non-limiting examples of such nucleic acid sequences are also listed in SEQ ID NOS: 3889-4694 and 6581- 6980 of the Sequence Listing. In some embodiments, the nucleic acids include a first nucleic acid sequence having at least 70% sequence identity to a nucleic acid sequence being any one of SEQ ID NOS: 3085-3888 and 6181-6580; and a second nucleic acid sequence having at least 70% sequence identity to a nucleic acid sequence being any one of SEQ ID NOS: 3889-4694 and 6581-6980. [0220] Generally, the length of the nucleic acids of the present disclosure is greater than about 30 nucleotides in length (e.g., at least or greater than about 35, 40, 45, 50, 55, 60, 70, 80, 90, 100, 120, 140, 160, 180, 200, 250, 300, 350, 400, 450, 500, 600, 700, 800, 900, 1,000, 1,100, 1,200, 1,300, 1,400, 1,500, 1,600, 1,700, 1,800, 1,900, 2,000, 2,500, and 3,000, 4,000, 5,000, 6,000, 7,000, 8,000, 9,000, 10,000, 20,000, 30,000, 40,000, 50,000, 60,000, 70,000, 80,000, 90,000 or up to and including 100,000 nucleotides). [0221] In some embodiments, the nucleic acid of the present disclosure includes from about 30 to about 100,000 nucleotides (e.g., from 30 to 50, from 30 to 100, from 30 to 250, from 30 to 500, from 30 to 1,000, from 30 to 1,500, from 30 to 3,000, from 30 to 5,000, from 30 to 7,000, from 30 to 10,000, from 30 to 25,000, from 30 to 50,000, from 30 to 70,000, from 100 to 250, from 100 to 500, from 100 to 1,000, from 100 to 1,500, from 100 to 3,000, from 100 to 5,000, from 100 to 7,000, from 100 to 10,000, from 100 to 25,000, from 100 to 50,000, from 100 to 70,000, from 100 to 100,000, from 500 to 1,000, from 500 to 1,500, from 500 to 2,000, from 500 to 3,000, from 500 to 5,000, from 500 to 7,000, from 500 to 10,000, from 500 to 25,000, from 500 to 50,000, from 500 to 70,000, from 500 to 100,000, from 1,000 to 1,500, from 1,000 to 2,000, from 1,000 to 3,000, from 1,000 to 5,000, from 1,000 to 7,000, from 1,000 to 10,000, from 1,000 to 25,000, from 1,000 to 50,000, from 1,000 to 70,000, from 1,000 to 100,000, from 1,500 to 3,000, from 1,500 to 5,000, from 1,500 to 7,000, from 1,500 to 10,000, from 1,500 to 25,000, from 1,500 to 50,000, from 1,500 to 70,000, from 1,500 to 100,000, from 2,000 to 3,000, from 2,000 to 5,000, from 2,000 to 7,000, from 2,000 to 10,000, from 2,000 to 25,000, from 2,000 to 50,000, from 2,000 to 70,000, and from 2,000 to 100,000). [0222] The nucleic acids of the disclosure are not limited to sequences that encode polypeptides (e.g., antibodies); some or all of the non-coding sequences that lie upstream or downstream from a coding sequence (e.g., the coding sequence of an antibody) can also be included. Those of ordinary skill in the art of molecular biology are familiar with routine procedures for isolating nucleic acid molecules. In the event the nucleic acid molecule is a ribonucleic acid (RNA), molecules can be produced, for example, by in vitro transcription. [0223] The nucleic acids of the disclosure, including variants and naturally-occurring nucleic acid sequences, can be produced using a number of methods including, for example, those described in Sambrook 2012, supra. For example, the sequence of a nucleic acid molecule can be modified with respect to a naturally-occurring sequence from which it is derived using a variety of techniques including, but not limited to, classic mutagenesis techniques and recombinant DNA techniques, such as but not limited to site-directed mutagenesis, chemical treatment of a nucleic acid molecule to induce mutations, restriction enzyme cleavage of a nucleic acid fragment, ligation of nucleic acid fragments, PCR amplification and/or mutagenesis of selected regions of a nucleic acid sequence, recombinational cloning, and chemical synthesis, including chemical synthesis of oligonucleotide mixtures and ligation of mixture groups to “build” a mixture of nucleic acid molecules, and combinations thereof. Modified nucleic acids [0224] In some embodiments, the nucleic acid is an RNA molecule. In some embodiments, the RNA molecule is a messenger RNA (mRNA) molecule. In some embodiments, the nucleic acid comprises one or more modified nucleosides (termed “modified nucleic acid” or “modified nucleic acid molecule”) which have useful properties including the lack of a substantial induction of the innate immune response of a cell into which the nucleic acid (e.g., mRNA) is introduced. In some embodiments, one or more chemical modifications can be located on the nucleobase of the nucleotide. In some embodiments, one or more chemical modifications can be located on the sugar moiety of the nucleotide. In some embodiments, one or more chemical modifications can be located on the phosphate backbone of the nucleotide. [0225] Modified nucleosides and nucleotides can be prepared according to methods known in the art, for example, Ogata et al. Journal of Organic Chemistry 74:2585-2588, 2009; Purmal et al. Nucleic Acids Research 22(1): 72-78, 1994; Fukuhara et al. Biochemistry 1(4): 563-568, 1962; and Xu et al. Tetrahedron 48(9): 1729-1740, 1992. [0226] Modified nucleic acids (e.g., mRNAs) need not be uniformly modified along the entire length of the molecules. Different nucleotide modifications and/or backbone structures may exist at various positions in the nucleic acid. One of ordinary skill in the art will appreciate that the nucleotide analogs or other modification(s) may be located at any position(s) of a nucleic acid such that the function of the nucleic acid is not substantially decreased. A modification may also be a 5′ or 3′ terminal modification. The nucleic acids of the disclosure may contain at a minimum one and at maximum 100% modified nucleotides, or any intervening percentage, such as at least 50% modified nucleotides, at least 80% modified nucleotides, or at least 90% modified nucleotides. [0227] For example, the modified nucleic acids (e.g., mRNAs) may contain a modified pyrimidine such as uracil or cytosine. In some embodiments, at least 5%, at least 10%, at least 25%, at least 50%, at least 80%, at least 90% or 100% of the uracil in the nucleic acid may be replaced with a modified uracil. The modified uracil can be replaced by a compound having a single unique structure, or can be replaced by a plurality of compounds having different structures (e.g., 2, 3, 4 or more unique structures). In some embodiments, at least 5%, at least 10%, at least 25%, at least 50%, at least 80%, at least 90% or 100% of the cytosine in the nucleic acid may be replaced with a modified cytosine. The modified cytosine can be replaced by a compound having a single unique structure, or can be replaced by a plurality of compounds having different structures (e.g., 2, 3, 4 or more unique structures). [0228] In some embodiments, modified nucleosides may include pyridin-4-one ribonucleoside, 5-aza-uridine, 2-thio-5-aza-uridine, 2-thiouridine, 4-thio-pseudouridine, 2-thio- pseudouridine, 5-hydroxyuridine, 3-methyluridine, 5-carboxymethyl-uridine, 1-carboxymethyl- pseudouridine, 5-propynyl-uridine, 1-propynyl-pseudouridine, 5-taurinomethyluridine, 1- taurinomethyl-pseudouridine, 5-taurinomethyl-2-thio-uridine, 1-taurinomethyl-4-thio-uridine, 5- methyl-uridine, 1-methyl-pseudouridine, 4-thio-1-methyl-pseudouridine, 2-thio-1-methyl- pseudouridine, 1-methyl-1-deaza-pseudouridine, 2-thio-1-methyl-1-deaza-pseudouridine, dihydrouridine, dihydropseudouridine, 2-thio-dihydrouridine, 2-thio-dihydropseudouridine, 2- methoxyuridine, 2-methoxy-4-thio-uridine, 4-methoxy-pseudouridine, and 4-methoxy-2-thio- pseudouridine. In some embodiments, modified nucleosides include 5-aza-cytidine, pseudoisocytidine, 3-methyl-cytidine, N4-acetylcytidine, 5-formylcytidine, N4-methylcytidine, 5-hydroxymethylcytidine, 1-methyl-pseudoisocytidine, pyrrolo-cytidine, pyrrolo- pseudoisocytidine, 2-thio-cytidine, 2-thio-5-methyl-cytidine, 4-thio-pseudoisocytidine, 4-thio-1- methyl-pseudoisocytidine, 4-thio-1-methyl-1-deaza-pseudoisocytidine, 1-methyl-1-deaza- pseudoisocytidine, zebularine, 5-aza-zebularine, 5-methyl-zebularine, 5-aza-2-thio-zebularine, 2- thio-zebularine, 2-methoxy-cytidine, 2-methoxy-5-methyl-cytidine, 4-methoxy- pseudoisocytidine, and 4-methoxy-1-methyl-pseudoisocytidine. [0229] In other embodiments, modified nucleosides may include 2-aminopurine, 2, 6- diaminopurine, 7-deaza-adenine, 7-deaza-8-aza-adenine, 7-deaza-2-aminopurine, 7-deaza-8-aza- 2-aminopurine, 7-deaza-2,6-diaminopurine, 7-deaza-8-aza-2,6-diaminopurine, 1- methyladenosine, N6-methyladenosine, N6-isopentenyladenosine, N6-(cis- hydroxyisopentenyl)adenosine, 2-methylthio-N6-(cis-hydroxyisopentenyl) adenosine, N6- glycinylcarbamoyladenosine, N6-threonylcarbamoyladenosine, 2-methylthio-N6-threonyl carbamoyladenosine, N6,N6-dimethyladenosine, 7-methyladenine, 2-methylthio-adenine, and 2- methoxy-adenine. [0230] In other embodiments, modified nucleosides may include inosine, 1-methyl-inosine, wyosine, wybutosine, 7-deaza-guanosine, 7-deaza-8-aza-guanosine, 6-thio-guanosine, 6-thio-7- deaza-guanosine, 6-thio-7-deaza-8-aza-guanosine, 7-methyl-guanosine, 6-thio-7-methyl- guanosine, 7-methylinosine, 6-methoxy-guanosine, 1-methylguanosine, N2-methylguanosine, N2,N2-dimethylguanosine, 8-oxo-guanosine, 7-methyl-8-oxo-guanosine, 1-methyl-6-thio- guanosine, N2-methyl-6-thio-guanosine, and N2,N2-dimethyl-6-thio-guanosine. [0231] In some embodiments, the nucleotide may be modified on the major groove face and can include replacing hydrogen on C-5 of uracil with a methyl group or a halo group. In some embodiments, a modified nucleoside is 5′-O-(1-Thiophosphate)-Adenosine, 5′-O-(1- Thiophosphate)-Cytidine, 5′-O-(1-Thiophosphate)-Guanosine, 5′-O-(1-Thiophosphate)-Uridine or 5′-O-(1-Thiophosphate)-Pseudouridine. Pharmaceutical compositions and lipid nanoparticles [0232] As discussed above, the nucleic acids and compositions of the disclosure can be incorporated into formulations suitable for various downstream applications, for example, pharmaceutical compositions. [0233] In some embodiments, such compositions include one or more of the antibodies, antigen-binding fragments, and/or nucleic acids as disclosed herein in an amount, a combination, or in a form that is not found in nature. For example, in some embodiments, the compositions of the disclosure include one or more of the antibodies, antigen-binding fragments, and/or nucleic acids as disclosed herein that have been isolated (e.g., purified) to an extent that they no longer in a form in which they would be found be nature. In another example, in some embodiments, the compositions of the disclosure include the antibodies, antigen-binding fragments, and/or nucleic acids of the disclosure in amounts that do not occur in nature. In yet another example, in some embodiments, the antibodies, antigen-binding fragments, and/or nucleic acids of the disclosure are combined in formulations and/or combinations that do not occur in nature. In some embodiments, such compositions include a therapeutically or prophylactically effective amount of an antibody or antigen-binding fragment thereof in admixture with a suitable excipient, e.g., a pharmaceutically acceptable carrier. In some embodiments, an effective amount of a composition sufficient for achieving a therapeutic or prophylactic effect, ranges from about 0.000001 mg per kilogram body weight per administration to about 10,000 mg per kilogram body weight per administration. Suitably, the dosage ranges are from about 0.0001 mg per kilogram body weight per administration to about 100 mg per kilogram body weight per administration. [0234] Generally, pharmaceutically acceptable carriers suitable for use in the compositions of the disclosure include, but are not limited to, means any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents, and the like that are physiologically compatible. Non-limiting examples of pharmaceutically acceptable carriers are water, saline, phosphate buffered saline, dextrose, glycerol, ethanol and the like, as well as combinations thereof. In some embodiments, the compositions of the disclosure include isotonic agents, for example, sugars, polyalcohols such as mannitol, sorbitol, or sodium chloride in the composition. Other examples of pharmaceutically acceptable substances are wetting agents or minor amounts of auxiliary substances such as wetting or emulsifying agents, preservatives or buffers, which enhance the shelf life or effectiveness of the antibody. Additional pharmaceutically acceptable carriers suitable for use in the compositions of the disclosure include, but are not limited to, excipients, diluents, antioxidants, preservatives, coloring, flavoring and diluting agents, emulsifying agents, suspending agents, solvents, fillers, bulking agents, buffers, delivery vehicles, tonicity agents, cosolvents, wetting agents, complexing agents, buffering agents, antimicrobials, and surfactants. [0235] In one aspect, the antibodies, antigen-binding fragments, and/or nucleic acids of the disclosure can be incorporated into compositions suitable for various downstream applications, for example, pharmaceutical compositions. Exemplary compositions of the disclosure include pharmaceutical compositions which generally include one or more of the antibodies, antigen- binding fragments, and/or nucleic acids as described herein and a pharmaceutically acceptable excipient, e.g., carrier or diluent. In some embodiments, the composition is a sterile composition. In some embodiments, the composition is a lyophilized, desiccated, or freeze-dried composition. In some embodiments, the composition is formulated as a vaccine. In some embodiments, the composition further includes an adjuvant. [0236] In some embodiments of the disclosure, the compositions of the disclosure are formulated into a lipid nanoparticle (LNP) comprising at least one lipid. In principle, there are no particular limitations with regard to methods and processes to be used for the making of the LNPs disclosed herein. Suitable methods and processes for making LNPs include, but not limited to, continuous mixing methods, direct dilution processes, and in-line dilution processes. Additional examples of suitable methods for making LNPs are described in, for example, Semple et al. (2010) Nat. Biotechnol.28:172-176; Jayarama et al. (2012), Angew. Chem. Int. Ed., 51: 8529-8533; and Maier et al. (2013) Molecular Therapy 21, 1570-1578, U.S. Patent Nos. 10,898,574 and 10,702,600, which are herein incorporated by reference. [0237] In some embodiments, the LNPs according to embodiments of the present disclosure may be prepared by standard T-tube mixing techniques, turbulent mixing, trituration mixing, agitation promoting orders self-assembly, or passive mixing of all the elements with self- assembly of elements into nanoparticles. In some embodiments, the LNPs disclosed herein may be produced via a continuous mixing method, e.g., a process that includes providing an aqueous solution comprising an antigen-binding molecule or nucleic acid (e.g., mRNA) in a first reservoir, providing an organic lipid solution in a second reservoir (wherein the lipids present in the organic lipid solution are solubilized in an organic solvent, e.g., a lower alkanol such as ethanol), and mixing the aqueous solution with the organic lipid solution such that the organic lipid solution mixes with the aqueous solution so as to substantially instantaneously produce a lipid vesicle (e.g., liposome) encapsulating the antigen-binding molecule or nucleic acid within the lipid vesicle. This process and the apparatus for carrying out this process are known and described in detail in, for example, U.S. Patent Publication No.20040142025, the disclosure of which is herein incorporated by reference in its entirety. [0238] The action of continuously introducing lipid and buffer solutions into a mixing environment, such as in a mixing chamber, causes a continuous dilution of the lipid solution with the buffer solution, thereby producing a lipid vesicle substantially instantaneously upon mixing. In this process, the lipid solution is diluted sufficiently rapidly in a hydration process with sufficient force to effectuate vesicle generation. By mixing the aqueous solution comprising an antigen-binding molecule or nucleic acid with the organic lipid solution, the organic lipid solution undergoes a continuous stepwise dilution in the presence of the buffer solution (i.e., aqueous solution) to produce an LNP. [0239] The LNPs of the present disclosure can be assessed for size using devices that size nanoparticles, e.g., in solution, such as the Malvern™ Zetasizer™. In some embodiments, the LNPs formed using the continuous mixing method can have a size of from about 30 nm to about 150 nm, from about 40 nm to about 150 nm, from about 50 nm to about 150 nm, from about 60 nm to about 130 nm, from about 70 nm to about 110 nm, from about 70 nm to about 100 nm, from about 80 nm to about 100 nm, from about 90 nm to about 100 nm, from about 70 to about 90 nm, from about 80 nm to about 90 nm, from about 70 nm to about 80 nm, less than about 120 nm, 110 nm, 100 nm, 90 nm, or 80 nm, or about 30 nm, 35 nm, 40 nm, 45 nm, 50 nm, 55 nm, 60 nm, 65 nm, 70 nm, 75 nm, 80 nm, 85 nm, 90 nm, 95 nm, 100 nm, 105 nm, 110 nm, 115 nm, 120 nm, 125 nm, 130 nm, 135 nm, 140 nm, 145 nm, or 150 nm (or any fraction thereof or range therein). In some embodiments, the LNPs thus formed do not aggregate and are optionally sized to achieve a substantially uniform particle size. [0240] In some embodiments, the LNPs disclosed herein may be produced via a direct dilution process that includes forming a lipid vesicle (e.g., liposome) solution and immediately and directly introducing the lipid vesicle solution into a collection vessel containing a controlled amount of dilution buffer. In some embodiments, the collection vessel includes one or more elements configured to stir the contents of the collection vessel to facilitate dilution. In one aspect, the amount of dilution buffer present in the collection vessel is substantially equal to the volume of lipid vesicle solution introduced thereto. As a non-limiting example, a lipid vesicle solution in 45% ethanol when introduced into the collection vessel containing an equal volume of dilution buffer will advantageously yield smaller particles. [0241] In yet some other embodiments, the LNPs disclosed herein may be produced via an in-line dilution process in which a third reservoir containing dilution buffer is fluidly coupled to a second mixing region. In these embodiments, the lipid vesicle (e.g., liposome) solution formed in a first mixing region is immediately and directly mixed with dilution buffer in the second mixing region. In some embodiments, the second mixing region includes a T-connector arranged so that the lipid vesicle solution and the dilution buffer flows meet as opposing 180° flows; however, connectors providing shallower angles can be used, e.g., from about 20° to about 180° (e.g., about 90°). A pump mechanism delivers a controllable flow of buffer to the second mixing region. In one embodiment, the flow rate of dilution buffer provided to the second mixing region is controlled to be substantially equal to the flow rate of lipid vesicle solution introduced thereto from the first mixing region. This embodiment advantageously allows for more control of the flow of dilution buffer mixing with the lipid vesicle solution in the second mixing region, and therefore also the concentration of lipid vesicle solution in buffer throughout the second mixing process. Such control of the dilution buffer flow rate advantageously allows for small particle size formation at reduced concentrations. [0242] These processes and the apparatuses for carrying out these direct dilution and in- line dilution processes are known and described in detail in, for example, U.S. Patent Publication No.20070042031, the disclosure of which is herein incorporated by reference. [0243] The LNPs formed using the direct dilution and in-line dilution processes can have a size of from about 30 nm to about 150 nm, from about 40 nm to about 150 nm, from about 50 nm to about 150 nm, from about 60 nm to about 130 nm, from about 70 nm to about 110 nm, from about 70 nm to about 100 nm, from about 80 nm to about 100 nm, from about 90 nm to about 100 nm, from about 70 to about 90 nm, from about 80 nm to about 90 nm, from about 70 nm to about 80 nm, less than about 120 nm, 110 nm, 100 nm, 90 nm, or 80 nm, or about 30 nm, 35 nm, 40 nm, 45 nm, 50 nm, 55 nm, 60 nm, 65 nm, 70 nm, 75 nm, 80 nm, 85 nm, 90 nm, 95 nm, 100 nm, 105 nm, 110 nm, 115 nm, 120 nm, 125 nm, 130 nm, 135 nm, 140 nm, 145 nm, or 150 nm (or any fraction thereof or range therein). In some embodiments, the nanoparticles thus formed do not aggregate and are optionally sized to achieve a substantially uniform particle size. [0244] If needed, the lipid nanoparticles of the present disclosure can be sized by any of the methods available for sizing liposomes and/or lipid nanoparticles. The sizing may be conducted in order to achieve a desired size range and relatively narrow distribution of particle sizes. [0245] Several techniques are available for sizing the particles to a desired size. One sizing method, used for liposomes and equally applicable to the present particles, is described in U.S. Pat. No.4,737,323, the disclosure of which is herein incorporated by reference. Sonicating a particle suspension either by bath or probe sonication produces a progressive size reduction down to particles of less than about 50 nm in size. Homogenization is another method which relies on shearing energy to fragment larger particles into smaller ones. In a typical homogenization procedure, particles are recirculated through a standard emulsion homogenizer until selected particle sizes, typically between about 60 and about 80 nm, are observed. In both methods, the particle size distribution can be monitored by conventional laser-beam particle size discrimination, or QELS. [0246] In some embodiments, the LNPs disclosed herein have an average diameter of less than about 1000 nm, about 500 nm, about 250 nm, about 200 nm, about 150 nm, about 100 nm, about 75 nm, about 50 nm, or about 25 nm. In some embodiments, the LNPs have an average diameter ranging from about 70 nm to 100 nm. In some embodiments, the LNPs have an average diameter ranging from about 88 nm to about 92 nm, from 82 nm to about 86 nm, or from about 80 nm to about 95 nm. [0247] In some embodiments, the LNP has a mean diameter ranging from about 10 nm to about 200 nm. In some embodiments, the LNP has a mean diameter ranging from about 10 nm to about 500 nm, from about 20 to about 400 nm, from about 30 to about 300 nm, or from about 40 to about 200 nm. In some embodiments, the LNP has a mean diameter ranging from about 50 to about 150 nm, from about 50 to about 200 nm, from about 80 to about 100 nm, or from about 80 to about 200 nm. [0248] In some embodiments, the compositions of the disclosure may be formulated into a LNP that includes one or more of ionizable cationic lipid, cationic lipid, anionic lipid, neutral lipid, sterol, and PEG-modified lipid. In some embodiments, the lipid may be a cationic lipid such as, but not limited to, DLin-DMA, DLin-D-DMA, DLin-MC3-DMA (MC3), DLin-KC2- DMA (MC2), DODMA, 98N12-5, C12-200, C14-PEG2000, XTC, MD1, 7C1, and amino alcohol lipids. In some embodiments, the lipid may be an ionizable cationic lipid, such as 2,2- dilinoleyl-4-dimethylaminoethyl-[1,3]-dioxolane (DLin-KC2-DMA), dilinoleyl-methyl-4- dimethylaminobutyrate (DLin-MC3-DMA), or di((Z)-non-2-en-1-yl) 9-((4- (dimethylamino)butanoyl)oxy)heptadecanedioate (L319), ALC-0315, C12-200, LN16, MC3, MD1, SM-102. In some embodiments, the lipid may be a neutral lipid such as, but not limited to, DPSC, DPPC, POPC, DOPE, and SM. Non-limiting examples of lipids suitable for the compositions and methods of the disclosure include DLin-DMA, DLin-K-DMA, 98N12-5, C12- 200, DLin-MC3-DMA, DLin-KC2-DMA, DODMA, PLGA, PEG, PEG-DMG, PEGylated lipids and amino alcohol lipids. The amino alcohol cationic lipid may be the lipids described in and/or made by the methods described in U.S. Patent Publication No. US20130150625, herein incorporated by reference in its entirety. Additional lipids suitable for the compositions and methods of the present disclosure can be found in U.S. Patent Nos.10,898,574 and 10,702,600, which are incorporated by reference in their entireties. [0249] In some embodiments, the LNP compositions may further include a neutral lipid, a sterol and a molecule capable of reducing particle aggregation, for example a PEG or PEG- modified lipid. In some embodiments, the LNP further includes phosphatidyl choline. In some embodiments, the sterol is cholesterol. [0250] In some embodiments, the LNPs of the disclosure further include non-lipid polycations which are useful to promote the lipofection of cells using the present compositions. Examples of suitable non-lipid polycations include hexadimethrine bromide (e.g., POLYBRENE®, Aldrich Chem) or other salts of hexadimethrine. Other suitable polycations include, for example, salts of poly-L-ornithine, poly-L-arginine, poly-L-lysine, poly-D-lysine, polyallylamine, and polyethyleneimine. Addition of these salts is generally after the particles have been formed. [0251] One skilled in the art will appreciate that the lipid(s) can be combined with the antigen-binding molecules and/or nucleic acids of the disclosure in a wide range molar ratios to produce a LNP. In some embodiments, the mass ratio (wt/wt) of lipid to antigen-binding polypeptide/nucleic acid in the LNP ranges from about 2:1 to about 100:1. In some embodiments, the mass ratio (wt/wt) of lipid to antigen-binding polypeptide/nucleic acid in the LNP is about 100:1 to about 3:1, about 70:1 to 10:1, or 16:1 to 4:1. In some embodiments, the mass ratio (wt/wt) of lipid to antigen-binding polypeptide/nucleic acid in the LNP is about 16:1 to 4:1. In some embodiments, mass ratio (wt/wt) of lipid to antigen-binding polypeptide/nucleic acid in the LNP is about 20:1. In some embodiments, the mass ratio of lipid to nucleic acid in the LNP delivery system is about 8:1. [0252] In some embodiments, the lipid to antigen-binding polypeptide/nucleic acid ratios (wt/wt) in an LNP may range from about 1 (1:1) to about 100 (100:1), from about 5 (5:1) to about 100 (100:1), from about 1 (1:1) to about 50 (50:1), from about 2 (2:1) to about 50 (50:1), from about 3 (3:1) to about 50 (50:1), from about 4 (4:1) to about 50 (50:1), from about 5 (5:1) to about 50 (50:1), from about 1 (1:1) to about 25 (25:1), from about 2 (2:1) to about 25 (25:1), from about 3 (3:1) to about 25 (25:1), from about 4 (4:1) to about 25 (25:1), from about 5 (5:1) to about 25 (25:1), from about 5 (5:1) to about 20 (20:1), from about 5 (5:1) to about 15 (15:1), from about 5 (5:1) to about 10 (10:1), or about 5 (5:1), 6 (6:1), 7 (7:1), 8 (8:1), 9 (9:1), 10 (10:1), 11 (11:1), 12 (12:1), 13 (13:1), 14 (14:1), 15 (15:1), 16 (16:1), 17 (17:1), 18 (18:1), 19 (19:1), 20 (20:1), 21 (21:1), 22 (22:1), 23 (23:1), 24 (24:1), or 25 (25:1), or any fraction thereof or range therein. The ratio of the starting materials (input) also falls within this range. [0253] In some embodiments, the lipid nanoparticles described herein may be made in a sterile environment. [0254] In some embodiments, the compositions disclosed herein, e.g., LNP compositions, include a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a first antibody or antigen-binding fragment belonging to bin 1 or bin 2 described in Example 14, and a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 3, bin 4, or bin 3/4 described in Example 14. In some embodiments, the first agent is, comprises, or encodes a first antibody or antigen-binding fragment belonging to bin 1 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 3, bin 4, or bin 3/4 described in Example 14. In some embodiments, the first agent is, comprises, or encodes a first antibody or antigen-binding fragment belonging to bin 2 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 3, bin 4, or bin 3/4 described in Example 14. In some embodiments, the first agent is, comprises, or encodes a first antibody or antigen-binding fragment belonging to bin 3 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 4 described in Example 14. In some embodiments, the first agent is, comprises, or encodes a first antibody or antigen- binding fragment belonging to bin 3 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 3/4 described in Example 14. In some embodiments, the first agent is, comprises, encodes a first antibody or antigen-binding fragment belonging to bin 4 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 3/4 described in Example 14. [0255] In some embodiments, the first agent and the second agent are formulated into a single LNP. In some embodiments, the first and the second agents are formulated into separate LNPs, e.g., the first agent is formulated into a first LNP and the second agent is formulated into a second LNP. In some embodiments, the fist and the second LNPs may have similar (e.g., identical) physicochemical attributes. In some embodiments, the fist and the second LNPs may have different physicochemical properties to achieve desired (e.g., optimal) therapeutic effects. [0256] As described above, several antibodies described herein are pan-coronavirus antibodies that bind with high affinity to the NTD of SARS-CoV-2 S protein and to a spike protein of one or more SARS-CoV variants (e.g.., beta, gamma, kappa, and omicron), endemic human coronaviruses (HCoVs), and variants of thereof (e.g., HCoV-229E, HCoV-OC43, and HCoV-HKU1). These broad and potently neutralizing NTD-targeting antibodies could be particularly useful in therapeutic combination against SARS-CoV-2 and other coronaviruses and in combination with RBD-binding or non-S1 