KR20230150184A - SARS-CoV-2 스파이크 단백질에 결합하는 단일 도메인 항체 - Google Patents

SARS-CoV-2 스파이크 단백질에 결합하는 단일 도메인 항체 Download PDF

Info

Publication number
KR20230150184A
KR20230150184A KR1020227041509A KR20227041509A KR20230150184A KR 20230150184 A KR20230150184 A KR 20230150184A KR 1020227041509 A KR1020227041509 A KR 1020227041509A KR 20227041509 A KR20227041509 A KR 20227041509A KR 20230150184 A KR20230150184 A KR 20230150184A
Authority
KR
South Korea
Prior art keywords
seq
cdr3
cdr2
ser
cdr1
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Pending
Application number
KR1020227041509A
Other languages
English (en)
Korean (ko)
Inventor
젠둥 훠
레이먼드 오웬스
제임스 네이스미스
데이비드 스튜어트
Original Assignee
더 로잘린드 프랭클린 인스티튜트
다이아몬드 라이트 소스 리미티드
옥스포드 유니버시티 이노베이션 리미티드
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Priority claimed from GBGB2006589.2A external-priority patent/GB202006589D0/en
Priority claimed from GBGB2010861.9A external-priority patent/GB202010861D0/en
Application filed by 더 로잘린드 프랭클린 인스티튜트, 다이아몬드 라이트 소스 리미티드, 옥스포드 유니버시티 이노베이션 리미티드 filed Critical 더 로잘린드 프랭클린 인스티튜트
Publication of KR20230150184A publication Critical patent/KR20230150184A/ko
Pending legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/08—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from viruses
    • C07K16/10—RNA viruses
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
    • G01N33/56983—Viruses
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
    • A61P31/12—Antivirals
    • A61P31/14—Antivirals for RNA viruses
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/08—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from viruses
    • C07K16/10—RNA viruses
    • C07K16/102—Coronaviridae (F)
    • C07K16/104—Severe acute respiratory syndrome coronavirus 2 [SARS‐CoV‐2]
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
    • C07K2317/22—Immunoglobulins specific features characterized by taxonomic origin from camelids, e.g. camel, llama or dromedary
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
    • C07K2317/33—Crossreactivity, e.g. for species or epitope, or lack of said crossreactivity
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
    • C07K2317/35—Valency
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
    • C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
    • C07K2317/565—Complementarity determining region [CDR]
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
    • C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
    • C07K2317/567—Framework region [FR]
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
    • C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
    • C07K2317/569—Single domain, e.g. dAb, sdAb, VHH, VNAR or nanobody®
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
    • C07K2317/64—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising a combination of variable region and constant region components
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
    • C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
    • C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/005—Assays involving biological materials from specific organisms or of a specific nature from viruses
    • G01N2333/08—RNA viruses
    • G01N2333/165—Coronaviridae, e.g. avian infectious bronchitis virus
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2469/00—Immunoassays for the detection of microorganisms
    • G01N2469/10—Detection of antigens from microorganism in sample from host

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Virology (AREA)
  • Immunology (AREA)
  • Molecular Biology (AREA)
  • Medicinal Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Biochemistry (AREA)
  • Biomedical Technology (AREA)
  • Hematology (AREA)
  • Urology & Nephrology (AREA)
  • Animal Behavior & Ethology (AREA)
  • Veterinary Medicine (AREA)
  • Public Health (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Communicable Diseases (AREA)
  • Oncology (AREA)
  • Microbiology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Biophysics (AREA)
  • Genetics & Genomics (AREA)
  • Cell Biology (AREA)
  • Biotechnology (AREA)
  • Tropical Medicine & Parasitology (AREA)
  • Food Science & Technology (AREA)
  • Physics & Mathematics (AREA)
  • Analytical Chemistry (AREA)
  • General Physics & Mathematics (AREA)
  • Pathology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Mycology (AREA)
  • Epidemiology (AREA)
  • Peptides Or Proteins (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
KR1020227041509A 2020-05-04 2021-05-04 SARS-CoV-2 스파이크 단백질에 결합하는 단일 도메인 항체 Pending KR20230150184A (ko)

Applications Claiming Priority (5)