binding therapeutic antibodies. [0257] In some embodiments, the compositions disclosed herein, e.g., LNP compositions, include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing NTD-targeting antibody, and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing antibody that does not target the NTD. In some embodiments, the second agent is or comprises a neutralizing RBD-targeting antibody. In some embodiments, the neutralizing NTD-targeting antibody is TXG-0060, TXG- 0066, TXG-0071, TXG-0076, TXG-0078, TXG-0079, TXG-0099, TXG-0104, TXG-0116, TXG-0119, TXG-0131, TXG-0132, TXG-0137, TXG-0162, TXG-0163, TXG-0164, TXG-0168, TXG-0170, TXG-0173, TXG-0174, TXG-0184 , TXG-0136, or an antigen-binding fragment of any thereof (see, e.g., Tables 6 and 9); and the neutralizing antibody that does not bind the NTD is TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG- 0057, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0093, TXG-0094, TXG-0100, TXG-0109, TXG-0115, TXG-0120, TXG-0126, TXG-0129, TXG-0140, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0183, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG- 0201, TXG-0202, TXG-0204, TXG-0210, or an antigen-binding fragment of any thereof (see, e.g., Table 12). [0258] In some embodiments, the compositions disclosed herein e.g., LNP compositions, include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing (e.g., has an IC50 of 1000 ng/ml or less) NTD-targeting antibody, and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing RBD antibody. In some embodiments, the potently neutralizing NTD-targeting antibody is TXG-0066, TXG-0076, TXG-0078, TXG-0099, TXG-0104, TXG- 0170, TXG-0173, and TXG-0174, or an antigen-binding fragment of any thereof; and the potently neutralizing RBD antibody is TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG- 0006, TXG-0008, TXG-0009, TXG-0057, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0093, TXG-0094, TXG-0100, TXG-0109, TXG-0115, TXG-0120, TXG-0126, TXG-0129, TXG-0140, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0180, , TXG-0183, TXG- 0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, TXG-0210, or an antigen-binding fragment of any thereof (see, e.g., Table 12). [0259] In some embodiments, the compositions disclosed herein e.g., LNP compositions, include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs). In some embodiments, the neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs) TXG-0072, TXG-0078, TXG-0099, TXG-0174, or an antigen- binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs) is TXG- 0006, TXG-0049, TXG-0057, TXG-0070, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0109, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0180, TXG-0183, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, TXG-0210, or an antigen-binding fragment of any thereof. [0260] In some embodiments, the compositions disclosed herein e.g., LNP compositions, include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs). In some embodiments, the neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs) is TXG- 0072, TXG-0078, TXG-0099, TXG-0174, or an antigen-binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0091, TXG-0006, TXG-0154, or an antigen-binding fragment of any thereof. [0261] In some embodiments, the compositions disclosed herein e.g., LNP compositions, include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs). In some embodiments, the potently neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs) is TXG-0078, TXG-0099, TXG-0174, or an antigen-binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0006, TXG-0091, TXG-0154, or an antigen-binding fragment of any thereof. [0262] In some embodiments, the compositions disclosed herein e.g., LNP compositions, include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for the omicron variant of SARS-CoV-2 and at least one endemic human coronaviruses (HCoVs). In some embodiments, the potently neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS- CoV-2 or at least one endemic human coronaviruses (HCoVs) is TXG-0078, TXG-0099, TXG- 0174, or an antigen-binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for the omicron variant of SARS-CoV-2 and at least one endemic human coronaviruses (HCoVs) is TXG-0091 or an antigen-binding fragment thereof. [0263] In some embodiments, the compositions disclosed herein e.g., LNP compositions, include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing NTD-targeting antibody with binding affinity for at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs). In some embodiments, the potently neutralizing NTD-targeting antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0078 or an antigen-binding fragment thereof; and the neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0006, TXG-0091, TXG-0154, or an antigen-binding fragment of any thereof. [0264] In some embodiments, the compositions disclosed herein, e.g., LNP compositions, include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a TXG-0078 or an antigen-binding fragment thereof, and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is or comprises TXG-0091 or an antigen-binding fragment thereof. In some embodiments, the compositions disclosed herein include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a NTD- targeting antibody with binding affinity for at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs). In some embodiments, the NTD-targeting antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0078, TXG-0114, TXG-0136, or an antigen-binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0091, TXG-0006, TXG- 0154, or an antigen-binding fragment of any thereof. [0265] In some embodiments, the compositions disclosed herein e.g., LNP compositions, include (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is or comprises or encodes an antibody being any one of TXG-0078 or TXG-0174; and an antigen-binding fragment of any thereof; and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is or comprises or encodes an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0081, TXG-0115, TXG-0154, or TXG-0180; or an antigen-binding fragment of any thereof. METHODS OF THE DISCLOSURE Methods of treatment [0266] As discussed above, one aspect of the disclosure relate to methods for treating, preventing, or ameliorating a health condition or viral infection (e.g., reducing the likelihood of a viral infection such as coronavirus infection) by therapeutically or prophylactically administering a composition described herein to a subject in need of such treatment, prevention, or amelioration. In some embodiments, the methods include therapeutically or prophylactically administering to the subject an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all six CDRs from an antibody identified in the Sequence Listing, and wherein the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the spike (S) protein of two, three, four, five or more variants of SARS- CoV-2, and/or for one or more human coronaviruses (HCoVs) that is any one of HCoV-229E, HCoV-OC43, or HCoV-HKU1; or a variant of any thereof. In some embodiments, the one or more HCoVs is HCoV-229E or HCoV-OC43. [0267] In some embodiments, the antibody is any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230. In some embodiments, the antibody is any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203. [0268] In one aspect, provided herein are methods for reducing binding of a spike (S) protein of a coronavirus (CoV-S) to a cell in a subject and/or reducing entry of the coronavirus into a cell of a subject, wherein the methods include therapeutically or prophylactically administering to the subject: (a) an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike (S) protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof includes all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230; and optionally wherein the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the spike (S) protein of two, three, four, five or more variants of SARS-CoV-2, and/or for one or more human coronaviruses (HCoVs) being any one of HCoV-229E, HCoV-OC43, HCoV-HKU1, or a combination thereof, or a variant of any thereof; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof of (a). In some embodiments, the one or more HCoVs is HCoV-229E and/or HCoV-OC43. [0269] In some embodiments, the binding of the CoV-S protein to a cell in a subject is reduced at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or at least 2 times, at least 3 times, at least 4 times, at least 5 times, at least 6 times, at least7 times, at least 8 times, at least 9 times, or at least 10 times, as compared to its binding in a reference subject who has not been administered with the composition. In some embodiments, the entry of the coronavirus into a cell of a subject is reduced at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or at least 2 times, at least 3 times, at least 4 times, at least 5 times, at least 6 times, at least7 times, at least 8 times, at least 9 times, or at least 10 times, as compared to its entry in a reference subject who has not been administered with the composition. [0270] In another aspect, provided herein are methods for inducing an immune response in a subject, wherein the methods include administering to the subject a composition as disclosed herein. In another aspect, provided herein are methods for aiding in the neutralization of two, three, four, five or more variants of SARS-CoV-2, wherein said aiding includes providing: (a) an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike (S) protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof includes all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen- binding fragment thereof of (a). In some embodiments, the neutralization takes place in a single subject who has been infected by two, three, four, five or more variants of SARS-CoV-2. In some embodiments, the neutralization takes place in plurality of subjects who have each been infected by a different variant. [0271] In yet another aspect, provided herein are methods for in reducing the viral load of two, three, four, five or more variants of SARS-CoV-2, wherein said aiding includes providing: (a) an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike (S) protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof includes all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen- binding fragment thereof of (a). [0272] In another aspect, provided herein are methods for aiding in the neutralization of two, three, four, five or more variants of SARS-CoV-2, wherein said aiding includes providing a composition as disclosed herein. In another aspect, provided herein are methods for aiding in reducing the viral load of two, three, four, five or more variants of SARS-CoV-2, wherein said aiding includes providing a composition as disclosed herein. [0273] Non-limiting exemplary embodiments of the methods as described herein can include one or more of the following features. In some embodiments, the neutralization and/or the reduction of viral load takes place in a single subject who has been infected by two, three, four, five or more variants of SARS-CoV-2. In some embodiments, the neutralization and/or the reduction of viral load takes place in plurality of subjects who have each been infected by a different SARS-CoV-2 variant. In some embodiments, the antigen-binding molecule or antigen- binding fragment thereof includes all six CDRs from an antibody of Table 1A or Table 1B. In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof includes all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG- 0203. [0274] In some embodiments, the coronavirus belongs to a genus being any one or alphacoronavirus, betacoronavirus, gammacoronavirus, or deltacoronavirus. In some embodiments, the coronavirus belongs to a betacoronavirus lineage such as, for example, lineage A, lineage B, lineage C, and lineage D. In some embodiments, the coronavirus is human coronavirus 229E, OC43, HKU1, NL63, SARS-CoV-1, SARS-CoV-2, MERS-CoV, or a variant of any thereof. In some embodiments, the coronavirus is SARS-CoV-2 or a variant thereof. Non- limiting examples of SARS-CoV-2 variants suitable for the compositions and methods of the disclosure include alpha, beta, delta, gamma, kappa, and omicron. In some embodiments, at least one of the SARS-CoV-2 variants is omicron. [0275] In some embodiments, the methods of the disclosure include administering (e.g., therapeutically or prophylactically) one or more compositions of the disclosure to a subject. In some embodiments, the compositions of the disclosure may be administered prophylactically to the subject, e.g., before the subject is infected or diagnosed with a coronavirus infection, or prior to the development of one or more clinical symptoms, or administered to a subject that is free of infection or has not been suspected of being infected with a coronavirus. In some embodiments, the compositions of the disclosure may be administered therapeutically to the subject, e.g., after the subject is infected or diagnosed with a coronavirus infection, or after symptoms appear, or for treatment of an existing infection or symptom. For example, in some embodiments, the compositions may be therapeutically or prophylactically administered to a subject who is suspected of being infected with a coronavirus. In some embodiments, the subject has been diagnosed of having a coronavirus infection. In some embodiments, the compositions of the disclosure may be therapeutically or prophylactically administered to a subject who is at risk of having a coronavirus infection. In some embodiments, the subject has been infected with a coronavirus. In some embodiments, the subject has been vaccinated. In some embodiments, the subject has been recovered from a coronavirus infection. In some embodiments, the subject is an immunocompromised subject or has been previously treated for coronavirus infection. In some embodiments, the subject is a mammalian subject. In some embodiments, the mammalian subject is a human subject. [0276] In some embodiments, the subject is about 5 years old or younger. For example, the subject may be between the ages of about 1 year and about 5 years (e.g., about 1, 2, 3, 4 or 5 years), or between the ages of about 6 months and about 1 year (e.g., about 6, 7, 8, 9, 10, 11 or 12 months). In some embodiments, the subject is about 12 months or younger (e.g., 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2 months or 1 month). In some embodiments, the subject is about 6 months or younger. [0277] In some embodiments, the subject was born full term (e.g., about 37-42 weeks). In some embodiments, the subject was born prematurely, for example, at about 36 weeks of gestation or earlier (e.g., about 36, 35, 34, 33, 32, 31, 30, 29, 28, 27, 26 or 25 weeks). For example, the subject may have been born at about 32 weeks of gestation or earlier. In some embodiments, the subject was born prematurely between about 32 weeks and about 36 weeks of gestation. In such subjects, the compositions of the disclosure may be therapeutically or prophylactically administered later in life, for example, at the age of about 6 months to about 5 years, or older. [0278] In some embodiments, the subject is pregnant (e.g., in the first, second or third trimester) when administered a composition as disclosed herein. In some embodiments, the subject is a young adult between the ages of about 20 years and about 50 years (e.g., about 20, 25, 30, 35, 40, 45 or 50 years old). In some embodiments, the subject is an elderly subject about 60 years old, about 70 years old or older (e.g., about 60, 65, 70, 75, 80, 85 or 90 years old). [0279] In some embodiments of the methods disclosed herein, the composition is therapeutically or prophylactically administered at a total dose of about 0.0001 mg/kg to about 40 mg/kg, such as, from about 0.0001 mg/kg to about 100 mg/kg, from about 0.01 mg/kg to about 50 mg/kg, from about 0.1 mg/kg to about 40 mg/kg, from about 0.5 mg/kg to about 30 mg/kg, from about 0.01 mg/kg to about 10 mg/kg, from about 0.1 mg/kg to about 10 mg/kg, or from about 1 mg/kg to about 25 mg/kg, of subject body weight per day, one or more times a day, to obtain the desired therapeutic, diagnostic or prophylactic effect. In some embodiments, the desired dosage may be delivered three times a day, two times a day, once a day, every other day, every third day, every week, every two weeks, every three weeks, or every four weeks. [0280] In some embodiments, the total dose may be therapeutically or prophylactically administered using multiple administrations (e.g., two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, or more administrations). When multiple administrations are employed, split dosing regimens may be used. One skilled in the art will understand that a “split dose” is the division of single unit dose or total daily dose into two or more doses. A “single unit dose” is a dose of any therapeutic administered in one dose/at one time/single route/single point of contact, e.g., single administration event. As used herein, a “total daily dose” is an amount given or prescribed in 24-hour period. It may be administered as a single unit dose. In some embodiments, the multiple administrations occur on a schedule according to any one of the following: three times a day, twice a day, once a day, every other day, every third day, weekly, biweekly, every three weeks, every four weeks, and monthly. In some embodiments, the composition is administered by intravenous, intramuscular, subcutaneous, and/or local administration. [0281] In some embodiments, the administered composition reduces binding of the CoV-S protein to and/or reduces coronavirus entry into a cell of the subject. In some embodiments, the administered composition neutralizes against the coronavirus. [0282] In some embodiments, the administered composition treats, prevents, or ameliorates a heath condition associate with a coronavirus infection in the subject. In some embodiments, the treatment methods of the disclosure include reducing or eliminating the incidence of viral infection, or lowering or depleting the viral load. For example, the treatment methods of the disclosure may reduce a symptom of a condition characterized by a viral infection, including, but not limited to, decreasing viral load, by, e.g., at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% at least 95%, or at least 100% in the subject as compared to a reference subject who has not been administered with the composition. In some embodiments, the viral load in the subject is reduced by 5% or greater, 10% or greater, 20% or greater, 30% or greater, 40% or greater, 50% or greater, or 75% or greater relative to the viral load in a reference subject that has not been administered with the composition. In some embodiments, the viral load in the subject is reduced by at least 0.5 log unit, at least 1 log unit, at least 2 log units, at least 3 log units, at least 4 log units, at least 10 log units, at least 15 log units, or by at least 20 log units relative to the viral load in a reference subject that has not been administered with the composition. Those of skill in the art will know the appropriate symptoms or indicators associated with a specific type of ailment and will know how to determine if an individual is a candidate for treatment as disclosed herein. [0283] In some embodiments, the treatment methods involve therapeutically or prophylactically administering an antigen-binding molecule or antigen-binding fragment and/or an LNP composition of the present disclosure (e.g., of Table 1A or Table 1B), to a subject having one or more signs or symptoms of a disease or infection, e.g., viral infection, for which the antigen-binding polypeptide is effective when administered to the subject at an effective or therapeutically effective amount or dose. An effective or therapeutically effective dose of antigen-binding molecule or antigen-binding fragment and/or LNP composition, for treating or preventing a viral infection refers to the amount of the antibody or fragment sufficient to alleviate one or more signs and/or symptoms of the infection in the treated subject, whether by inducing the regression or elimination of such signs and/or symptoms or by inhibiting the progression of such signs and/or symptoms. Health conditions and symptoms associated with SARS-CoV-2 infection include respiratory tract infections, often in the lower respiratory tract. Accordingly, some embodiments of the disclosure relate to methods of for reducing one or more signs or symptoms associated with coronavirus infection, such as high fever, dry cough, shortness of breath, pneumonia, gastro-intestinal symptoms such as diarrhea, organ failure (kidney failure and renal dysfunction), septic shock, and death in severe cases. In some embodiments, a sign or symptom of a coronavirus infection in a subject is survival or proliferation of virus in the body of the subject, e.g., as determined by viral titer assay (e.g., coronavirus propagation in embryonated chicken eggs or coronavirus spike protein assay). Other signs and symptoms of viral infection include, but are not limited to fever or feeling feverish/chills, cough, sore throat, runny or stuffy nose, sneezing, muscle or body aches, headaches, fatigue (tiredness), vomiting, diarrhea, respiratory tract infection, chest discomfort, shortness of breath, bronchitis, and pneumonia [0284] In some embodiments, a therapeutically effective amount of an antigen-binding molecule or antigen-binding fragment and/or an LNP composition disclosed herein reduces the incidence of viral infection by, e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 100%. In some embodiments, a therapeutically effective amount of an antigen-binding molecule or antigen-binding fragment and/or an LNP composition herein reduces the incidence of viral infection by, e.g., at most 10%, at most 15%, at most 20%, at most 25%, at most 30%, at most 35%, at most 40%, at most 45%, at most 50%, at most 55%, at most 60%, at most 65%, at most 70%, at most 75%, at most 80%, at most 85%, at most 90%, at most 95% or at most 100%. In yet other aspects of this embodiment, a therapeutically effective amount of a therapeutic disclosed herein reduces the incidence of viral infection by, e.g., about 10% to about 100%, about 10% to about 90%, about 10% to about 80%, about 10% to about 70%, about 10% to about 60%, about 10% to about 50%, about 10% to about 40%, about 20% to about 100%, about 20% to about 90%, about 20% to about 80%, about 20% to about 20%, about 20% to about 60%, about 20% to about 50%, about 20% to about 40%, about 30% to about 100%, about 30% to about 90%, about 30% to about 80%, about 30% to about 70%, about 30% to about 60%, or about 30% to about 50%. Combination therapies [0285] As discussed above, according to some specific examples, the methods of the disclosure include therapeutically or prophylactically administering to a subject one or more additional agents in combination with an antigen-binding molecule or antigen-binding fragment and/or an LNP composition as described herein. In some embodiments, the antigen-binding molecule or antigen-binding fragment and/or an LNP composition may be used or administered in combination with one or more other therapeutic, prophylactic, diagnostic, or imaging agents. By “in combination with,” it is not intended to imply that the agents must be administered at the same time and/or formulated for delivery together, although these methods of delivery are within the scope of the present disclosure. Compositions can be administered concurrently with, prior to, or subsequent to, one or more other desired therapeutics or medical procedures. In general, each agent will be administered at a dose and/or on a time schedule determined for that agent. [0286] For example, when antigen-binding molecule or antigen-binding fragment and/or the LNP composition of the disclosure is administered “before,” the additional agent can be administered for about 72 hours, about 60 hours, or about 48 hours, to the pharmaceutical composition containing the anti-CoV-S antibody or antigen-binding fragment thereof. About 36 hours, about 24 hours, about 12 hours, about 10 hours, about 8 hours, about 6 hours, about 4 hours, about 2 hours, about 1 hour, about 30 minutes, about 15 minutes, or about 10 minutes before. When the antigen-binding molecule or antigen-binding fragment and/or the LNP composition of the disclosure is administered “after”, the additional therapy can be administered for about 10 minutes, about 15 minutes, about 30 minutes, about 1 hour, about 2 hours, about 4 hours, about 6 hours, about 8 hours, about 10 hours, about 12 hours, about 24 hours, about 36 hours, about 48 hours, about 60 hours, or about 72 hours after. [0287] In some embodiments, the present disclosure encompasses the delivery of pharmaceutical, prophylactic, diagnostic, or imaging compositions in combination with agents that may improve their bioavailability, reduce and/or modify their metabolism, inhibit their excretion, and/or modify their distribution within the body. [0288] It will further be appreciated that therapeutically, prophylactically, diagnostically, or imaging active agents utilized in combination may be administered together in a single composition or administered separately in different compositions. In general, it is expected that agents utilized in combination with be utilized at levels that do not exceed the levels at which they are utilized individually. In some embodiments, the levels utilized in combination will be lower than those utilized individually. In one embodiment, the combinations, each or together may be administered according to appropriate split dosing regimens. [0289] The particular combination of therapies (therapeutics or procedures) to employ in a combination regimen will take into account compatibility of the desired therapeutics and/or procedures and the desired therapeutic effect to be achieved. It will also be appreciated that the therapies employed may achieve a desired effect for the same disorder (for example, a composition useful for treating cancer in accordance with the invention may be administered concurrently with a chemotherapeutic agent), or they may achieve different effects (e.g., control of any adverse effects). [0290] The combination therapy may include an antigen-binding molecule or antigen- binding fragment and/or an LNP composition of the disclosure and any additional therapeutic agent that can be advantageously combined with an anti-CoV-S antibody or antigen-binding fragment of the disclosure. [0291] For example, an additional therapeutic agent may be used to help reduce viral load in the lungs, such as an antiviral agent (e.g., ribavirin). Antibodies can also be used in combination with other therapies as described above, including vaccines specific to CoV, secondary antibodies specific to CoV, antiviral agents, anti-inflammatory agents, antibodies specifically binds the serine protease TMPRSS2 of a target cell, and additional antibodies or antigen-binding fragment thereof that specifically bind to CoV-S protein. In some embodiments, the additional therapeutic agent include an antibody approved by FDA for treatment of coronavirus infection such as, for example, Remdesivir, Baricitinib, Azithromycin, Nirmatrelvir, Ritonavir, Molnupiravir, Casirivimab, Imdevimab, Bamlanivimab, Etesevimab, Sotrovimab, Cilgavimab, Bebtelovimab, Tocilizumab, and Tixagevimab. Accordingly, in some embodiments, the additional therapeutic agent may be any one of Remdesivir, Baricitinib, Azithromycin, Nirmatrelvir, Ritonavir, Molnupiravir, Casirivimab, Imdevimab, Bamlanivimab, Etesevimab, Sotrovimab, Cilgavimab, Bebtelovimab, Tocilizumab, Tixagevimab, or a combination thereof. In some embodiments, the additional therapeutic agent includes an antibody and/or small molecule entity having affinity for an immune pathway target. [0292] In some embodiments, the methods disclosed herein include administering (e.g., therapeutically or prophylactically) to a subject a first agent which is, comprises, or encodes a first antibody or antigen-binding fragment belonging to bin 1 or bin 2 described in Example 14, and a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 3, bin 4, or bin 3/4 described in Example 14. In some embodiments, the first agent is, comprises, or encodes a first antibody or antigen-binding fragment belonging to bin 1 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 3, bin 4, or bin 3/4 described in Example 14. In some embodiments, the first agent is, comprises, or encodes a first antibody or antigen-binding fragment belonging to bin 2 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen- binding fragment belonging to bin 3, bin 4, or bin 3/4 described in Example 14. In some embodiments, the first agent is, comprises, or encodes a first antibody or antigen-binding fragment belonging to bin 3 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 4 described in Example 14. In some embodiments, the first agent is, comprises, or encodes a first antibody or antigen- binding fragment belonging to bin 3 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 3/4 described in Example 14. In some embodiments, the first agent is, comprises, encodes a first antibody or antigen-binding fragment belonging to bin 4 described in Example 14, and the second agent is, comprises, or encodes a second antibody or antigen-binding fragment belonging to bin 3/4 described in Example 14. [0293] As described above, several antibodies described herein are pan-coronavirus antibodies that bind with high affinity to the NTD of SARS-CoV-2 S protein and to a spike protein of one or more SARS-CoV variants (e.g.., beta, gamma, kappa, and omicron), endemic human coronaviruses (HCoVs), and variants of thereof (e.g., HCoV-229E, HCoV-OC43, and HCoV-HKU1). These broad and potently neutralizing NTD-targeting antibodies could be particularly useful in therapeutic combination against SARS-CoV-2 and other coronaviruses and in combination with RBD-binding or non-S1 binding therapeutic antibodies. [0294] In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing NTD-targeting antibody, and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing antibody that does not target the NTD. In some embodiments, the second agent is or comprises a neutralizing RBD-targeting antibody. In some embodiments, the neutralizing NTD-targeting antibody is TXG-0060, TXG- 0066, TXG-0071, TXG-0076, TXG-0078, TXG-0079, TXG-0099, TXG-0104, TXG-0116, TXG-0119, TXG-0131, TXG-0132, TXG-0137, TXG-0162, TXG-0163, TXG-0164, TXG-0168, TXG-0170, TXG-0173, TXG-0174, TXG-0184 , TXG-0136, or an antigen-binding fragment of any thereof (see, e.g., Tables 6 and 9); and the neutralizing antibody that does not bind the NTD is TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG- 0057, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0093, TXG-0094, TXG-0100, TXG-0109, TXG-0115, TXG-0120, TXG-0126, TXG-0129, TXG-0140, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0183, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG- 0201, TXG-0202, TXG-0204, TXG-0210, or an antigen-binding fragment of any thereof (see, e.g., Table 12). [0295] In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing (e.g., has an IC50 of 1000 ng/ml or less) NTD-targeting antibody, and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing RBD antibody. In some embodiments, the potently neutralizing NTD-targeting antibody is TXG-0066, TXG-0076, TXG-0078, TXG-0099, TXG-0104, TXG- 0170, TXG-0173, and TXG-0174, or an antigen-binding fragment of any thereof; and the potently neutralizing RBD antibody is TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG- 0006, TXG-0008, TXG-0009, TXG-0057, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0093, TXG-0094, TXG-0100, TXG-0109, TXG-0115, TXG-0120, TXG-0126, TXG-0129, TXG-0140, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0180, , TXG-0183, TXG- 0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, TXG-0210, or an antigen-binding fragment of any thereof (see, e.g., Table 12). [0296] In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs). In some embodiments, the neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs) TXG-0072, TXG-0078, TXG-0099, TXG-0174, or an antigen- binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs) is TXG- 0006, TXG-0049, TXG-0057, TXG-0070, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0109, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0180, TXG-0183, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, TXG-0210, or an antigen-binding fragment of any thereof. [0297] In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs). In some embodiments, the neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs) is TXG- 0072, TXG-0078, TXG-0099, TXG-0174, or an antigen-binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0091, TXG-0006, TXG-0154, or an antigen-binding fragment of any thereof. [0298] In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs). In some embodiments, the potently neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs) is TXG-0078, TXG-0099, TXG-0174, or an antigen-binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0006, TXG-0091, TXG-0154, or an antigen-binding fragment of any thereof. [0299] In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for the omicron variant of SARS-CoV-2 and at least one endemic human coronaviruses (HCoVs). In some embodiments, the potently neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS- CoV-2 or at least one endemic human coronaviruses (HCoVs) is TXG-0078, TXG-0099, TXG- 0174, or an antigen-binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for the omicron variant of SARS-CoV-2 and at least one endemic human coronaviruses (HCoVs) is TXG-0091 or an antigen-binding fragment thereof. [0300] In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a potently neutralizing NTD-targeting antibody with binding affinity for at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs). In some embodiments, the potently neutralizing NTD-targeting antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0078 or an antigen-binding fragment thereof; and the neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0006, TXG-0091, TXG-0154, or an antigen-binding fragment of any thereof. [0301] In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a TXG-0078 or an antigen-binding fragment thereof, and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is or comprises TXG-0091 or an antigen-binding fragment thereof. In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a NTD-targeting antibody with binding affinity for at least one endemic human coronaviruses (HCoVs), and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is, comprises, or encodes a neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs). In some embodiments, the NTD-targeting antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG-0078, TXG-0114, TXG-0136, or an antigen-binding fragment of any thereof; and the neutralizing RBD antibody with binding affinity for at least one endemic human coronaviruses (HCoVs) is TXG- 0091, TXG-0006, TXG-0154, or an antigen-binding fragment of any thereof. [0302] In some embodiments, the methods disclosed herein include administering to a subject (i) a first agent (e.g., therapeutic agent or prophylactic agent) which is or comprises or encodes an antibody being any one of TXG-0078, TXG-0174, or an antigen-binding fragment of any thereof; and (ii) a second agent (e.g., therapeutic agent or prophylactic agent) which is or comprises or encodes an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG- 0005, TXG-0006, TXG-0008, TXG-0009, TXG-0081, TXG-0115, TXG-0154, or TXG-0180, or an antigen-binding fragment of any thereof. [0303] As noted above, in some embodiments of the disclosure, the subject may be a non- human animal, and the antigen-binding polypeptides (e.g., antibodies and antigen-binding fragments) discussed herein may be used in a veterinary context to treat and/or prevent disease associated with coronavirus in the non-human animals (e.g., cats, dogs, pigs, cows, horses, goats, rabbits, sheep, etc.). Methods of detection [0304] As discussed above, one aspect of the present disclosure relates to methods for detecting the presence of SARS-CoV-2 S protein and/or SARS-CoV-2 in a biological sample for, for example, diagnosing, monitoring, or imaging a virus or a disease, a disorder, and/or a health condition. In some embodiments, the antigen-binding molecule or antigen-binding fragment includes the HCDR1, HCDR2, and HCDR3 of an antibody of Table 1A or Table 1B. In some embodiments, the antigen-binding molecule or antigen-binding fragment includes the LCDR1, LCDR2, and LCDR3 of an antibody of Table 1A or Table 1B. In some embodiments, the antigen-binding molecule or antigen-binding fragment includes all six CDRs from an antibody of Table 1A or Table 1B. In some embodiments, the antigen-binding molecule or antigen-binding fragment includes all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, and wherein the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic human coronaviruses (HCoVs) being any one of 229E, OC43, and HKU1, or a combination thereof. In some embodiments, the antigen-binding molecule or antigen-binding fragment thereof includes all six complementary determining regions (CDRs) from an antibody being any one of TXG- 0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203; and optionally wherein the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic human coronaviruses (HCoVs) that is any one of 229E, OC43, HKU1, or a combination thereof. [0305] In another aspect, provided herein are methods for detecting the presence of SARS- CoV-2 S protein and/or SARS-CoV-2 in a biological sample, wherein the methods include contacting a biological sample with an antigen-binding molecule having an amino acid sequence being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG- 0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, or an antigen-binding fragment of any thereof, wherein optionally the antigen-binding molecule or antigen-binding fragment has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof. [0306] Non-limiting exemplary embodiments of the detection methods as described herein can include one or more of the following features. In some embodiments, the biological sample is from a subject suspected of being infected with a coronavirus. In some embodiments, the subject has been diagnosed of having a coronavirus infection. In some embodiments, the subject is at risk of having a coronavirus infection. In some embodiments, the subject has been infected with a coronavirus. In some embodiments, the subject has been vaccinated. In some embodiments, the subject has been recovered from a coronavirus infection. In some embodiments, the methods further include detecting a complex formed between the antigen- binding molecule or antigen-binding fragment with an SARS-CoV-2 S antigen. In some embodiments, said detecting includes visualizing the formed complex using one or more suitable assays and techniques. Non-limiting examples of assays and techniques suitable for the methods disclosed herein include one or more detection reagents such as an enzyme, a secondary antibody, a colored dye, a fluorescent dye, a chemiluminescent molecule, a molecule containing a radioactive atom, and/or a molecule containing a heavy metal. [0307] In another aspect, provided herein are methods for aiding in the diagnosis, prognosis, monitoring, and/or evaluation of coronavirus infection and/or treatment thereof in a subject, wherein said aiding includes providing: (a) an antigen-binding molecule having an amino acid sequence being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG- 0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, or an antigen-binding fragment of any thereof, and wherein optionally the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof. K^ITS [0308] Further provided herein are kits for the practice of a method described herein, including methods for preventing, treating, diagnosing, prognosing, monitoring, or imaging a virus (e.g., a coronavirus), a disease, a disorder, and/or a health condition. In some embodiments, provided herein are kits for aiding in the prevention, treatment, diagnosis, prognosis, monitoring, or imaging a virus (e.g., a coronavirus), a disease, a disorder, and/or a health condition. In some embodiments, provided herein are kits for use in detecting the presence of SARS-CoV-2 S protein and/or SARS-CoV-2 in a biological sample. In some embodiments, the kits of the disclosure can include one or more antigen-binding molecules or antigen-binding fragments as disclosed herein. [0309] Also provided, in some embodiments of the disclosure, are kits for use in (i) inducing an immune response in a subject, (ii) reducing binding of a spike protein of a coronavirus (CoV-S) to a cell in a subject and/or reducing entry of the coronavirus into a cell of a subject, or (iii) treating, preventing, or ameliorating a health condition associated with SARS- CoV-2 infection in a subject. In some embodiments, the kits of the disclosure can include one or more antigen-binding molecules or antigen-binding fragments as disclosed herein. [0310] In some embodiments, the subject is suspected of being infected with a coronavirus. In some embodiments, the subject has been diagnosed of having a coronavirus infection. In some embodiments, the subject is at risk of having a coronavirus infection. In some embodiments, the subject has been infected with a coronavirus. In some embodiments, the subject has been vaccinated. In some embodiments, the subject has been recovered from a coronavirus infection. [0311] A kit can include instructions for use thereof and one or more of the antibodies or antigen-binding fragments thereof, nucleic acids, and compositions as described and provided herein. For example, some embodiments of the disclosure provide kits that include one or more of the antibodies described herein and/or antigen-binding fragments thereof, and instructions for use. In some embodiments, provided herein are kits that include one or more nucleic acids as described herein and instructions for use thereof. In some embodiments, provided herein are kits that include one or more compositions as described herein and instructions for use thereof. [0312] In some embodiments, the components of a kit can be in separate containers. In some other embodiments, the components of a kit can be combined in a single container. Accordingly, in some embodiments of the disclosure, the kit includes an anti-CoV-S antigen- binding polypeptide, e.g., an antibody or antigen-binding fragment thereof as described herein (e.g., those identified as such in the Sequence Listing), or a pharmaceutical composition thereof in one container (e.g., in a sterile glass or plastic vial, a chromatography column, hollow bore needle, or a syringe cylinder) and a further therapeutic agent in another container (e.g., in a sterile glass or plastic vial, a chromatography column, hollow bore needle, or a syringe cylinder). [0313] If the kit includes a pharmaceutical composition for parenteral administration to a subject, the kit can include a device (e.g., an injection device or catheter) for performing such administration. For example, the kit can include one or more hypodermic needles or other injection devices as discussed above containing the compositions of the present disclosure (e.g., identified as such in the Sequence Listing). [0314] In some embodiments, a kit can further include instructions for using the components of the kit to practice a method described herein. For example, the kit can include a package insert including information concerning the pharmaceutical compositions and dosage forms in the kit. Generally, such information aids patients and physicians in using the enclosed pharmaceutical compositions and dosage forms effectively and safely. For example, the following information regarding a combination of the disclosure may be supplied in the insert: pharmacokinetics, pharmacodynamics, clinical studies, efficacy parameters, indications and usage, contraindications, warnings, precautions, adverse reactions, overdosage, proper dosage and administration, how supplied, proper storage conditions, references, manufacturer/distributor information and intellectual property information. [0315] The instructions for practicing the method are generally recorded on a suitable recording medium. For example, the instructions can be printed on a substrate, such as paper or plastic, etc. The instructions can be present in the kit as a package insert, in the labeling of the container of the kit or components thereof (e.g., associated with the packaging or sub- packaging), etc. The instructions can be present as an electronic storage data file present on a suitable computer readable storage medium, e.g. CD-ROM, diskette, flash drive, etc. In some instances, the actual instructions are not present in the kit, but means for obtaining the instructions from a remote source (e.g., via the internet), can be provided. An example of this embodiment is a kit that includes a web address where the instructions can be viewed and/or from which the instructions can be downloaded. As with the instructions, this means for obtaining the instructions can be recorded on a suitable substrate. [0316] All publications and patent applications mentioned in this disclosure are herein incorporated by reference to the same extent as if each individual publication or patent application was specifically and individually indicated to be incorporated by reference. [0317] No admission is made that any reference cited herein constitutes prior art. The discussion of the references states what their authors assert, and the Applicant reserves the right to challenge the accuracy and pertinence of the cited documents. It will be clearly understood that, although a number of information sources, including scientific journal articles, patent documents, and textbooks, are referred to herein; this reference does not constitute an admission that any of these documents forms part of the common general knowledge in the art. [0318] The discussion of the general methods given herein is intended for illustrative purposes only. Other alternative methods and alternatives will be apparent to those of skill in the art upon review of this disclosure, and are to be included within the spirit and purview of this application. [0319] In another aspect, provided herein are methods of manufacturing a pharmaceutical composition, the methods including: (a) admixing a lipid solution with an aqueous buffer solution including a buffer agent thereby forming a lipid nanoparticle solution including a lipid nanoparticle (LNP); and (b) adding to the lipid nanoparticle: (i) an antigen-binding molecule, or an antigen-binding fragment include any thereof, including all 6 CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, wherein optionally the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof; and/or (ii) a nucleic acid encoding the antigen-binding molecule or antigen- binding fragment thereof of (a), thereby forming a LNP formulation including the LNP associated with the antigen-binding molecule or antigen-binding fragment thereof, and/or with the nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof. EXAMPLES [0320] The practice of the present invention will employ, unless otherwise indicated, conventional techniques of molecular biology, microbiology, cell biology, biochemistry, nucleic acid chemistry, and immunology, which are well known to those skilled in the art. Such techniques are explained fully in the literature, such as Sambrook, J., & Russell, D. W. (2012). Molecular Cloning: A Laboratory Manual (4th ed.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory and Sambrook, J., & Russel, D. W. (2001). Molecular Cloning: A Laboratory Manual (3rd ed.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory (jointly referred to herein as “Sambrook”); Ausubel, F. M. (1987). Current Protocols in Molecular Biology. New York, NY: Wiley (including supplements through 2014); Bollag, D. M. et al. (1996). Protein Methods. New York, NY: Wiley-Liss; Huang, L. et al. (2005). Nonviral Vectors for Gene Therapy. San Diego: Academic Press; Kaplitt, M. G. et al. (1995). Viral Vectors: Gene Therapy and Neuroscience Applications. San Diego, CA: Academic Press; Lefkovits, I. (1997). The Immunology Methods Manual: The Comprehensive Sourcebook of Techniques. San Diego, CA: Academic Press; Doyle, A. et al. (1998). Cell and Tissue Culture: Laboratory Procedures in Biotechnology. New York, NY: Wiley; Mullis, K. B., Ferré, F. & Gibbs, R. (1994). PCR: The Polymerase Chain Reaction. Boston: Birkhauser Publisher; Greenfield, E. A. (2014). Antibodies: A Laboratory Manual (2nd ed.). New York, NY: Cold Spring Harbor Laboratory Press; Beaucage, S. L. et al. (2000). Current Protocols in Nucleic Acid Chemistry. New York, NY: Wiley, (including supplements through 2014); and Makrides, S. C. (2003). Gene Transfer and Expression in Mammalian Cells. Amsterdam, NL: Elsevier Sciences B.V., the disclosures of which are incorporated herein by reference. [0321] Additional embodiments are disclosed in further detail in the following examples, which are provided by way of illustration and are not in any way intended to limit the scope of this disclosure or the claims. EXAMPLE 1 Biological samples [0322] Sample procurement: The experiments described in the below Examples were performed with peripheral blood mononuclear cells (PBMCs) collected from convalescent human survivors of natural infection with SARS-2. Specifically, Donor 531 PBMCs were purchased from Cellero (~112m/vial product, Cat. # 1146-4785JY20) and used in these experiments. [0323] Sample background/timeline: The donor tested positive via nasopharyngeal swab while presenting asymptomatic/presymptomatic on Day 0. Hospitalization was not required. The donor tested negative for SARS-2 on Day 23. Plasma and apheresis sample collection were performed on Day 104. The donor is also seropositive for cytomegalovirus, a ubiquitous human herpesvirus. EXAMPLE 2 Enrichment of B cells [0324] A vial of frozen PBMCs was thawed for 1-2 min in a water bath, then transferred into 8-10 mL of 10% Fetal Bovine Serum (FBS) in PBS, and centrifuged for 5 min at 350g. The cell pellet was washed three times by resuspending in 0.04% Bovine Serum Albumin (BSA) in PBS and centrifuging at RT at 350g for 5 min each wash, with the final pellet resuspended to a concentration of ~20 million cells per mL in a total volume of 5 mL (~100 million cells total). B cells were enriched using the B Cell Isolation Kit II (human; MACS™ Miltenyi) according to manufacturer’s instructions, and approximately 50 million cells were applied to each of two LS columns designed for positive selection of cells. The effluent was concentrated and prepared for cell labeling. EXAMPLE 3 Antigen sourcing, preparation, and conjugation [0325] Biotinylated antigens were sourced from suppliers as follows: [0326] 1) Biotinylated trimerized S (SARS-2) was sourced from ACRO Biosystems, catalog # SPN-C82E9-25 (https://www.acrobiosystems.com/P3345-Biotinylated-SARS-CoV-2- S-protein-HisAvitag™-Superstable-trimer-%28MALS-verified%29.html). This protein carries a polyhistidine tag at the C-terminus, followed by an Avi tag. Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin. [0327] 2) Biotinylated trimerized S D614G (SARS-2), from ACRO Biosystems, catalog # SPN-C82E3-25 (https://www.acrobiosystems.com/P3431-Biotinylated-SARS-CoV-2-S- protein-%28D614G%29-HisAvitag™-Super-stable-trimer-%28MALS-verified%29.html). This protein contains D614G mutation, which has become increasingly common in SARS-CoV-2 viruses from around the world. This protein also carries a polyhistidine tag at the C-terminus, followed by an Avi tag. Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin. [0328] 3) Biotinylated Human Serum Albumin (HSA) HSA-H82E3, from Sapphire (https://sapphireusa.com/product.jsp?q=ns%3ANS0000368507). [0329] Biotinylated antigens were each solubilized per manufacturer’s instructions. In each case, they were thawed and dissolved in sterile deionized water for 30-60 minutes at room temperature with occasional gentle mixing for a final concentration of 100 microgram/mL (for HSA) or 200 microgram/mL for both of the trimerized S antigens. [0330] Solubilized antigens were each conjugated with, e.g., allowed to form a complex with (or bind to) one of the following TotalSeqC reagents, supplied by BioLegend, which each contain a unique barcoded DNA oligonucleotide supplied by the vendor as follows: [0331] 1) TotalSeq-C0951 PE Streptavidin was conjugated to biotinylated trimerized S glycoprotein (SARS-2). [0332] 2) TotalSeq-C0952 PE Streptavidin was conjugated to biotinylated human serum albumin. [0333] 3) TotalSeq-C0956 APC Streptavidin was conjugated to biotinylated trimerized S D614G glycoprotein (SARS-2). [0334] 4) TotalSeq-C0957 APC Streptavidin with biotinylated human serum albumin. Briefly, each TotalSeq-C barcoded streptavidin PE or APC reagent was diluted to 0.1 mg/mL and then mixed with biotinylated antigen at a 5X molar excess of antigen to streptavidin, based on a fixed amount of 0.5 μg PE-SA. One fifth of the streptavidin-oligo PE or APC conjugate was added to the antigen every 20 minutes at 4^oC. The reaction was then quenched with 5 μl of 4mM biotin (Pierce, Thermo Fisher) for 30 minutes for a total probe volume of 20 μL. The final conjugated antigen probes (streptavidin-antigen complexes) were then immediately used for cell labeling at a dilution of 1:50. EXAMPLE 4 Cell labeling [0335] This Example describes experiments performed to stain B cells with a number of barcoded antibodies and conjugated antigens. In these experiments, approximately 4.4 million enriched B cells were first resuspended in labeling buffer (1% BSA in PBS) and performed Fc blocking for 10 minutes on ice using Human TruStain FcX (BioLegend). [0336] Next, cells were stained with the following cocktail of antibodies, antigens and dyes: CD19 PE-Cy7 (clone SJ25C1, BD Pharmingen) for discrimination of CD19+ cells by using fluorescence-activated cell sorting (FACS). [0337] Barcoded Antibodies for 10x Single Cell Immune profiling, which included the following TotalSeq-C oligo barcoded antibodies: [0338] - TotalSeq-C0389 anti-human CD38. [0339] - TotalSeq-C0154 anti-human CD27. [0340] - TotalSeq-C0189 anti-human CD24. [0341] - TotalSeq-C0384 anti-human IgD. [0342] - TotalSeq-C0100 anti-human CD20. [0343] - TotalSeq-C0050 anti-human CD19 (clone HIB19, to distinguish it from the flow clone). [0344] - TotalSeq-C0049 anti-human CD3E. [0345] - TotalSeq-C0045 anti-human CD4. [0346] - TotalSeq-C0046 anti-human CD8A. [0347] - TotalSeq-C0051 anti-human CD14. [0348] - TotalSeq-C0083 anti-human CD16. [0349] - TotalSeq-C0090 mouse IgG1 K isotype control. [0350] - TotalSeq-C0091 mouse IgG2a K isotype control. [0351] - TotalSeq-C0092 mouse IgG2b K isotype control. [0352] Final conjugated antigens: [0353] - TotalSeq-C0951 PE trimerized S (SARS-2). [0354] - TotalSeq-C0952 PE Human Serum Albumin. [0355] - TotalSeq-C0956 APC trimerized S D614G (SARS-2). [0356] - TotalSeq-C0957 APC Human Serum Albumin. [0357] - 7AAD for live/dead cell discrimination. [0358] Cells were stained in labeling buffer (1% BSA in PBS) in the dark for 30 minutes on ice, then cells were washed 3 times with 2 mL of cold labeling buffer at 350*g for 5 minutes at 4^oC, resuspended in cold labeling buffer and a 1:200 addition of live/dead cell discriminating agent 7AAD for 10 minutes on ice in the dark, then washed one more time with labeling buffer at 350*g for 5 minutes at 4C, then resuspended in labeling buffer and loaded into a Sony MA900 Cell Sorter using a 70 µm sorting chip. EXAMPLE 5 Antigen-specific enrichment via FACS [0359] Cells were initially gated on being single, live (7AAD^negative) and PE-Cy7-CD19+ and then sorted on their PE and/or APC status directly into master mixed and water based on one of four criteria: [0360] 1) PE+, representing trimerized S (SARS-2) antigen+ and/or HSA+ control antigen cells (gate Q1 in FIG.1; 2,430 cells); [0361] 2) APC+, representing trimerized S D614G (SARS-2) antigen and/or HSA control antigen cells (gate Q3 in FIG.1; 728 cells); [0362] 3) Dual PE+ and APC+, representing a combination of trimerized S (SARS-2) antigen+, trimerized S D614G (SARS-2) antigen+ and/or HSA control antigen-positive cells (gate Q2 in FIG.1; 828 cells); [0363] 4) PE and APC negative cells, representing cells not binding either SARS-2 antigen or control HSA antigen (gate Q4 in FIG.1; 5,000 cells). [0364] In FIG.1, the Y axis represents PE (representing trimerized S (SARS-2) antigen+ and/or HSA+ control antigen cells) signal. The X axis represents APC trimerized S (SARS-2) D614G antigen+ and/or HSA+ control antigen cells. The numbers adjacent to each gate name represent the fraction of events of the parent population (single, live, CD19+ cells) for that gate. FACS data were analyzed with FlowJo. [0365] The resulting volume was adjusted with additional water to match the recommended volume and target for loading with the 10× 5’V2 Single Cell Immune Profiling kit. FACS data were analyzed using FlowJo. Standard gene expression, V(D)J, and barcoded antigen libraries were constructed using the 10× 5’V2 Single Cell Immune Profiling kit per manufacturer's instructions. Additional information in this regard can be found at “support.10xgenomics.com/permalink/getting-started-immune-profiling-feature-barcoding.” E^XAMPLE 6 Sequencing analysis [0366] The libraries resulting from the experiments described in Example 6 above were sequenced on a NovaSeq 3 using a NovaSeq S4200 cycles 2020 v1.5 kit, targeting using read 28, 10, 10, and 90 cycles targeting 20,000, 30,000, or 6000 reads per cell for gene expression, barcoded antigen, or Ig libraries, respectively. Sequence analysis (described further herein, see, e.g., Example 7) identified a total of 239 antibodies. The binding affinity of 161 exemplary antibodies to a trimerized wild-type SARS-CoV-2 spike protein (FIG.15A and SEQ ID NO: 3045) and a SARS-CoV-2 spike protein variant with D614G substitution (FIG.15B and SEQ ID NO: 3046) is summarized in Tables 3A-3B below. In these experiments, the binding affinity of an antigen-binding molecule (e.g., antibody) to a target antigen (wild-type S protein or a variant thereof) was determined based on quantity/numbers of unique molecular identifiers (UMIs) associated with each of the antigen-binding molecules bound to the target antigen. Generally, the higher target antigen UMI counts were used as a predictor of higher binding affinity. When an antibody was found “fluorophore reactive” or “biotin-reactive” then it was categorized as a non- specific antibody, even if it had non-zero target antigen UMI counts. As shown in Tables 3A-3B below, all of the identified antibodies displayed high target antigen counts and low non-target antigen counts. As such, they were predicted to have specific binding affinity for the target antigen and were distinguishable from non-specific binders. TABLE 3A: Binding affinity of 159 exemplary antibodies. The integer values displayed in the table below represent antigen UMI counts for each of the individual on-target (Wild-type S or D416G mutant (Mutant S)) and off-target (human serum albumin control/HSA 1, human serum albumin control/HSA 2) antigens.