Application Number Priority Date Filing Date Title
GBGB2006589.2A GB202006589D0 (en) 2020-05-04 2020-05-04 Single domain antibodies
GB2006589.2 2020-05-04
GBGB2010861.9A GB202010861D0 (en) 2020-07-14 2020-07-14 Single domain antibodies
GB2010861.9 2020-07-14
PCT/GB2021/051069 WO2021224606A1 (en) 2020-05-04 2021-05-04 Single domain antibodies binding to sars-cov-2 spike protein

Publications (1)

Publication Number Publication Date
KR20230150184A true KR20230150184A (ko) 2023-10-30

Family

ID=75977769

Family Applications (1)

Application Number Title Priority Date Filing Date
KR1020227041509A Pending KR20230150184A (ko) 2020-05-04 2021-05-04 SARS-CoV-2 스파이크 단백질에 결합하는 단일 도메인 항체

Country Status (7)

Country Link
US (1) US20230348572A1 (https=)
EP (1) EP4146689A1 (https=)
JP (1) JP2023524573A (https=)
KR (1) KR20230150184A (https=)
AU (1) AU2021269176A1 (https=)
CA (1) CA3177766A1 (https=)
WO (1) WO2021224606A1 (https=)

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2023104933A1 (en) * 2021-12-07 2023-06-15 new/era/mabs GmbH Camelid antibodies for use in therapy and diagnosis
EP4194054A1 (en) * 2021-12-07 2023-06-14 new/era/mabs GmbH Camelid antibodies for use in therapy and diagnosis
CN114478757B (zh) * 2022-03-31 2022-07-05 深圳市人民医院 靶向新冠病毒的纳米抗体及其制备方法和应用
CN114736293B (zh) * 2022-06-14 2022-09-02 中国农业科学院生物技术研究所 SARS-CoV-2中和性纳米抗体、自组装铁蛋白融合纳米抗体及制备方法和应用
WO2025147701A1 (en) * 2024-01-07 2025-07-10 Abalone Bio, Inc. Cannabinoid receptor type 2 antibodies and uses thereof
WO2026006639A1 (en) * 2024-06-26 2026-01-02 Rutgers, The State University Of New Jersey Antigen binding molecules targeting transferrin receptor 1
GB202413879D0 (en) 2024-09-20 2024-11-06 Rosalind Franklin Inst Single domain antibodies

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN111333722A (zh) 2020-03-03 2020-06-26 江苏省疾病预防控制中心(江苏省公共卫生研究院) SARS-CoV-2抑制剂及其应用
CN114163523B (zh) 2020-03-17 2023-07-18 北京凯因科技股份有限公司 一种针对新型冠状病毒的单域抗体及其应用
CN111647076B (zh) 2020-04-27 2021-02-26 南京医科大学 抗新型冠状病毒SARS-Cov-2的中和性单域抗体及其应用

Non-Patent Citations (63)