TABLE 3B: Binding affinity of 80 exemplary antibodies. The integer values displayed in the table below represent antigen UMI counts for each of the individual on-target (Wild-type S or D416G mutant (Mutant S) and off-target (human serum albumin control/HSA 1, human serum albumin control/HSA 2) antigens.

[0367] It was observed that the antibodies identified in these experiments were diverse in their VH, VL, and isotype/subclass (see Table 3C below). T^ABLE 3C:

[0368] As demonstrated, BEAM-Ab directly captures full length antibody sequences, enabling rapid expression of the native antibody, including somatic hypermutation. Furthermore, BEAM-Ab is highly reproducible: 220 of 240 screened binders were re-identified in separate samples from the same blood draw. EXAMPLE 7 Statistical analysis [0369] Binding antibodies with a maximum spike antigen count greater than 40 UMIs (as summarized in Table 3 above) were selected for further analysis using 10x Genomics “Enclone” (available at https://bit.ly/enclone), which is a computational tool developed for clonal grouping to study the adaptive immune system. In this computational tool, the 10x Genomics Chromium Single Cell V(D)J data containing B cell receptor (BCR) and T cell receptor (TCR) RNA sequences are provided as input data to Enclone. Based on the input, Enclone finds and organizes cells arising from the same progenitors into groups (e.g., clonotype families) and compactly displays each clonotype along with its salient features, including mutated amino acids. Antibodies in the dataset were classified into 3 categories, as listed below, via a process termed “barcode-enabled antigen mapping by sequencing” (BEAM-seq): [0370] Category 1. (e.g., Fluorophore-reactive): Antibodies are classified into this category if the mix of antigens includes target and non-target antigens linked to different fluorophores, and counts are detected for target and non-target antigen linked to fluorophore 1 but not fluorophore 2, which indicates that the antibodies bind to the fluorophore and not the target antigen. In this particular Example, antibodies were classified into this category if counts were detected for only one spike protein and the corresponding albumin labeled with the same fluorophore. [0371] Category 2. (e.g., Biotin-reactive, streptavidin-reactive, or polyreactive): Antibodies are classified into this category if the mix of antigens includes target and non-target antigens linked to different fluorophores, and counts are detected for target and non-target antigen linked to both fluorophores, which indicates that the antibodies does not bind the antigen but instead binds to a core component of the reagent (e.g., streptavidin, biotin) or is polyreactive (e.g., sticky and non-specific). In this particular Example, antibodies were classified into this category (e.g., classified as biotin-reactive, streptavidin-reactive, or polyreactive, if counts were detected for both spike proteins (trimerized wild-type S and trimerized S D614G) and both albumins (PE-HSA and APC-HSA). [0372] Category 3. (e.g., Candidate SARS-2-reactive antibodies): Antibodies are classified into this category if counts are detected for target antigen but absent or at lower levels for non-target antigen, which indicates that the antibodies specifically binds the target antigen and has affinity for the target antigen. In this particular Example, antibodies were classified into this category (e.g., classified as candidate SARS-2-reactive antibodies, if counts were considerably higher for one or both spike proteins relative to the albumins; most antibodies bound the wild-type spike protein and the common population variant D614G. Category 3 antibodies are disclosed herein (see, e.g., Tables 1A-1B and Table 3). [0373] In a dataset where there is considerable enrichment for genuine antigen-binding cells, the binding affinity of an antigen-binding molecule (e.g., antibody or antigen-binding fragment) to a target antigen (such as S protein) were determined based on a quantity/number of unique molecular identifiers (UMIs) associated with the antigen bound to each cell. BEAM scores are approximately normally distributed, increase exponentially as target antigen-binding relative to expressed antibody and control antigen increases, are correlated with generation probability of the HCDR3 junction, e.g., following the known general relationship of somatic hypermutation (SHM) and increasing affinity, and also reveal that class switching increases predicted relative affinity in concordance with the literature (FIGS.2 and 3). BEAM scores are also generally higher within sublineages that contain more daughter antibodies than narrow sublineages (representative example shown in FIG.4). EXAMPLE 8 Antibody synthesis, cloning, expression, and purification [0374] Variable heavy chain and light chain domains of anti-SARS-CoV-2 antibodies were reformatted to IgG1 and synthesized and cloned into mammalian expression vector pTwist CMV BG WPRE Neo utilizing the Twist Bioscience eCommerce portal. Light chain variable domains were reformatted into kappa and lambda frameworks accordingly. Clonal genes were delivered as purified plasmid DNA ready for transient transfection in human embryonic kidney (HEK) Expi293 cells (Thermo Scientific). Cultures in a volume of 1.2 ml were grown to four days, harvested and purified using Protein A resin (PhyNexus) on the Hamilton Microlab STAR platform into 43 mM Citrate 148 mM HEPES, pH 6. EXAMPLE 9 Further characterization of binding affinity [0375] This Example describes the results of experiments performed to further characterize binding affinity of select antibodies described herein. [0376] Antibodies with high predicted binding affinity based on antigen UMI count profiles were selected for further screening and analysis. Subsequently, surface plasmon resonance (SPR) analyses were performed on the selected antibodies by using a Carterra LSA SPR biosensor equipped with a HC30M chip at 25°C in HBS-TE (10 mM HEPES pH 7.4, 150 mM NaCl, 3 mM EDTA, 0.05% Tween-20). Antibodies were diluted to 5 µg/ml in sodium acetate buffer, pH 4.5, and amine-coupled to the sensor chip by EDC/NHS activation, followed by ethanolamine HCl quenching. Increasing concentrations of ligand were flowed over the sensor chip in HBSTE (10 mM HEPES pH 7.4, 150 mM NaCl, 3 mM EDTA, 0.05% Tween-20) with 0.5 mg/ml BSA with 5 minute association and 15 minute dissociation. Following each injection cycle the surface was regenerated with 2x 30 second injections of IgG elution buffer (Thermo). The following antigens and catalog #s from Acro Biosystems were used for serial analysis at the specified concentration ranges: [0377] (1) SARS-CoV-2 S protein, His Tag, Super stable trimer (MALS & NS-EM verified), SPN-C52H9; 0 - 100 nM. [0378] (2) SARS-CoV-2 S protein (D614G), His Tag, Super stable trimer (MALS verified), SPN-C52H3; 0 - 100 nM. [0379] (3) SARS-CoV-2 (COVID-19) S protein RBD (triple mutant K417N, E484K, N501Y), His Tag (MALS verified), SPD-C52Hp; 0 - 500 nM. [0380] (4) SARS-CoV-2 (COVID-19) S1 protein NTD, His Tag, S1D-C52H6; 0 - 500 nM. [0381] (5) SARS-CoV-2 (COVID-19) S2 protein, His Tag, S2N-C52H5; 0 - 500 nM. [0382] (6) MERS S1 protein, His Tag, S1N-M52H5; 0 - 500 nM. [0383] (7) HCoV-HKU1 (isolate N5) S1 protein, His Tag, SIN-V52H6; 0 - 500 nM. [0384] Traces were analyzed and fit using Carterra's Kinetics Tool software, fit to a 1:1 receptor-ligand binding model. [0385] Table 4 below provides a summary of the binding affinity of the exemplary antibodies to the following antigens: (1) a trimerized wild-type SARS-CoV-2 S protein (FIG. 15A and SEQ ID NO: 3045), (2) a SARS-CoV-2 S protein variant with D614G substitution (FIG.15B and SEQ ID NO: 3046). For comparative analysis, also included in this study were the four following FDA-approved therapeutic antibodies previously reported to bind SARS- CoV-2 S protein: (1) imdevimab (REGN-COV2), (2) bamlanivimab (Eli Lilly / AbCellera), (3) etesevimab (Eli Lilly / AbCellera), and sotrovimab (Vir / GlaxoSmithKline). It was observed that the majority of antibodies tested in this study could bind to both wild-type S protein and D614G mutant in picomolar and nanomolar range. Remarkably, several antibodies described herein were found to have binding affinities as good as or superior to FDA-approved antibodies or antibodies in late clinical development. See also, FIGS.16A-16B and 19. TABLE 4: Binding affinity of exemplary antibodies. CTRL-0005: Imdevimab. CTRL-0006: Bamlanivimab. CTRL-0007: Etesevimab. CTRL-0008: Sotrovimab. ND: not determined.

[0386] Furthermore, as shown in Table 5 below, it was observed that several antibodies described herein demonstrated high binding affinity to a RBD fragment of SARS-CoV-2 S protein with triple amino acid substitutions K417N, E484K, and N501Y. For comparative analysis, also included in this study were two therapeutic antibodies previously reported to bind RBD of SARS-CoV-2 S protein (i.e., etesevimab, and sotrovimab). It was observed that 21 antibodies tested in this study could bind to the triple mutant RBD in low to mid nanomolar range. In addition, several antibodies were found to bind the triple escape variant of RBD with binding affinities as good as or superior to FDA-approved antibodies or antibodies in late clinical development. See also, FIGS.17A-17B. TABLE 5: Binding affinity of exemplary antibodies to a RBD variant of SARS-CoV-2 S protein. Triple mutant RBD tested in this study contained a combination of three amino acid substitutions K417N, E484K, and N501Y. CTRL-0007: Etesevimab. CTRL-0008: Sotrovimab.

[0387] Remarkably, several antibodies (e.g., TXG-0091, TXG-0112, TXG-0136, TXG- 0192, TXG-228, and TXG-0230) were found to be pan-coronavirus antibodies that recognizes a conserved epitope in the S1 subunit and bind with high affinity to the S1 subunit of a new human coronavirus strain HCoV-HKU1. In particular, antibody TXG-0091 was found to be a pan- coronavirus antibody that recognizes a conserved epitope in the S1 subunit and bind with high affinity to the S1 subunit of a new human coronavirus strain HCoV-HKU1 (KD = 543 pM) (see, e.g., Table 6). Accordingly, without being bound to any particular theory, this antibody could be particularly useful in therapeutic combination against SARS-CoV-2 and other coronaviruses and in combination with RBD-binding, NTD-binding, or non-S1 binding therapeutic antibodies. [0388] As shown in Table 6, several antibodies (e.g., TXG-0063, TXG-0072, TXG-0173, TXG-0174, and TXG-0230) were found to bind N-terminal domain of SARS-CoV-2 S protein with high affinity. In particular, antibody TXG-0063 was found to bind N-terminal domain of SARS-CoV-2 S protein with high affinity (KD = 102 nM). Accordingly, this antibody could be particularly useful in therapeutic combination against SARS-2 with RBD-binding and non-S1 binding therapeutic antibodies. TABLE 6: Binding affinity of antibodies TXG-0063, TXG-0072, TXG-0091, TXG-0112, TXG-0136, TXG-0173, TXG-174, TXG-0192, TXG-228, and TXG-0230 to the N-terminal domain of SARS-CoV-2 S protein and/or the S1 subunit of HCoV-HKU1.

EXAMPLE 10 Identification of antibodies with desired kinetic profiles [0389] Further analyses were performed using SPR binding curves to identify antibodies with particularly low K_off constants. As shown in Table 7 below, it was observed that antibodies could be stratified into two major classes: optimal binding kinetics and less optimal binding kinetics. For example, it was found that one could identify antibodies with visibly longer half-lives have a Koff lower than 4e-4, with an additional subclass of antibodies that have exceptionally long half-lives and a Koff lower than 1e-4 (see, e.g., Table 7 and FIGS.18A-18D). Antibody half-life values and mean-life values reported in Table 7 were calculated by using formula ln(2)/Koff and formula 1/Koff, respectively. [0390] A smaller number of antibodies have less optimal binding kinetics due to their higher Koff constants, which produce a less ideal KD even given their acceptable Kon constants (see, e.g., Table 7 and FIGS.18A-18D). For comparative analysis, etesevimab and sotrovimab were also included in this study. TABLE 7: Half-lives of exemplary antibodies. CTRL-0007: Etesevimab. CTRL-0008: Sotrovimab.

E^XAMPLE 11 Functional characterization of antibodies [0391] To further characterize the antibodies and antigen-binding fragments described in Examples 1-10 above, ligand-blocking assays are performed using GFP+ reporter cells expressing ACE2 and dose competition of pre-fusion D614G spike protein in dual-fluorescent format, where the antigens being competed are in tetrameric format. In these experiments, a relative KD value for each mAb can be generated. [0392] In addition, to determine whether the antibodies and antigen-binding fragments of the disclosure have a neutralizing activity (e.g., antagonistic activity) against SARS-CoV-2, e.g., able to bind to and neutralize the activity of SARS-CoV-S, additional live virus or pseudovirus neutralization assays are performed using these mAbs in a dose-dependent manner to generate an IC₅₀ of neutralization activity. In some experiments, a neutralization activity IC₅₀ value for each antibody can be determined in a quantitative focus reduction neutralization test (FRNT) described previously by Zost et al. (Nature, 584:443–449, 2020). In some experiments, neutralization assays are used to determine infectivity of SARS-CoV-2 S protein-containing virus-like particles. In these experiments, a neutralizing or antagonistic CoV-S antibody or antigen-binding fragment can be identified based on its ability to inhibit an activity of CoV-S to any detectable degree, e.g., inhibits or reduces the ability of CoV-S protein to bind to a receptor such as ACE2, to be cleaved by a protease such as TMPRSS2, or to mediate viral entry into a host cell or mediate viral reproduction in a host cell. EXAMPLE 12 Additional surface plasmon resonance (SPR) analysis [0393] This Example describes the results of an additional round of experiments performed to further characterize binding affinity of select antibodies described herein. [0394] A new lot of all 239 antibodies identified in Example 6 were synthesized, cloned, expressed, and purified according to the methods described in Example 8. [0395] A second SPR experiment was performed under the same experimental settings (flow times, antigen concentration, coupling method, buffer, etc.) with one set of measurements per antibody (in comparison to the triplicate measurements completed as part of the first SPR experiment). Trimeric forms of the SARS-CoV-2 Wuhan entry strain (WT), beta, gamma, and kappa pre-fusion spike, SARS-CoV-2 NTD, HcoV-HKU1 spike trimer, and human serum albumin were used as antigens to assess the affinity and reactivity of each antibody. The antigens used in these experiments were purchased from ACROBiosystems (His-tagged wild-type SARS- CoV-2: Cat# SPN-C52H9; His-tagged SARS-CoV-2 gamma variant: Cat# SPN-C52Hg; His- tagged SARS-CoV-2 kappa variant: Cat# SPN-C52Hr; His-tagged SARS-CoV-2 beta variant: Cat# SPN-C52Hk; His-tagged SARS-CoV-2 NTD: Cat# SPN-C52H6; and His-tagged HcoV- HKU1 (isolate N5) spike trimer: Cat# SPN-C52H5). In addition, His-tagged human serum albumin (HSA) was also purchased from ACROBiosystems (Cat# HSA-H5220). Mutations identified in the beta, gamma, and kappa variants are as follows. [0396] Beta variant: L18F, D80A, D215G, 242-244del, R246I, K417N, E484K, N501Y, D614G, A701V. [0397] Gamma variant: L18F, T20N, P26S, D138Y, R190S, K417T, E484K, N501Y, D614G, H655Y, T1027I, and V1176F. [0398] Kappa variant: T95I, G142D, E154K, L452R, E484Q, D614G, P681R, and Q1071H. [0399] It should be noted that the delta and kappa variants share two mutations E484Q and L452R. They were identified in India’s second COVID-19 wave, and have been reported to share significant similarity, presumably due to the fact that they are from the same lineage. [0400] As shown in Tables 8A-8B below, it was observed that several antibodies described herein demonstrated high binding affinity to various spike variants of interest (VoC), e.g., beta, gamma, and kappa variants. For comparative analysis, also included in this study were several control antibodies (denoted as CTRL) that had been previously described as having binding affinity for SARS-CoV-2 S protein. It was observed that several antibodies tested in this experiment could bind to one or more spike variants in low to mid nanomolar range. In addition, several antibodies were found to bind beta, gamma, and/or kappa variants with binding affinities as good as or superior to FDA-approved antibodies or antibodies in late clinical development. TABLES 8A AND 8B: Binding affinity of exemplary antibodies to beta, gamma, and kappa spike variants. A total of 51 control antibodies (CTRL) were included in these experiments, including: CTRL-0004: Casirivimab; CTRL-0005: Imdevimab; CTRL-0006: Bamlanivimab; CTRL-0007: Etesevimab; CTRL-0008: Sotrovimab; and CTRL-0009: Tixagevimab; (-): not determined.