* Cited by examiner, † Cited by third party
Title
Adams, M. L., Katz, D. L. & Grandpre, J. Population-Based Estimates of Chronic Conditions Affecting Risk for Complications from Coronavirus Disease, United States. Emerg Infect Dis 26, (2020).
Asarnow, D., Palovcak, E. & Cheng, Y. UCSF pyem v0.5. Zenodo. https://doi.org/10.5281/zenodo.3576630 (2019).
Bloch, E. M. et al. Deployment of convalescent plasma for the prevention and treatment of COVID-19. J Clin Invest 130, 2757-2765 (2020).
Burnley, T., Palmer, C. M. & Winn, M. Recent developments in the CCP-EM software suite. Acta Crystallogr D Struct Biol 73, 469-477 (2017).
Caly, L. et al. Isolation and rapid sharing of the 2019 novel coronavirus (SARS-CoV-2) from the first patient diagnosed with COVID-19 in Australia. Med J Aust 212, 459-462 (2020).
Chanier, T. & Chames, P. Nanobody Engineering: Toward Next Generation Immunotherapies and Immunoimaging of Cancer. Antibodies (Basel) 8, 13 (2019).
Chi, X. et al. Humanized Single Domain Antibodies Neutralize SARS-CoV-2 by Targeting Spike Receptor Binding Domain. bioRxiv (2020).
Davis, I. W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35, W375-83 (2007).
de Madrid, A. T. & Porterfield, J. S. A simple micro-culture method for the study of group B arboviruses. Bulletin of the World Health Organization 40, 113 (1969).
Docherty, A. B. et al. Features of 20 133 UK patients in hospital with covid-19 using the ISARIC WHO Clinical Characterisation Protocol: prospective observational cohort study. BMJ 369, (2020).
Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Struct Biol 60, 2126-2132 (2004).
Gallivan, J. P. & Dougherty, D. A. Cation-pi interactions in structural biology. Proc Natl Acad Sci U S A 96, 9459-9464 (1999).
Hanke, L. et al. An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction. Biochem Biophys Acta BioRxiv, (2020).
Hoffmann, M. et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell 181, 271-280.e8 (2020).
Huo, J. et al. Neutralization of SARS-CoV-2 by destruction of the prefusion Spike. Cell Host & Microbe Online, https://doi.org/10.1016/j.chom.2020.06.010 (2020).
Jaiswal, N. K. & Saxena, S. K. in Medical Virology: From Pathogenesis to Disease Control: Coronavirus Disease 2019 (COVID-19) 141-150 (Springer Singapore, Singapore, 2020).
Jakobi, A. J., Wilmanns, M. & Sachse, C. Model-based local density sharpening of cryo-EM maps. Elife 6, (2017).
Johnson, R. M., Dahlgren, L., Siegfried, B. D. & Ellis, M. D. Acaricide, fungicide and drug interactions in honey bees (Apis mellifera). PLoS One 8, e54092 (2013).
Joosten, R. P., Long, F., Murshudov, G. N. & Perrakis, A. The PDB_REDO server for macromolecular structure model optimization. IUCrJ 1, 213-220 (2014).
Jovcevska, I. & Muyldermans, S. The Therapeutic Potential of Nanobodies. BioDrugs 34, 11-26 (2020).
Kim, A. S., Leaman, D. P. & Zwick, M. B. Antibody to gp41 MPER alters functional properties of HIV-1 Env without complete neutralization. PLoS Pathog 10, e1004271 (2014).
Klarenbeek, A. et al. Camelid Ig V genes reveal significant human homology not seen in therapeutic target genes, providing for a powerful therapeutic antibody platform. MAbs 7, 693-706 (2015).
Kovalevskiy, O., Nicholls, R. A., Long, F., Carlon, A. & Murshudov, G. N. Overview of refinement procedures within REFMAC5: utilizing data from different sources. Acta Crystallogr D Struct Biol 74, 215-227 (2018).
Krissinel, E. & Henrick, K. Detection of protein assemblies in crystals. CompLife 3695, 163-174 (2005).
Kucharski, A. J. et al. Early dynamics of transmission and control of COVID-19: a mathematical modelling study. Lancet Infect Dis 20, 553-558 (2020).
Lan, J. et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature 581, 215-220 (2020).
Laskowski, R. A. & Swindells, M. B. LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J Chem Inf Model 51, 2778-2786 (2011).
Li, F. Structure, Function, and Evolution of Coronavirus Spike Proteins. Annu Rev Virol 3, 237-261 (2016).
Li, F., Li, W., Farzan, M. & Harrison, S. C. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science 309, 1864-1868 (2005).
Liebschner, D. et al. Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Acta Crystallogr D Struct Biol 75, 861-877 (2019).