Ant CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT CT

[0401] An UpSet plot was generated (see, e.g., FIG.25) wherein antibodies are binned into antigen bins based on two rounds of SPR binding affinity data. For an antibody to be placed into a bin a detectable kinetic fit at all concentrations of antigen was required from at least one of the SPR experiments described in Examples 9 and 12, or orthogonal neutralization data. The results described in FIG.25 illustrate that the BEAM-seq process described in the present disclosure allows for rapid identification of many antibodies with broad and robust binding affinity against several coronavirus S antigens, including several variants of concern (VoC), e.g., , beta, gamma, and kappa, as well as HKU1 (which is a different coronavirus). [0402] A third SPR experiment was performed under the same experimental settings (flow times, antigen concentration, coupling method, buffer, etc.) where the antibodies were assessed at minimum in duplicate and up to sextuplicate. Trimeric forms of the human coronavirus HCoV-OC43 pre-fusion trimeric spike, HCoV-229E pre-fusion trimeric spike, SARS-CoV-2 omicron pre-fusion trimeric spike and SARS-CoV-2 NTD were used as antigens to assess the affinity and reactivity of each antibody. As shown in Table 9 below, it was observed that several antibodies described herein demonstrated high binding affinity to SARS-CoV-2 omicron spike as well as HCoV-OC43 spike and HCoV-229E spike. For comparative analysis, also included in this study were several control antibodies (denoted as CTRL) that had been previously described as having binding affinity for SARS-CoV-2 S protein. [0403] In these experiments, it was observed that several antibodies tested in this experiment could bind to one or more spike variants in low to mid nanomolar range. In particular, thirty-seven (37) antibodies tested in this SPR experiment were found to exhibit binding affinity for the WT spike and the new SARS-CoV-2 strain omicron (see, e.g., Tables 8-9 and FIG.31). Of these 37 antibodies, at least 32 exhibit affinity for the beta variant, at least 34 exhibit affinity for the kappa variant, and at least 32 exhibit affinity for the gamma variants by SPR. In addition, at least 32 antibodies exhibit high affinity for the beta, gamma, and omicron variants by SPR, and at least antibodies exhibit high affinity for the gamma, kappa, and omicron variants by SPR. Exemplary antibodies exhibiting affinity for the gamma, kappa, and omicron variants include TXG-0057, TXG-0063, TXG-0070, TXG-0072, TXG-0091, TXG-0094, TXG- 0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0174, TXG-0180, TXG-0183, TXG-0187, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0404] Remarkably, at least 30 tested antibodies exhibit affinity for the WT spike and all four beta, gamma, kappa, and omicron variants. Exemplary antibodies exhibiting affinity for the WT spike and all four beta, gamma, kappa, and omicron variants include TXG-0057, TXG-0063, TXG-0070, TXG-0072, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0141, TXG-0144, TXG-0174, TXG-0180, TXG-0183, TXG-0187, TXG-0192, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230. [0405] Furthermore, several antibodies were found to be pan-coronavirus antibodies that bind with high affinity to N-terminal domain of SARS-CoV-2 S protein (NTD) and/or to a spike protein of the new SARS-CoV-2 strain omicron (see, e.g., TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0109, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, and TXG-0230 of Table 9 and FIG.31). Of these antibodies, at least five antibodies were found to have a high affinity to both (i) N-terminal domain of SARS-CoV-2 S protein (NTD) and (ii) a spike protein of the omicron variant. Exemplary antibodies having these binding characteristics include TXG-0072, TXG-0099, TXG-0114, TXG-0203, and TXG-0230. [0406] In addition, several antibodies were found to be promising pan-coronavirus antibodies that bind with affinity to N-terminal domain of SARS-CoV-2 S protein (NTD) and to a spike protein of the endemic human coronavirus HCoV-OC43 (see, e.g., TXG-0048, TXG- 0078, TXG-0114, TXG-0136, TXG-0192, and TXG-0203) or HCoV-229E (e.g., TXG-0078, TXG-0112, TXG-0114, TXG-0136, TXG-0192, TXG-0203, and TXG-0230). [0407] At least 8 antibodies tested in this experiments exhibit binding high affinity for the endemic coronavirus HCoV-229E. Exemplary antibodies with high affinity for HCoV-229E include TXG-0078, TXG-0112, TXG-0114, TXG-0136, TXG-0192, TXG-0203, TXG-0228, and TXG-0230. At least 10 tested antibodies exhibit binding affinity for the endemic coronavirus HCoV-OC43. Exemplary antibodies with affinity for HCoV-OC43 include TXG-0006, TXG- 0048, TXG-0070, TXG-0078, TXG-0100, TXG-0114, TXG-0136, TXG-0154, TXG-0192, and TXG-0203. Of these 10 antibodies, at least five exhibit high affinity for HCoV-OC43 (see, e.g., TXG-0100, TXG-0114, TXG-0136, TXG-0192, and TXG-0203). [0408] In addition, several antibodies were found to bind HCoV-OC43, HCoV-229E, SARS-CoV-2 omicron and SARS-CoV-2 NTD with binding affinities as good as or superior to FDA-approved antibodies or antibodies in late clinical development. Exemplary antibodies having this ultra-broad binding affinity include TXG-0114, TXG-0192, and TXG-0203. In particular, TXG-0114 and TXG-0203 were found to bind HCoV-OC43, HCoV-229E, SARS- CoV-2 omicron and SARS-CoV-2 NTD with high affinities. [0409] Several antibodies were found to exhibit binding affinity for the WT spike, the spike protein of beta, gamma, and kappa variants as well as the endemic coronaviruses HCoV- OC43, HKU1, and HCoV-229E. Exemplary antibodies having this ultra-broad binding affinity include TXG-0078, TXG-0114, TXG-0136, TXG-0192, and TXG-0203. [0410] Remarkably, at least three (3) antibodies tested in this experiment were found to exhibit binding affinity for the WT spike, all four variants (i.e., beta, gamma, kappa, and omicron) as well as the endemic coronaviruses HCoV-OC43 and HCoV-229E. [0411] Additionally, several antibodies were found to be pan-coronavirus antibodies that recognizes a conserved epitope in the S1 subunit and bind with high affinity to N-terminal domain of SARS-CoV-2 S protein (NTD) (see, e.g., TXG-0048, TXG-0060, TXG-0066, TXG- 0072, TXG-0074, TXG-0076, TXG-0078, TXG-0099, TXG-0114, TXG-0136, TXG-0170, TXG-0173, TXG-0181, TXG-0203, TXG-0230) and/or to the S1 subunit of a new human coronavirus strain HCoV-HKU1 (see, e.g., TXG-0078, TXG-0112, TXG-0114, TXG-0136, TXG-0187, TXG-0192, TXG-0203, and TXG-0230). Accordingly, without being bound to any particular theory, these antibodies could be particularly useful in therapeutic combination against SARS-CoV-2 and other coronaviruses and in combination with RBD-binding or non-S1 binding therapeutic antibodies. US

[0412] In addition, as shown in Table 10, several antibodies were found to be pan- coronavirus antibodies that recognizes a conserved epitope in the S1 subunit and bind with high affinity to the S1 subunit of a new human coronavirus strain HCoV-HKU1 (see, e.g., TXG-0078, TXG-0091, TXG-0112, TXG-0114, TXG-0136, TXG-0187, TXG-0192, TXG-0203, TXG-0228, and TXG-0230 in Tables 6 and 10). It was observed that several antibodies tested in this experiment could bind to human coronavirus strain HCoV-HKU1 in low to mid nanomolar range. Accordingly, without being bound to any particular theory, these antibodies could be particularly useful in therapeutic combination against SARS-CoV-2 and other coronaviruses and in combination with RBD-binding, NTD-binding, or non-S1 binding therapeutic antibodies. [0413] In addition, as shown in Table 10, several antibodies (e.g., TXG-0060, TXG- 0066, TXG-0072, TXG-0076, TXG-0078, TXG-0099, TXG-0104, TXG-0170, TXG-0173, TXG-0174, TXG-0175, and TXG-0230) were found to bind the N-terminal domain of SARS- CoV-2 S protein. Of these antibodies, at least 8 were found to bind the N-terminal domain of SARS-CoV-2 S protein with high affinity (e.g., TXG-0072, TXG-0076, TXG-0078, TXG-0099, TXG-0170, TXG-0173, TXG-0174, TXG-0175, and TXG-0230). Accordingly, these antibodies could be particularly useful in therapeutic combination against SARS-2 with RBD-binding and non-S1 binding therapeutic antibodies. T^ABLE 10: Binding affinity of exemplary antibodies to the NTD of SARS-CoV-2 S protein or the S1 subunit of HCoV-HKU1. (ND: not determined).

EXAMPLE 13 Neutralization assays [0414] All 239 antibodies identified in Example 6 above were screened in addition to 49 control antibodies of known SARS-2 and other viral binding. Assays were performed with a clinical isolate of the SARS-CoV-2 B.1 lineage (MEX-BC2/2020). This virus carries the D614G mutation in the spike protein (full sequence available at the GISAID/EpiCoV database ID: EPI_ISL_747242). The screen was performed with a microneutralization assay that utilizes prevention of the virus-induced cytopathic effect (CPE) in Vero E6 cells. All antibodies (i.e., test-items) were provided at varying concentrations (0.06 to 0.23mg/mL), and they were stored at 4°C until use. The screen was performed in ten different experiments performed in ten days, each one assessing the activity of approximately 30 Abs in parallel. All plates included a positive control—plasma from a convalescent patient who had also received the first dose of the Pfizer/BioNTech mRNA vaccine (BNT162b2). Plasma was collected 21 days after vaccination. [0415] For this screen, Vero E6 cells were used to evaluate the neutralization activity of the antibody test-items against a replication competent SARS-CoV-2 virus. Antibodies were pre- incubated first with the virus for 1 hour at 37°C before addition to cells. Following pre- incubation of Ab/virus samples, Vero E6 cells were challenged with the mixture. After addition to cells, antibodies were present in the cell culture for the duration of the infection (96 hours), at which time a “Neutral Red” uptake assay was performed to determine the extent of the virus- induced CPE. Prevention of the CPE was used as a surrogate marker to determine the neutralization activity of the test-items against SARS-CoV-2. [0416] Eight dilutions of the antibodies were tested in duplicates for the neutralization assay using a five- fold dilution scheme starting at 1,000 ng/mL. Representative raw data from neutralization assay is shown in FIGS.21 and 22. When possible, IC50 values of the antibodies displaying neutralizing activity were determined using GraphPad Prism software. Plasma control was assessed on each plate using singlet data-points (8 two-fold dilutions throughout 1:20480). Representative neutralization curves (IC50) for control antibodies and antibody test- items are shown in FIGS.23 and 24. Data analysis of CPE-based neutralization assay [0417] The average absorbance at 540nm (A540) observed in infected cells in the presence of vehicle alone was calculated first, and then subtracted from all samples to determine the inhibition of the virus induced CPE. Data points were then normalized to the average A540 signal observed in uninfected cells (“mock”) after subtraction of the absorbance signal observed in infected cells. [0418] In the neutral red CPE-based neutralization assay, uninfected cells remained viable and uptake the dye at higher levels than non-viable cells. In the absence of antibodies, the virus-induced CPE leads to cell death in infected cells and lowers the A540 signal (this value equals 0% neutralization). By contrast, incubation with neutralizing antibodies prevents the virus induced CPE and leads to absorbance levels similar to those observed in uninfected cells. Full recovery of cell viability in infected cells represents 100% neutralization of the virus. Each plate assessed 3 antibodies in triplicates (rows A-C and F-H) or duplicates (rows D and E). However, data analysis avoided samples located in rows A and H to minimize “edge effects.” Therefore, all antibodies were evaluated in duplicates. Uninfected cells and infected cells in the absence of antibodies were analyzed using six replica data-points of each. Control neutralizing plasma was run in singlet data-points (1:160 or 1:320 to 1:20480). [0419] Every plate was analyzed during a QC step before data was selected for analysis. QC included signal to background values greater than 2.5, and percentage CV in uninfected lower than 20 (CV<20%). All plates passed QC and there was no need to perform repeats. In some instances, data-points identified as outliers may have been removed, or they were exchanged by an additional data-point of the extra row not used (the latter only for antibodies in A-C or F-H). However, these actions were rarely needed, and overall variation of the screen was excellent and within the ranges typically seen in the neutralization studies described herein. Control inhibitors and quality controls in live SARS-CoV-2 assay [0420] Quality controls for the infectivity assays were performed on every plate to determine: i) signal to background (S/B) values; ii) inhibition by plasma with neutralizing activity against SARS-CoV-2, and; iii) variation of the assay, as measured by the coefficient of variation (C.V.) of all data points. All controls worked as anticipated for the assay, and variation was within typical ranges seen in vendor laboratories. [0421] The average of all C.V. (of all duplicate data-points) in each plate was below 10% (average CV 7.1% for the 10 plates, whereas the variation of uninfected controls (“mock”), which were repeated six times on each plate, was below 5% (average 3.2%) (see, e.g., Table 11). The ratio of signal-to-background (S/B) for the neutralization assays, estimated by dividing the average signal in uninfected cells (A540nm) by the average signal in infected cells (vehicle alone), was 4.1-fold for the ten representative plates. When comparing the signal in uninfected cells to the signal in “no-cells” background wells, the S/B ratio of the assay was greater than 10 (data not shown). S/B values and variation for each of the plates are available in the accompanying excel file summary. [0422] To evaluate the neutralization activity of 288 Abs against SARS-CoV-2, the clinical isolate (MEX- BC2/2020) carrying a D614G mutation in the viral spike protein was used. Full sequence of this isolate is available at the GISAID/EpiCoV database with the identifier EPI_ISL_747242. [0423] A CPE-based neutralization assay was performed by infecting Vero E6 cells in the presence or absence of antibodies. Infection of cells leads to significant cytopathic effect and cell death after 4 days of infection. In this screen, reduction of the virus CPE in the presence of antibodies was used as a surrogate marker to determine the neutralization activity of the tested items. [0424] Vero E6 cells were maintained in DMEM with 10% fetal bovine serum (FBS), referred herein as DMEM10. Twenty-four hours after cell seeding, test samples were submitted to serial dilutions with DMEM with 2% FBS (DMEM2) in a different plate. Then, virus diluted in DMEM2 or DMEM2 alone was pre-incubated with antibody test-items for 1 hour at 37°C in a humidified incubator. Following incubation, media was removed from cells, and then cells were challenged with the SARS-CoV-2 / antibody pre-incubated mix. The amount of viral inoculum was previously titrated to result in a linear response inhibited by antibodies with known neutralizing activity against SARS-CoV-2. Cell culture media with the virus inoculum was not removed after virus adsorption, and antibodies and virus were maintained in the media for the duration of the assay (96 hours). After this period, the extent of cell viability was monitored with the neutral red (NR) uptake assay. [0425] The virus-induced CPE was routinely monitored under the microscope after 3 days of infection, and after 4 days, cells were stained with neutral red to monitor cell viability. Viable cells incorporate neutral red in their lysosomes. The uptake of neutral red relies on the ability of live cells to maintain the pH inside the lysosomes lower than in the cytoplasm, a process that requires ATP. Inside the lysosome, the dye becomes charged and is retained. After a 3-h incubation with neutral red (0.017%), the extra dye is washed away, and the neutral red is extracted from lysosomes by incubating cells for 15 minutes with a solution containing 50% ethanol and 1% acetic acid. The amount of neutral red is estimated by measuring absorbance at 540nm in a plate reader. The general procedure followed to determine the anti-SARS-CoV-2 activity of antibody test-items is summarized in FIG.20. [0426] In these experiments, antibodies were evaluated in duplicates using five-fold serial dilutions starting at 1 μg/mL. Controls included uninfected cells (“mock-infected”), and infected cells treated with vehicle alone. Some cells were treated with a positive control plasma derived from a convalescent patient who was also administered the first dose of Pfizer / BioNTech mRNA vaccine (BNT162b2). Plasma was collected 21 days after the vaccine injection. Results [0427] Of the antibodies tested against SARS-CoV-2 (lineage B.1, carrying the D614G mutation), approximately 40% of all antibodies displayed measurable neutralization activity. Exemplary antibodies that displayed measurable neutralization activity include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0120, TXG-0126, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, and TXG-0210. [0428] Table 11 below provides a summary of neutralization activity of 49 exemplary potently neutralizing antibodies as determined by IC₅₀ in live SARS-CoV-2 assays. Generally, an antibody is determined to potently neutralize SARS-CoV 2 when its IC50 is 1,000 ng/mL or less. T^ABLE 11: Neutralization activity of exemplary potently neutralizing TXG antibodies as determined in testing against SARS-CoV-2 (lineage B.1, carrying the D614G mutation).

[0429] Excluding the 29 control antibodies, at least eighteen (18) of the hits displayed IC50 values below 100 ng/mL, including TXG-0001 (44 ng/mL), TXG-0004 (90 ng/mL), TXG- 0006 (11 ng/mL), TXG-0009 (97 ng/mL), TXG-0063 (89 ng/mL), TXG-0080 (42 ng/mL), TXG- 0088 (65 ng/mL), TXG-0109 (32 ng/mL), TXG-0120 (39 ng/mL), TXG-0129 (15 ng/mL), TXG- 154 (22 ng/mL), TXG-0189 (53 ng/mL), TXG-0197 (79 ng/mL), TXG-0200 (42 ng/mL), TXG- 0202 (45 ng/mL), TXG-0204 (47 ng/mL), TXG-0209 (50 ng/mL), and TXG-0210 (41 ng/mL). [0430] A summary of the antibodies’ neutralization potency is also shown in FIG.28. As indicated in Table 11, the most potent neutralizing antibodies (excluding those identifying as controls) were TXG-0006, TXG-0129, and TXG-0154. [0431] In these experiments, positive plasma controls (CS478 pi_vac_pf1, plasma of Pfizer vaccine) were run on every plate to determine the intra-plate and inter-day variation. The average NT50 value and standard deviation of all plates was 2,183 ± 551(CV=25.2%), with lower variation when plates in the same day were evaluated. Of note, NT50 values for the plasma control were generated with dose-response curves using singlet data-points (as compared to duplicates), and that may have increased the variation observed in these controls. [0432] Additionally, an UpSet plot of antibodies identified as having neutralization activity against live SARS-COV-2 was generated (see, e.g., FIG.26), wherein the antibodies are binned into antigen bins as described in FIG.25. The data described in this figure illustrates that the BEAM-seq process described in the present disclosure allows for rapid identification of many antibodies with broad and robust neutralizing activity against several SARS-CoV-2 S variants of concern (VoC), e.g., beta, gamma, and kappa, as well as HKU1 (which is a different coronavirus). [0433] In addition, two UpSet plots of the potently (IC50 <= 1000 ng / ml) neutralizing antibodies retrieved from the BEAM-seq workflow described herein were generated (see, e.g., FIGS.27A and 27B). FIG.27A is an Upset plot of the potently neutralizing antibodies selected from 239 antibodies identified in Example 6. FIG.27B is an Upset plot of the potently neutralizing antibodies selected from the antibodies of Table 3. In these UpSet plots, rows represent the binding of these neutralizing antibodies to pre-fusion spike trimers from major SARS-CoV-2 variants of concern, the endemic HKU1 coronavirus spike protein and the SARS- CoV-2 N terminal domain. It was also observed that the antibodies identified in these experiments were diverse in their VH, VL, and isotype/subclass (see Table 3). These antibodies were found to use 18 diverse VH genes and 46 unique VH :VL pairings. Taken together, the data described in these figures illustrate that the BEAM-seq process described in the present disclosure allows for rapid identification of many antibodies with potent and broad neutralizing activity against several SARS-CoV-2 S variants of concern (VoC). E^XAMPLE 14 Epitope binning assays [0434] This Example describes the results of experiments performed to assess binding characteristics of select antibodies described herein. Methodology [0435] 1) Antigens: [0436] a) Pre-fusion trimerized spike protein from SARS-CoV-2 USA-WA1/2020 isolate, ACRO Biosystems. [0437] b) Pre-fusion trimerized spike protein from SARS-CoV-2 delta variant, ACRO Biosystems. [0438] c) SARS-CoV-2 NTD, ACRO Biosystems. [0439] 2) Surface Plasmon Resonance (SPR) techniques: [0440] a) Competition/sandwich. [0441] b) Bidirectional/premix. [0442] Epitope binning experiments were performed in a premix format using a Carterra LSA SPR biosensor equipped with a HC30M chip at 25°C in HBS-TE (10 mM HEPES pH 7.4, 150 mM NaCl, 3 mM EDTA, 0.05% Tween-20). First, antibodies were amine-coupled to the sensor chip by EDC/NHS activation, followed by ethanolamine HCl quenching. Antibodies and SARS-CoV-2 prefusion stabilized S trimers were combined and incubated for 1 hour in HBS-TE with 0.5 mg/ml BSA at 120 nM and 7.5 nM, respectively. This constituted a 5-molar excess relative to the S trimer antigens, accounting for three (3) binding sites for each molecule. Each premix sample was injected over the immobilized antibodies to determine blocking, partial blocking, or non-blocking activity. The sensor chip was regenerated between injections with Pierce IgG Elution Buffer (Thermo Fisher Scientific). [0443] Data were analyzed using Carterra’s Epitope Tool software. Briefly, blocking assignments were determined relative to the binding responses for S trimer alone (normalized to 1); premixes giving binding responses less than 0.5 were determined to be blocking, 0.5-0.7 were intermediate blocking, and above 0.7 were not blocking. Heat maps representing the competition results were generated where red, yellow, and green cells represent blocked, intermediate, and not blocked analyte/ligand pairs, respectively. A summary of binding characteristics of exemplary antibodies described herein is presented in FIGS.29-30 and Table 12 below. T^ABLE 12: Epitope binning of exemplary antibodies as determined in testing against a pre- fusion trimerized spike protein from SARS-CoV-2 USA-WA1/2020 isolate (WA1) and/or SARS-CoV-2 delta variant (Delta) by using SPR competition assay and bidirectional assay. A number of control antibodies (CTRL) were included in these experiments, including: CTRL- 0004: Casirivimab; CTRL-0005 (Imdevimab), CTRL-0006: Bamlanivimab; CTRL-0007: (Etesevimab), CTRL-0008: Sotrovimab; and CTRL-0009: Tixagevimab. NA: not applicable. Other: antibodies capable of binding to an epitope different that the antibodies in any other of the bins identified in the same column of Table 12.