Mair-Jenkins, J. et al. The effectiveness of convalescent plasma and hyperimmune immunoglobulin for the treatment of severe acute respiratory infections of viral etiology: a systematic review and exploratory meta-analysis. J Infect Dis 211, 80-90 (2015).
McCoy, A. J. et al. Phaser crystallographic software. J Appl Crystallogr 40, 658-674 (2007).
Menachery, V. D. et al. A SARS-like cluster of circulating bat coronaviruses shows potential for human emergence. Nat Med 21, 1508-1513 (2015).
Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67, 355-367 (2011).
Painter, J. & Merritt, E. A. TLSMD web server for the generation of multi-group TLS models. J Appl Crystallogr. 39, 109-111 (2006).
Pettersen, E. F. et al. UCSF chimera - A visualization system for exploratory research and analysis. J. Comp.l Chem, 25, 1605-1612 (2004).
Peyvandi, F. et al. Caplacizumab reduces the frequency of major thromboembolic events, exacerbations and death in patients with acquired thrombotic thrombocytopenic purpura. J Thromb Haemost 15, 1448-1452 (2017).
Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat Methods 14, 290-296 (2017).
Richard, G. et al. In vivo neutralization of α-cobratoxin with high-affinity llama single-domain antibodies (VHHs) and a VHH-Fc antibody. PLoS One 8, e69495 (2013).
Ronco, C., Reis, T. & Husain-Syed, F. Management of acute kidney injury in patients with COVID-19. Lancet Resp. Med. 1-5 (2020).
Salje, H. et al. Estimating the burden of SARS-CoV-2 in France. Science (2020).
Schmitz, K. R., Bagchi, A., Roovers, R. C., van Bergen en Henegouwen, P. M. & Ferguson, K. M. Structural evaluation of EGFR inhibition mechanisms for nanobodies/VHH domains. Structure 21, 1214-1224 (2013).
Shang, J. et al. Structural basis of receptor recognition by SARS-CoV-2. Nature 581, 221-224 (2020).
Shen, C. et al. Treatment of 5 Critically Ill Patients With COVID-19 With Convalescent Plasma. JAMA 323, 1582-1589 (2020).
Slifka, M. K. & Amanna, I. J. Passive immunization. Plotkin's Vaccines, 7th Edition 8, 84-95 (2018).
Song, W., Gui, M., Wang, X. & Xiang, Y. Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. PLoS Pathog 14, e1007236 (2018).
Suits, M. D., Sperandeo, P., Deho, G., Polissi, A. & Jia, Z. Novel structure of the conserved gram-negative lipopolysaccharide transport protein A and mutagenesis analysis. J Mol Biol 380, 476-488 (2008).
Tian, X. et al. Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody. Emerg Microbes Infect 9, 382-385 (2020).
Vincke, C. et al. General strategy to humanize a camelid single-domain antibody and identification of a universal humanized nanobody scaffold. J Biol Chem 284, 3273-3284 (2009).
Wagner, T. et al. SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM. Commun Biol 2, 218 (2019).
Walls, A. C. et al. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell 181, 281-292.e6 (2020).
Wan, Y., Shang, J., Graham, R., Baric, R. S. & Li, F. Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus. J Virol 94, e00127-20 (2020).
Wang, C. et al. A human monoclonal 1 antibody blocking SARS-CoV-2 infection. Nature Comms 11, 2251 (2020).
Winarski, K. L. et al. Antibody-dependent enhancement of influenza disease promoted by increase in hemagglutinin stem flexibility and virus fusion kinetics. Proc Natl Acad Sci U S A 116, 15194-15199 (2019).
Winter, G. xia2: an expert system for macromolecular crystallography data reduction. J Appl Crystallogr 43, 186-190 (2009).
Winter, G., Lobley, C. M. & Prince, S. M. Decision making in xia2. Acta Crystallogr D Biol Crystallogr 69, 1260-1273 (2013).
Wrapp, D. et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science 367, 1260-1263 (2020).
Wrapp, D. et al. Structural Basis for Potent Neutralization of Betacoronaviruses by Single-domain Camelid Antibodies. Cell 181, 1436-1441 (2020).
Yan, R. et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science 367, 1444-1448 (2020).
Yuan, M. et al. A highly conserved cryptic epitope in the receptor-binding domains of SARS-CoV-2 and SARS-CoV. Science 368, 630-633 (2020).
Zhou, P. et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 579, 270-273 (2020).
Zhu, Z. et al. Potent cross-reactive neutralization of SARS coronavirus isolates by human monoclonal antibodies. Proc Natl Acad Sci U S A 104, 12123-12128 (2007).
Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. Elife 7, (2018).

Also Published As

Publication number Publication date
AU2021269176A8 (en) 2022-12-08
AU2021269176A1 (en) 2022-11-24
US20230348572A1 (en) 2023-11-02
CA3177766A1 (en) 2021-11-11
JP2023524573A (ja) 2023-06-12
WO2021224606A1 (en) 2021-11-11
EP4146689A1 (en) 2023-03-15

Similar Documents

Publication Publication Date Title
Dejnirattisai et al. The antigenic anatomy of SARS-CoV-2 receptor binding domain
Dang et al. An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections
Huo et al. Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2
Huo et al. A potent SARS-CoV-2 neutralising nanobody shows therapeutic efficacy in the Syrian golden hamster model of COVID-19
KR20230150184A (ko) SARS-CoV-2 스파이크 단백질에 결합하는 단일 도메인 항체
Rossey et al. Potent single-domain antibodies that arrest respiratory syncytial virus fusion protein in its prefusion state
CN112390879B (zh) 靶向SARS-CoV-2的抗体及其制备方法和应用
US20240043507A1 (en) Antibodies
JP2025515237A (ja) Ｓａｒｓ－ｃｏｖ－２を標的とする抗原結合分子
EP4230650B1 (en) Antibodies capable of binding to the spike protein of coronavirus sars-cov-2
WO2022241200A1 (en) Cross-reactive coronavirus antibodies
US20250154231A1 (en) Antibodies capable of binding to the spike protein of cononavirus sars-cov-2
Liu et al. Broadly neutralizing antibodies derived from the earliest COVID-19 convalescents protect mice from SARS-CoV-2 variants challenge
Cornish et al. Structural and functional characterization of nanobodies that neutralize Omicron variants of SARS-CoV-2
Abu-Shmais et al. A potently neutralizing and protective human antibody targeting antigenic site V on RSV and hMPV fusion glycoprotein
Huo et al. Structural characterisation of a nanobody derived from a naïve library that neutralises SARS-CoV-2
WO2024209076A1 (en) Combined antibodies against sarbecoviruses and uses thereof
Li et al. Function and structure of broadly neutralizing antibodies against SARS-CoV-2 Omicron variants isolated from prototype strain infected convalescents
Addetia et al. Potent neutralization of Marburg virus by a vaccine-elicited antibody
CN116867801A (zh) 与SARS-CoV-2刺突蛋白结合的单域抗体
Zhou et al. Antigenic landscape of Nipah virus attachment glycoprotein analysis reveals a protective immunodominant epitope across species
US20240401239A1 (en) Synthetic humanized llama nanobody library and use thereof to identify sars-cov-2 neutralizing antibodies
HK40098138A (en) Antibodies capable of binding to the spike protein of coronavirus sars-cov-2
HK40098138B (en) Antibodies capable of binding to the spike protein of coronavirus sars-cov-2
Naismith et al. Structural and functional characterization of nanobodies that neutralize Omicron variants of SARS-CoV-2

Legal Events

Date Code Title Description
PA0105 International application

St.27 status event code: A-0-1-A10-A15-nap-PA0105

T11-X000 Administrative time limit extension requested

St.27 status event code: U-3-3-T10-T11-oth-X000

T11-X000 Administrative time limit extension requested

St.27 status event code: U-3-3-T10-T11-oth-X000

T11-X000 Administrative time limit extension requested

St.27 status event code: U-3-3-T10-T11-oth-X000

T11-X000 Administrative time limit extension requested

St.27 status event code: U-3-3-T10-T11-oth-X000

T11-X000 Administrative time limit extension requested

St.27 status event code: U-3-3-T10-T11-oth-X000

T11-X000 Administrative time limit extension requested

St.27 status event code: U-3-3-T10-T11-oth-X000

T11-X000 Administrative time limit extension requested

St.27 status event code: U-3-3-T10-T11-oth-X000

P11-X000 Amendment of application requested

St.27 status event code: A-2-2-P10-P11-nap-X000

P13-X000 Application amended

St.27 status event code: A-2-2-P10-P13-nap-X000

PG1501 Laying open of application

St.27 status event code: A-1-1-Q10-Q12-nap-PG1501

PN2301 Change of applicant

St.27 status event code: A-3-3-R10-R13-asn-PN2301

St.27 status event code: A-3-3-R10-R11-asn-PN2301

PN2301 Change of applicant

St.27 status event code: A-3-3-R10-R13-asn-PN2301

St.27 status event code: A-3-3-R10-R11-asn-PN2301

N231 Notification of change of applicant
PN2301 Change of applicant

St.27 status event code: A-3-3-R10-R13-asn-PN2301

St.27 status event code: A-3-3-R10-R11-asn-PN2301

E13-X000 Pre-grant limitation requested

St.27 status event code: A-2-3-E10-E13-lim-X000

P11-X000 Amendment of application requested

St.27 status event code: A-2-2-P10-P11-nap-X000

P13-X000 Application amended

St.27 status event code: A-2-2-P10-P13-nap-X000

PA0201 Request for examination

St.27 status event code: A-1-2-D10-D11-exm-PA0201

R18-X000 Changes to party contact information recorded

St.27 status event code: A-3-3-R10-R18-oth-X000

P22-X000 Classification modified

St.27 status event code: A-2-2-P10-P22-nap-X000

P22-X000 Classification modified

St.27 status event code: A-2-2-P10-P22-nap-X000