Data interpretation [0444] In these experiments, antibodies that share an epitope bin are antibodies which compete for binding to the same epitopes in a dose-dependent manner. [0445] As shown in the table above and further described below, the discovered antibodies group into five prominent epitope bins. Furthermore, a number of the discovered antibodies group into unique bins outside of the five prominent bins. A. NTD targeting antibodies [0446] As shown in Table 12, nine (9) antibodies tested in these epitope binning experiments grouped into WA1 trimer bins 1 or 2. These likely represent antibodies that target NTD of the spike protein from SARS-CoV-2 USA-WA1/2020 isolate (WA1), based on SPR data indicating that antibodies that group into bins 1 and 2 exhibit high (nM) affinity for the NTD of SARS-CoV-2 S protein and the observation that they do not compete for binding with the antibodies in WA1 trimer bins 3, 4, or 3/4 (which include the FDA-authorized antibodies which have been shown to target RBD epitopes). Of these antibodies, as least fifteen antibodies were found to display measurable neutralization activity as determined by IC50 in live SARS-CoV-2 assays. Examples of antibodies that target NTD of the WA1 isolate and potently neutralize live SARS-CoV-2 include TXG-0066, TXG-0078, TXG-0104, TXG-0170, TXG-0173, and TXG- 0174. [0447] As shown in Table 12, seven (7) antibodies tested in these epitope binning experiments grouped into delta trimer bins 1, 1/2, or 2. These likely represent antibodies that target NTD of the spike protein from SARS-CoV-2 delta variant, based on SPR data indicating that antibodies that group into these bins exhibit high (nM) affinity for the NTD of SARS-CoV-2 S protein and the observation that they do not compete for binding with the antibodies in delta trimer bins 3, 4, or 3/4 (which include the FDA-authorized antibodies which have been shown to target RBD epitopes). All of these 7 antibodies were found to display measurable neutralization activity as determined by IC50 in live SARS-CoV-2 assays. Examples of antibodies that target NTD of the WA1 isolate and potently neutralize live SARS-CoV-2 include TXG-0078, TXG- 0091, TXG-0099, TXG-0170, and TXG-0174. [0448] B. RBD targeting antibodies [0449] As shown in Table 12, 36 antibodies tested in these epitope binning experiments grouped into WA1 trimer bins 3, 4, or 3/4. These likely represent antibodies targeting primarily RBD of the spike protein from SARS-CoV-2 USA-WA1/2020 isolate (WA1), based on the observation that they compete for binding with FDA-authorized antibodies which have been shown to target RBD epitopes. All of these 36 antibodies were found to display measurable neutralization activity as determined by IC50 in live SARS-CoV-2 assays. Examples of antibodies that target primarily RBD of the WA1 isolate and potently neutralize live SARS-CoV- 2 include TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0057, TXG-0063, TXG-0080, TXG-0081, TXG-0088, TXG-0091, TXG-0094, TXG-0100, TXG-0109, TXG-0115, TXG-0120, TXG-0129, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0180, TXG-0181, TXG-0183, TXG-0189, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, and TXG-0210. [0450] As shown in Table 12, eight (8) antibodies tested in these epitope binning experiments grouped into WA1 trimer bin 3, along with CTRL-0008 (sotrovimab). These likely represent antibodies that target a WA1 RBD epitope that is at least partially distinctive from those targeted by bins 3/4 or 4, e.g., a distinctive RBD epitope from those targeted by the tested FDA-approved antibodies save for sotrovimab. All of these 8 antibodies were found to display measurable neutralization activity as determined by IC₅₀ in live SARS-CoV-2 assays. Examples of antibodies in WA1 trimer bin 3 and which potently neutralize live SARS-CoV-2 include TXG-0057, TXG-0063, TXG-0091, TXG-0094, TXG-0120, TXG-0153, TXG-0181, and TXG- 0183. [0451] As shown in Table 12, 12 antibodies tested in these epitope binning experiments grouped into WA1 trimer bin 4, along with CTRL-0004 (Casirivimab), CTRL-0007 (Etesevimab), and CTRL-0009 (Tixagevimab). These likely represent antibodies that target a WA1 RBD epitope that is at least partially distinctive from those targeted by bins 3 or 3/4. All of these 12 antibodies were found to display potent neutralization activity as determined by IC50 in live SARS-CoV-2 assays. Examples of antibodies in WA1 trimer bin 4 and which potently neutralize live SARS-CoV-2 include TXG-0109, TXG-0115, TXG-0141, TXG-0144, TXG- 0154, TXG-0180, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, and TXG-0210. [0452] Fifteen (15) antibodies tested in these epitope binning experiments grouped into WA1 trimer bin 3/4, along with CTRL-0005 (Imdevimab) and CTRL-0006 (Bamlanivimab). These likely represent antibodies that target a WA1 RBD epitope that is at least partially distinctive from those targeted by bin 3 or bin 4, in that they partially compete with antibodies such bins. All of these antibodies displayed potent neutralization activity as determined by IC₅₀ in live SARS-CoV-2 assays. These antibodies include TXG-0001, TXG-0002, TXG-0004, TXG- 0005, TXG-0006, TXG-0008, TXG-0009, TXG-0080, TXG-0081, TXG-0088, TXG-0100, TXG-0115, TXG-0129, TXG-0154, and TXG-0189. [0453] As shown in Table 12, 25 antibodies tested in these epitope binning experiments grouped into delta trimer bins 3, 4, or 3/4. These likely represent antibodies targeting primarily RBD of the spike protein from SARS-CoV-2 delta variant, based on the observation that they compete for binding with FDA-authorized antibodies which have been shown to target RBD epitopes. Nearly all of these antibodies also grouped into WA1 trimer bins 3, 4, or 3/4. All of these 25 antibodies were found to display measurable neutralization activity as determined by IC₅₀ in live SARS-CoV-2 assays. Examples of antibodies that target primarily RBD of the SARS-CoV-2 delta variant and potently neutralize live SARS-CoV-2 include TXG-0001, TXG- 0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0063, TXG-0066, TXG-0094, TXG-0100, TXG-0120, TXG-0129, TXG-0141, TXG-0154, TXG-0180, TXG-0181, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, TXG-0209, and TXG- 0210. [0454] As shown in Table 12, four (4) antibodies tested in these epitope binning experiments grouped into delta trimer bin 3, along with CTRL-0008 (sotrovimab). These likely represent antibodies that target a delta RBD epitope that is at least partially distinctive from those targeted by bins 3/4 or 4, e.g., a distinctive delta RBD epitope from those targeted by the tested FDA-approved antibodies save for sotrovimab. These 4 antibodies also grouped into WAT1 trimer bin 3. All of these 4 antibodies were found to display potent neutralization activity as determined by IC50 in live SARS-CoV-2 assays. Antibodies that distinctively target RBD of the SARS-CoV-2 delta variant and potently neutralize live SARS-CoV-2 include TXG-0063, TXG- 0094, TXG-0120, and TXG-0181. [0455] Eight (8) antibodies tested in these epitope binning experiments grouped into delta trimer bin 4, along with CTRL-0004 (Casirivimab), CTRL-0007 (Etesevimab), and CTRL- 0009 (Tixagevimab). These likely represent antibodies that target a delta RBD epitope that is at least partially distinctive from those targeted by bins 3 or 3/4. All of these 8 antibodies were found to display potent neutralization activity as determined by IC50 in live SARS-CoV-2 assays. Examples of antibodies in delta trimer bin 4 and which potently neutralize live SARS-CoV-2 include TXG-0180, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0204, and TXG-0209. [0456] Thirteen (13) antibodies tested in these epitope binning experiments grouped into delta trimer bin 3/4, along with CTRL-0005 (Imdevimab). These likely represent antibodies that target a delta RBD epitope that is at least partially distinctive from those targeted by bin 3 or bin 4, in that they partially compete with antibodies such bins. Of these, 13 display potent neutralization activity as determined by live SARS-CoV-2 assays. Examples of antibodies in delta trimer bin 3/4 and which potently neutralize live SARS-CoV-2 include TXG-0001, TXG- 0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0066, TXG-0100, TXG-0129, TXG-0141, TXG-0154, and TXG-0210. [0457] C. Other epitopes [0458] Nine (9) antibodies tested in these epitope binning experiments grouped into WA1 trimer bins “Other”. These likely represent antibodies that target epitopes that are distinctive from the epitopes targeted by any other of the WA1 trimer bins. Exemplary antibodies in these categories include TXG-0076, TXG-0099, TXG-0112, TXG-0114, TXG-0187, TXG- 0192, TXG-0203, TXG-0228, and TXG-0230. Of these eleven antibodies, at least two are potent neutralizers. Example antibodies that belong in the WA1 trimer “Other” bin and potently neutralize live SARS-CoV-2 include TXG-0076 and TXG-0099. Of these nine antibodies, at least TXG-0099 exhibits high (nM) affinity for WT spike and the gamma, kappa, and beta variants by SPR. Of these nine antibodies, at least eight exhibit nanomolar affinity for NTD. Example antibodies that belong in the WA1 trimer “Other” and exhibit high (nM) affinity for NTD include TXG-0076, TXG-0099, TXG-0112, TXG-0114, TXG-0187, TXG-0192, TXG- 0203, and TXG-0230. Of these nine antibodies, at least seven exhibit nanomolar affinity for HKU. Example antibodies that belong in the WA1 trimer “Other” bin and exhibit nanomolar affinity for HKU include TXG-0112, TXG-0114, TXG-0187, TXG-0192, TXG-0203, TXG- 0228, and TXG-0230. [0459] Nine (9) antibodies tested in these epitope binning experiments grouped into delta trimer bin 5. These likely represent antibodies that target a distinct delta variant epitope from other binned groups, e.g., distinct from any of the tested FDA approved antibodies. Exemplary antibodies in this category include TXG-0080, TXG-0115, TXG-0136, TXG-0175, TXG-0192, and TXG-0230. Of these, three display potent neutralization activity as determined by live SARS-CoV-2 assays. Examples of antibodies in delta trimer bin 5 and which potently neutralize live SARS-CoV-2 include TXG-0080, TXG-0115, and TXG-0175. [0460] Fifteen (15) antibodies tested in these epitope binning experiments grouped into delta trimer bins “Other”, along with CTRL-0006 (bamlanivimab). These likely represent antibodies that target epitopes that are distinctive from the epitopes targeted by any other of the delta trimer bins. Exemplary antibodies in these categories include TXG-0057, TXG-0076, TXG-0081, TXG-0088, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0144, TXG-0173, TXG-0183, TXG-0187, TXG-0189, TXG-0203, and TXG-0228. Of these 15 antibodies, 10 exhibit potent neutralization activity. Examples of antibodies in delta trimer bin “Other” and which potently neutralize live SARS-CoV 2 include TXG-0057, TXG-0076, TXG-0081, TXG- 0088, TXG-0104, TXG-0109, TXG-0144, TXG-0173, TXG-0183, and TXG-0189. Of these 15 antibodies, at least 12 exhibit high (nM) affinity for WT spike and the kappa and gamma variants by SPR, and at least 9 exhibit high (nM ) affinity for WT spike and the beta, gamma, and kappa variants by SPR. Exemplary antibodies that belong in the delta trimer “Other” bin and exhibit high (nM) affinity for WT spike and the gamma and kappa variants include TXG-0057, TXG- 0076, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0144, TXG-0173, TXG-0183, TXG-0187, TXG-0203, and TXG-0228. Exemplary antibodies that belong in the delta trimer “Other “ bin and exhibit high (nM) affinity for WT spike and the beta, gamma, and kappa variants include TXG-0057, TXG-0109, TXG-0112, TXG-0114, TXG-0144, TXG-0183, TXG- 0187, TXG-0203, and TXG-0228. [0461] Antibodies that group into different epitope bins can advantageously be used in a therapeutic antibody cocktail or combination therapy regimen. For example, a neutralizing antibody from bin A can thus be combined with a neutralizing antibody from bin B effectively as the two antibodies do not bind in the same location. Examples of such complementary bins that may be advantageously used in a combination therapy or antibody cocktail include: [0462] NTD and RBD targeting combination: a. Antibody 1: an antibody from bin 1 or bin 2, both of which represent NTD- binding antibodies b. Antibody 2: an antibody from bin 3, 4, or 3/4, which represent antibodies targeting primarily RBD [0463] RBD distinctive targeting combination: a. Antibody 1: an antibody from bin 3 (sotrovimab-like antibodies) b. Antibody 2: an antibody from bin 4 [0464] RBD partially distinctive targeting combination: a. Antibody 1: an antibody from bin 3 or 4 b. Antibody 2: an antibody from bin 3/4 which partially competes with an antibody from bin 3 or 4. EXAMPLE 15 LNP and pharmacokinetic (pK) studies [0465] This Example describes the results of experiments demonstrating that antibodies described in the present disclosure can be administered to subjects using lipid nanoparticles (LNP) as delivery vehicle and subsequently be detected in animal pK models. Some experiments described in this Example are performed to demonstrate that antibodies of defined affinities and antigen specificities can exert protective functions through non-neutralizing and neutralizing activities. [0466] In these experiments, twenty (20) antibodies are selected based on their relevant binding affinity, functional information, nucleotide coding sequences, including the rearranged VDJ/VJ and constant region identities. This study includes both neutralizing (n=13) and non- neutralizing antibodies (n=7) with IgM, IgA, and IgG isotypes as indicated in Table 13 below. TABLE 13: Twenty (20) antibodies selected for LNP and pharmacokinetic studies. O escape: broad recognition of SARS-CoV-2 variants but no recognition of omicron variant.

[0467] mRNA-containing LNPs of each candidate antibody are manufactured according to the methods described above. These LNPs are injected into mice for pK studies with a duration of 1 week, with a total of 5 mice per antibody candidate (100 mice total). At least 5 time-points are collected and measured, every 12 hours over the first 2 days and then minimally at least one more time point 96 hours after injection. It is expected that one or more of the antibodies are successfully detected via anti-human immunoglobulin secondary antibodies recognizing the corresponding human IgM, IgA, and IgG isotypes, e.g., at a concentration of ≥100 ng/ml peak serum levels . [0468] In vivo functional studies [0469] Sufficient LNP for each antibody is used to passively immunize Syrian hamsters (5- 8 hamsters are tested per antibody). These Syrian hamsters are then challenged with a lethal concentration of live SARS-CoV-2 virus (strain 2019nCoV/USA-WA01/2020). In these experiments, the primary endpoint is survival; the secondary endpoint is prevention of weight loss; and additional exploratory endpoints include detectable viral subgenomic RNAs and infectious plaque-forming units in lung and affected tissue. Hamsters in the control/comparator group (n=8) receive LNPs containing a non-translating Factor IX RNA (NTFIX). The experiments are completed over the course of 3 months’ time. It is expected that at least one antibody shows differential protection from death or weight loss during the challenge studies, as measured by comparison to the sham-treated hamsters, of which a large number (50%) are expected to die and/or lose significant body weight. EXAMPLE 16 Structural definition of a broadly conserved NTD neutralizing epitope [0470] This Example describes the results of experiments performed to characterize structural features of the epitope to which TX-0078 binds. It was noted that although a number of NTD-specific nAbs have been reported, none exhibited the breadth of TXG-0078, making the specific molecular interactions between the antibody and its target particularly important. Experiments were performed to obtain a 3.9Å cryo-EM reconstruction of TXG-0078 in complex with the WA1 SARS-CoV-2 Spike (see, e.g., FIG.32A). It was observed that TXG-0078 has an angle of approach similar to that of 4A8, a previously reported (Chi et al.2020) NTD-specific nAb (see, e.g., FIG.32B), with binding interactions between all three heavy chain complementarity determining region (CDR) loops and the N3 and N5 loops of NTD (see, e.g., FIG.32C). Separately, a separate 3Å negative-stain EM image of TXG-0078 Fab in complex with the spike trimer from SARS-CoV-2 Wuhan entry strain (WT) was also obtained to confirm the angle of approach (see, e.g., FIG.32D). [0471] The cryo-EM studies show that TXG-0078 is an NTD supersite-targeting antibody. Such NTD supersite-targeting antibodies arise in response to SARS-CoV-2 infection but have not been known to broadly target other human coronaviruses. However, as disclosed herein, TXG-0078 has picomolar affinity to the WA-1/2020, beta, kappa, and gamma variants of SARS- CoV-2, and micromolar affinity to the spike proteins of the OC-43, HKU1, and 229E endemic human coronaviruses. This result is surprising, and highlights TXG-0078 as a broadly neutralizing antibody that targets the NTD domain of the spike protein and that broadly target a large number of SARS-CoV2 variants as well as other endemic human coronaviruses. EXAMPLE 17 In vivo studies in mouse model confirms prophylactic efficacy of TXG-0078 [0472] This Example describes the results of experiments performed in mouse models demonstrating that antibodies described in the present disclosure can prophylactically protect mice from in vivo SARS-CoV-2 challenge. Animal challenge study [0473] Each group (n=5) was passively immunized with 20 µg of each mAb through intraperitoneal injections 24 hours prior to infection. Mice were infected with 30,000 FFU of SARS-CoV-2 (WA1/2020). Mice were weighed daily, and percent baseline weight was calculated relative to day 0 weight. On day 5, mice were euthanized and lung lobes were extracted for viral titer quantification. [0474] In these experiments, 20 μg of prophylactic antibody was administered to a total of 15 ACE2 transgenic mice in 3 treatment groups: (i) TXG-0078, (ii) anti-RBD antibody, and (iii) Control antibody. In these experiments, the Control antibody was an antibody targeting a different virus species, Zika virus (ZIKV), and the anti-RBD antibody was a RBD-targeting pan- coronavirus antibody which was markedly broader and less potent than TXG-0078. [0475] Each mouse was weighed at Day 0 (baseline), and weighed daily for another 5 days before sacrifice. It was observed that mice receiving TXG-0078 were protected from weight loss and showed reduced viral load in the lung (see, e.g., FIGS.33A-33B). These results demonstrate a markedly superior prophylactic effect of the TXG-0078 antibody as compare to the reference anti-RBD antibody. [0476] It was observed that although the anti-RBD antibody used in this experiment was markedly broader than TXG-0078, it was less potent; the IC50 of TXG-0078 against SARS-CoV- 2 in these experiments was 170 ng/ml. Without being bound to any particular theory, it is believed that the anti-RBD antibody used in this experiment and similar antibodies could arise easily given the correct immune stimuli. EXAMPLE 18 In vivo studies assessing prophylactic efficacy of cocktails of antibodies targeting different epitopes [0477] This Example describes experiments performed in mouse models to demonstrate that therapeutic cocktails of antibodies targeting different epitope regions of the spike protein can provide superior protection in vivo to SARS-CoV-2 challenge. [0478] In these experiments, each group (n=10) is passively immunized with 20 µg of each antibody cocktail through intraperitoneal injections 24 hours prior to infection. Mice are infected with 30,000 FFU of SARS-CoV-2. The SARS-CoV-2 can be WA1/2020, a beta variant, a gamma variant, a kappa variant, a delta variant, or an omicron variant (e.g., BA.4 variant, BA.5 variant, BA.2 variant such as BA.2.75). Mice are weighed daily, and percent baseline weight is calculated relative to day 0 weight. On day 5, mice were euthanized and lung lobes were extracted for viral titer quantification. [0479] In these experiments, 20 μg of prophylactic antibody is administered to a total of 50 ACE2 transgenic mice in 5 treatment groups: [0480] (1) Groups 1-3 are administered with antibody cocktail comprising: [0481] (i) a potently neutralizing NTD-targeting antibody with binding affinity for the omicron variant of SARS-CoV-2 or at least one endemic human coronaviruses (HCoVs)(i.e., containing TXG-0078, TXG-0099, or TXG-0174 in Groups 1, 2, and 3, respectively), and [0482] (ii) a neutralizing RBD antibody with binding affinity for the omicron variant of SARS-CoV-2 and at least one endemic human coronaviruses (HCoVs): TXG-0091 [0483] (1) Group 4 is administered with Control 1 containing only anti-RBD antibody, and [0484] (2) Group 5 is administered with Control 2 containing only potently neutralizing NTD-targeting antibody. [0485] Each mouse is weighed at Day 0 (baseline), and is weighed daily for another 5 days before sacrifice. It is predicted that mice of Groups 1-3 receiving an antibody cocktail are better protected from weight loss and show reduced viral load in the lung, to demonstrate a markedly superior prophylactic effect of the antibody cocktail as compared to Groups 4 and 5. [0486] While particular alternatives of the present disclosure have been disclosed, it is to be understood that various modifications and combinations are possible and are contemplated within the true spirit and scope of the appended claims. There is no intention, therefore, of limitations to the exact abstract and disclosure herein presented.

Claims

CLAIMS WHAT IS CLAIMED IS: 1. A composition comprising a nucleic acid encoding an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all six complementary determining regions (CDRs) from an antibody identified in Tables 1A-1B, and wherein optionally the composition is formulated in a lipid-based nanoparticle (LNP).

2. A composition comprising an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all six CDRs from an antibody identified in Tables 1A-1B, and wherein optionally the composition is formulated in a lipid-based nanoparticle (LNP).

3. The composition of any one of claims 1 to 2, wherein the antigen-binding molecule is any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230.

4. The composition of any one of claims 1 to 3, wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all six complementary determining regions (CDRs) from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203.

5. The composition of any one of claims 1 to 4, wherein the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for a spike (S) protein of SARS-CoV-2.

6. The composition of any one of claims 1 and 3-5, wherein the nucleic acid is a DNA molecule or an RNA molecule.

7. The composition of claim 5, wherein the RNA molecule is a messenger RNA (mRNA) molecule.

8. The composition of any one of claims 6 to 7, wherein the nucleic acid comprises one or more modified nucleosides.

9. The composition of claim 8, wherein the one or more modified nucleosides comprises pyridin-4-one ribonucleoside, 5-aza-uridine, 2-thio- 5-aza-uridine, 2-thiouridine, 4-thio- pseudouridine, 2-thio-pseudouridine, 5- hydroxyuridine, 3-methyluridine, 5-carboxymethyl- uridine, 1-carboxymethyl- pseudouridine, 5-propynyl-uridine, 1-propynyl-pseudouridine, 5- taurinomethyluridine, 1- taurinomethyl-pseudouridine, 5-taurinomethyl-2-thio-uridine, 1 - taurinomethyl-4-thio- uridine, 5-methyl-uridine, 1-methyl-pseudouridine, 4-thio-l-methyl- pseudouridine, 2- thio- 1 -methyl-pseudouridine, 1 -methyl- 1 -deaza-pseudouridine, 2-thio- 1 - methyl- 1 -deaza- pseudouridine, dihydrouridine, dihydropseudouridine, 2-thio-dihydrouridine, 2-thio- dihydropseudouridine, 2-methoxyuridine, 2-methoxy-4-thio-uridine, 4-methoxy- pseudouridine, 4-methoxy-2-thio-pseudouridine, 5-aza-cytidine, pseudoisocytidine, 3- methyl- cytidine, N4-acetylcytidine, 5-formylcytidine, N4-methylcytidine, 5- hydroxymethylcytidine, 1 - methyl-pseudoisocytidine, pyrrolo-cytidine, pyrrolo- pseudoisocytidine, 2-thio-cytidine, 2-thio- 5-methyl-cytidine, 4-thio-pseudoisocytidine, 4- thio- 1 -methyl-pseudoisocytidine, 4-thio- 1 - methyl- 1 -deaza-pseudoisocytidine, 1 -methyl- 1 -deaza-pseudoisocytidine, zebularine, 5-aza- zebularine, 5-methyl-zebularine, 5-aza-2- thio-zebularine, 2-thio-zebularine, 2-methoxy-cytidine, 2-methoxy-5-methyl-cytidine, 4- methoxy-pseudoisocytidine, 4-methoxy- 1 -methyl- pseudoisocytidine, 2-aminopurine, 2, 6-diaminopurine, 7-deaza-adenine, 7-deaza-8-aza-adenine, 7-deaza-2-aminopurine, 7- deaza-8-aza-2-aminopurine, 7-deaza-2,6-diaminopurine, 7-deaza-8- aza-2,6- diaminopurine, 1 -methyladenosine, N6-methyladenosine, N6-isopentenyladenosine, N6- (cis-hydroxyisopentenyl)adenosine, 2-methylthio-N6-(cis-hydroxyisopentenyl) adenosine, N6-glycinylcarbamoyladenosine, N6-threonylcarbamoyladenosine, 2- methylthio-N6-threonyl carbamoyladenosine, N6,N6-dimethyladenosine, 7- methyladenine, 2-methylthio-adenine, and 2- methoxy-adenine, inosine, 1 -methyl-inosine, wyosine, wybutosine, 7-deaza-guanosine, 7-deaza- 8-aza-guanosine, 6-thio-guanosine, 6- thio-7-deaza-guanosine, 6-thio-7-deaza-8-aza-guanosine, 7-methyl-guanosine, 6-thio-7- methyl-guanosine, 7-methylinosine, 6-methoxy-guanosine, 1 - methylguanosine, N2- methylguanosine, N2,N2-dimethylguanosine, 8-oxo-guanosine, 7-methyl- 8-oxo- guanosine, l-methyl-6-thio-guanosine, N2-methyl-6-thio-guanosine, and N2,N2- dimethyl-6-thio-guanosine, and combinations thereof.

10. The composition of any one of claims 1 to 9, wherein the lipid nanoparticle comprises an ionizable cationic lipid, a cationic lipid, an anionic lipid, a neutral lipid, a sterol, a PEG-modified lipid, or a combination of any thereof.

11. The composition of claim 10, wherein the lipid nanoparticle further comprises phosphatidyl choline.

12. The composition of claim 10, wherein the sterol is cholesterol.

13. The composition of any one of claims 1 to 12, wherein the mean ratio of lipid to nucleic acid (wt/wt) ranges from about 2:1 to about 100:1.

14. The composition of any one of claims 1 to 13, wherein the LNP has a mean diameter ranging from about 10 nm to about 200 nm.

15. The composition of any one of claims 1 to 14, wherein the antigen-binding molecule or antigen-binding fragment has a binding affinity for the spike (S) protein of two, three, four, five or more variants of SARS-CoV-2.

16. The composition of claim 15, wherein the SARS-CoV-2 variants comprise any one of alpha, beta, delta, gamma, kappa, omicron, or a combination thereof.

17. The composition of claim 16, wherein at least one of the SARS-CoV-2 variants is omicron.

18. The composition of any one of claims 1 to 17, wherein the antigen-binding molecule or antigen-binding fragment further has a binding affinity for one or more human coronaviruses (HCoVs) being any one of HCoV-229E, HCoV-OC43, HCoV-HKU1, or a variant of any thereof, or a combination thereof.

19. The composition of claim 18, wherein the one or more HCoVs is any one of HCoV-229E, HCoV-OC43, or a combination thereof.

20. The composition of any one of claims 1 to 18, wherein the antigen-binding molecule or antigen-binding fragment has a sub-nanomolar binding affinity for a spike (S) protein of SARS- CoV-2, a fragment thereof, or a multimeric form thereof.

21. The composition of any one of claims 1 to 20, wherein the antigen-binding molecule or antigen-binding fragment has a sub-picomolar binding affinity for a SARS-CoV-2 S protein, a fragment thereof, or a multimeric form thereof.

22. The composition of any one of claims 1 to 21, wherein the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for S1 subunit of the SARS-CoV-2 S protein.

23. The composition of claim 22, wherein the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for a receptor binding domain (RBD) and/or a N-terminal domain (NTD) of the S1 subunit.

24. The composition of claim 23, wherein the antigen-binding molecule or antigen-binding fragment has a binding affinity to the NTD of the S1 subunit.

25. The composition of any one of claims 1 to 24, wherein the antigen-binding molecule or antigen-binding fragment thereof has binding affinity for a trimeric form of the SARS-CoV-2 S protein.

26. The composition of any one of claims 1 to 25, wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all framework regions (FWRs) from the antibody selected from Tables 1A-1B.

27. The composition of any one of claims 3 to 26, wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all framework regions (FWRs) from the antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG- 0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230.

28. The composition of any one of claims 1 to 27, wherein the antigen-binding molecule or antigen-binding fragment further comprises a heavy chain constant region.

29. The composition of claim 28, wherein the heavy chain constant region is an IgA, IgD, IgE, IgG, or IgM heavy chain constant region.

30. The composition of any one of claims 28 to 29, wherein the heavy chain constant region is of the same isotype and subclass as the antibody identified in Tables 1A-1B.

31. The composition of any one of claims 28 to 29, wherein the heavy chain constant region is of the same isotype and subclass as the antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230.

32. The composition of any one of claims 1 to 31, wherein the antigen-binding molecule or antigen-binding fragment further comprises a light chain constant region.

33. The composition of claim 32, wherein the light chain constant region is a kappa type or lambda type light chain constant region.

34. The composition of any one of claims 32 to 33, wherein the light chain constant region is the same light chain constant region of the antibody identified in Tables 1A-1B.

35. The composition of any one of claims 32 to 33, wherein the light chain constant region is the same light chain constant region of the antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230.

36. A method for reducing binding of a spike protein of a coronavirus (CoV-S) to a cell in a subject and/or reducing entry of the coronavirus into a cell of a subject, wherein the method comprising therapeutically or prophylactically administering to the subject: (a) an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike (S) protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG- 0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG- 0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG- 0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG- 0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG- 0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG- 0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, and wherein the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the spike (S) protein of two, three, four, five or more variants of SARS-CoV-2, and/or for one or more human coronaviruses (HCoVs) is any one of HCoV-229E, HCoV-OC43, HCoV- HKU1, or a variant of any thereof, or a combination thereof; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof of (a).

37. A method for inducing an immune response in a subject, the method comprising therapeutically or prophylactically administering to the subject a composition according to any one of claims 1 to 35.

38. A method for aiding in the neutralization of two, three, four, five or more variants of SARS-CoV-2, wherein said aiding comprises providing: (a) an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike (S) protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG- 0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG- 0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG- 0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG- 0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG- 0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG- 0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof of (a).

39. A method for aiding in the neutralization of two, three, four, five or more variants of SARS-CoV-2, wherein said aiding comprises providing a composition according to any one of claims 3 to 35.

40. A method for reducing a viral load of two, three, four, five or more variants of SARS-CoV- 2, the method comprises providing: (a) an antigen-binding molecule, or an antigen-binding fragment thereof, that binds to a spike (S) protein of SARS-CoV-2, wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all six CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG- 0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG- 0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG- 0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG- 0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG- 0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG- 0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG- 0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof of (a).

41. A method for reducing the viral load of two, three, four, five or more variants of SARS- CoV-2, wherein said method comprises providing a composition according to any one of claims 3 to 35.

42. A method of any one of claims 36 to 41, wherein the antigen-binding molecule or antigen- binding fragment thereof comprises all six complementary determining regions (CDRs) from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG- 0008, TXG-0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203.

43. The method of any one of claims 36 to 42, wherein the subject is suspected of being infected with a coronavirus, has been infected with a coronavirus, has been vaccinated, or has been recovered from a coronavirus infection.

44. The method of any one of claims 36 to 43, wherein the subject is an immunocompromised subject or has been previously treated for coronavirus infection.

45. The method of any one of claims 36 to 44, wherein the subject is a mammalian subject.

46. The method of claim 45, wherein the mammalian subject is a human subject.

47. The method of any one of claims 36 to 46, wherein the coronavirus belongs to a genus being any one of alphacoronavirus, betacoronavirus, gammacoronavirus, or deltacoronavirus.

48. The method of claim 47, wherein the coronavirus belongs to a betacoronavirus lineage being any one of lineage A, lineage B, lineage C, or lineage D.

49. The method of claim 48, wherein the coronavirus is human coronavirus 229E, OC43, HKU1, NL63, SARS-CoV-1, SARS-CoV-2, MERS-CoV, or a variant of any thereof.

50. The method of claim 49, wherein the coronavirus is SARS-CoV-2 or a variant thereof is any one of alpha, beta, delta, gamma, kappa, and omicron.

51. The method of any one of claims 36 to 50, wherein one of the two, three, four, five or more variants of SARS-CoV-2 is omicron.

52. The method of any one of claims 36 to 51, wherein one of the one or more of the HCoVs being any one of HCoV-229E, HCoV-OC43, or a combination thereof; and HCoV-HKU1 is HCoV-229E or HCoV-OC43.

53. The method of any one of claims 36 to 50, wherein the composition is administered at a total dose of about 0.0001 mg/kg to about 40 mg/kg.

54. The method of any one of claims 36 to 53, wherein the composition is administered on a schedule being any one of the following: three time a day, twice a day, once a day, every other day, every third day, weekly, biweekly, every three weeks, every four weekly, and monthly.

55. The method of any one of claims 36 to 54, wherein the total dose is administered by multiple administrations.

56. The method of claim 55, wherein the multiple administrations occur on a schedule being any one of the following: three times a day, twice a day, once a day, every other day, every third day, weekly, biweekly, every three weeks, every four weekly, and monthly.

57. The method of any one of claims 36 to 56, wherein the composition is administered by intravenous, intramuscular, subcutaneous, and/or local administration.

58. The method of any one of claims 36 to 57 wherein the administered composition reduces binding of the CoV-S protein to and/or reduces coronavirus entry into a cell of the subject.

59. The method of any one of claims 36 to 58, wherein the administered composition neutralizes against the coronavirus.

60. The method of any one of claims 36 to 59, wherein the administered composition treats, prevents, or ameliorates a heath condition associate with a coronavirus infection in the subject.

61. The method of claim 60, wherein the administered composition reduces the viral load in the subject as compared to a reference subject who has not been administered with the composition.

62. The method of any one of claims 36 to 61, further comprising administering to the subject an additional therapy.

63. The method of claim 62, wherein the additional therapy comprises an anti-viral agent being any one of interferon, Remdesivir, Baricitinib, Azithromycin, Nirmatrelvir, Ritonavir, Molnupiravir, Casirivimab, Imdevimab, Bamlanivimab, Etesevimab, Sotrovimab, Cilgavimab, Bebtelovimab, Tocilizumab, Tixagevimab, or a combination thereof.

64. A method for detecting the presence of SARS-CoV-2 S protein and/or SARS-CoV-2 in a biological sample, the method comprising contacting a biological sample with an antigen- binding molecule having an amino acid sequence that is any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, or an antigen-binding fragment of any thereof, and wherein optionally the antigen-binding molecule or antigen-binding fragment has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof.

65. The method of claim 64, wherein the antigen-binding molecule or antigen-binding fragment thereof comprises all six complementary determining regions (CDRs) from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG- 0009, TXG-0048, TXG-0070, TXG-0078, TXG-0081, TXG-0087, TXG-0114, TXG-0115, TXG-0154, TXG-0174, TXG-0175, TXG-0180, TXG-0192, or TXG-0203.

66. The method of any one of claims 64 to 65, wherein the biological sample is from a subject suspected of being infected with a coronavirus, has been infected with a coronavirus, has been vaccinated, or has been recovered from a coronavirus infection.

67. The method of any one of claims 64 to 66, further comprising detecting a complex formed between the antigen-binding molecule or antigen-binding fragment with an SARS-CoV-2 S antigen.

68. The method of claim 67, wherein said detecting comprises visualizing the complex by using an enzyme, a secondary antibody, a colored dye, a fluorescent dye, a chemiluminescent molecule, a molecule containing a radioactive atom, or a molecule containing a heavy metal.

69. A method for aiding in the diagnosis, prognosis, monitoring, and/or evaluation of a coronavirus infection and/or treatment thereof in a subject, wherein said aiding comprises providing: an antigen-binding molecule having an amino acid sequence being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG- 0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG- 0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG- 0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG- 0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230; or an antigen-binding fragment of any thereof, wherein optionally the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof.

70. Kit for preventing, treating, diagnosing, or imaging a virus, a disease, a disorder, and/or a health condition, the kit comprising: (a) an antigen-binding molecule, or an antigen-binding fragment of any thereof, comprising all 6 CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG-0230, wherein optionally the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof; and/or (b) a nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof of (a); and instructions for performing the method of any one of claims 36 to 69.

71. A method of manufacturing a pharmaceutical composition, the method comprising: (a) admixing a lipid solution with an aqueous buffer solution comprising a buffer agent thereby forming a lipid nanoparticle solution comprising a lipid nanoparticle (LNP); and (b) adding to the lipid nanoparticle: (i) an antigen-binding molecule, or an antigen-binding fragment of any thereof, comprising all 6 CDRs from an antibody being any one of TXG-0001, TXG-0002, TXG-0004, TXG-0005, TXG-0006, TXG-0008, TXG-0009, TXG-0048, TXG-0057, TXG-0060, TXG-0063, TXG-0066, TXG-0070, TXG-0072, TXG-0074, TXG-0076, TXG-0078, TXG-0080, TXG-0081, TXG-0087, TXG-0088, TXG-0091, TXG-0094, TXG-0098, TXG-0099, TXG-0100, TXG-0104, TXG-0109, TXG-0112, TXG-0114, TXG-0115, TXG-0120, TXG-0129, TXG-0136, TXG-0141, TXG-0144, TXG-0153, TXG-0154, TXG-0170, TXG-0173, TXG-0174, TXG-0175, TXG-0180, TXG-0181, TXG-0183, TXG-0187, TXG-0189, TXG-0192, TXG-0197, TXG-0198, TXG-0200, TXG-0201, TXG-0202, TXG-0203, TXG-0204, TXG-0209, TXG-0210, TXG-0228, or TXG- 0230, wherein optionally the antigen-binding molecule or antigen-binding fragment thereof has a binding affinity for the omicron variant of SARS-CoV-2 or one or more endemic HCoVs that is any one of 229E, OC43, HKU1, or a combination thereof; and/or (ii) a nucleic acid encoding the antigen-binding molecule or antigen-binding fragment thereof of (a), thereby forming a LNP formulation comprising the LNP associated with the antigen-binding molecule or antigen-binding fragment thereof, and/or with the nucleic acid encoding the antigen- binding molecule or antigen-binding fragment thereof.