CN115137806B - Use of rhizoma Polygonati lectin in blocking invasion and infection of novel coronavirus - Google Patents
Use of rhizoma Polygonati lectin in blocking invasion and infection of novel coronavirus Download PDFInfo
- Publication number
- CN115137806B CN115137806B CN202110342884.9A CN202110342884A CN115137806B CN 115137806 B CN115137806 B CN 115137806B CN 202110342884 A CN202110342884 A CN 202110342884A CN 115137806 B CN115137806 B CN 115137806B
- Authority
- CN
- China
- Prior art keywords
- protein
- lectin
- rhizoma polygonati
- infection
- virus
- 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.)
- Active
Links
Images
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/168—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K36/00—Medicinal preparations of undetermined constitution containing material from algae, lichens, fungi or plants, or derivatives thereof, e.g. traditional herbal medicines
- A61K36/18—Magnoliophyta (angiosperms)
- A61K36/88—Liliopsida (monocotyledons)
- A61K36/896—Liliaceae (Lily family), e.g. daylily, plantain lily, Hyacinth or narcissus
- A61K36/8969—Polygonatum (Solomon's seal)
-
- 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
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Natural Medicines & Medicinal Plants (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Virology (AREA)
- Botany (AREA)
- Epidemiology (AREA)
- Immunology (AREA)
- Gastroenterology & Hepatology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Alternative & Traditional Medicine (AREA)
- Biotechnology (AREA)
- Medical Informatics (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Organic Chemistry (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Abstract
The invention discloses a rhizoma polygonati lectinPolygonatum cyrtonemaHuaLecin) protein, in the preparation of medicines for resisting novel coronavirus. The antiviral experiment shows that the rhizoma polygonati lectin protein can effectively block the infection of novel coronaviruses on VERO cells, and the antiviral capability of the protein is greatly reduced or even lost after mannose is added to seal the binding site of the rhizoma polygonati lectin protein. Therefore, the rhizoma polygonati lectin protein can be used as an active ingredient for preparing the novel coronavirus-resistant medicament, and the specific application is that a proper amount of pharmaceutically acceptable matrix or auxiliary materials can be added, and the novel coronavirus-resistant medicament can also be combined with a proper medicament for application.
Description
Technical Field
The invention belongs to the field of biological medicine, and in particular relates to a novel blocking method for blocking SRAS-CoV-2 invasive infection by utilizing polygonatum lectin protein.
Background
The respiratory disease-2019 coronavirus disease (COVID-19) caused by the novel coronavirus (SARS-CoV-2) is the most troublesome public health problem worldwide at present, and seriously jeopardizes human health and world economic and social development. Currently, global scientists are actively developing vaccines and new coronavirus medicines aiming at the novel coronavirus, and a plurality of vaccines are put into use in the global at present, but the protection effect of the vaccines is still to be tested.
The novel coronaviruses have mainly four structural proteins, namely two membrane proteins, namely, spinous process (or spike) glycoprotein (S protein), small envelope glycoprotein (E, protein) and membrane glycoprotein (M protein) which are highly exposed on the virus surface, and nucleocapsid protein (N protein). The infectivity of SARS-CoV-2 virus is mainly determined by S protein, it is combined with the membrane receptor of host cell to mediate the fusion of virus and cell membrane, and angiotensin converting enzyme 2 (ACE 2) widely distributed on the epithelial cell membrane of host nasal cavity, lung, small intestine and other organs is the main receptor of S protein.
Studies have shown that the highly exposed spike protein (S protein) on the viral surface is the most major weapon for virus to invade the body and is the key part of virus attachment and infection of host cells, and that by forming homotrimers, the S protein forms distinct spikes on the viral surface, mediating membrane fusion and viral entry into cells. Wherein the receptor Recognition Binding Domain (RBD) of the S protein is critical for its binding to ACE2 (Wrapp, D).et al.Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.Science367, 1260-1263). Given that the S protein plays an indispensable role in viral invasion and infection, the recognition and binding of the S protein to ACE2 trigger the viral infection host cell, so that the interruption or interference of the interaction of the S protein of spinous process with ACE2 in any way is crucial for controlling viral invasion, which is the main strategy for the design of medicines such as vaccines and neutralizing antibodies at present. Therefore, the design of S protein targeting drugs and vaccines becomes the most important direction of SARS-CoV-2 preventive and therapeutic drug development, and peptide fragments (skeletons) of specific parts of S protein polypeptide chains, especially key peptide fragments of RBD targeting parts, are the most main targets of current vaccine design, neutralizing antibodies and other drug development.
The S protein of SARS-CoV-2 is a highly glycosylated glycoprotein, each S protein monomer comprising at least 22N-linked sugar chains, trimersThe S protein has at least 66 glycosylation sites, and a large number of mannose-oligosaccharide type, high mannose type and mannose-containing complex type sugar chains (Zhang, Y) are attached to the surface.et al.Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins.Molecular&cellular proteomics : MCP20, 100058). This means that the new coronavirus is a so-called "sugar-coated virus", in which so many glycosylation sites are linked to a large number of polysaccharide chains as if the surface were covered with a thick "sugar chain barrier" or "sugar shield". While this layer is in a dynamic, floating indefinite "sugar chain barrier" covering more than 90% of the viral surface area (Casalino, L).et al.Beyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein.ACS central science6, 1722-1734) may present difficulties in the development of vaccines and targeted drugs. Antibodies produced by targeted drugs or injected vaccines often have difficulty entering the interior through the surface layer coated with a thick sugar coating to bind to the target peptide backbone. Meanwhile, sugar chains which float in a swimming way can shield and even hide the binding site of an antibody or a drug, so that the antibody and the drug cannot recognize the target site, thereby being difficult to play the role of the antibody and the drug, and further causing immune escape and drug off-target. The research shows that the sugar chains of the glycosylation sites N165 and N234 of the S protein can stabilize the open conformation of the S protein, thereby promoting the combination of RBD and ACE 2; furthermore, the sugar chains of N165, 234, 343 can also shield RBD in the closed conformation of S protein, and thus protect (Watanabe, y., allen, j.d., wrapp, d., mcLellan, j.s.&Crispin, M. Site-specific glycan analysis of the SARS-CoV-2 spike.Science369, 330-333). Therefore, the sugar chain not only protects and shields the S protein peptide chain, but also can promote the combination of virus and receptor protein, thereby promoting the occurrence of infection.
Thus, immune escape and drug off-target problems caused by the high degree of glycosylation of S protein are obstacles and challenges faced by SARS-CoV-2 vaccine and other drug development.
Aiming at the possible bottleneck problem of the research and development of the novel coronavirus drug, the vaccine design aiming at the specific part of the S protein peptide chain skeleton and the possible sugar chain trap and obstacle of the research and development of other targeted drugs at present are avoided, a novel strategy of taking the sugar chain of the S protein as the target is adopted, and the protein polypeptide compound specifically combined with the sugar chain of the S protein is used for blocking the S protein sugar chain, which is a novel "peaked soldier" of a host cell infected by the coronavirus, so as to block the identification and combination of the virus and a host cell receptor (ACE 2), and further achieve the aim of preventing and treating the virus infection. Therefore, blocking the recognition and binding of viruses and host cells by binding to the glycoprotein chains blocking the surfaces of viruses may be a strategy for effectively blocking and preventing viral infections, and thus blocking infections targeting carbohydrate chains may be a new break in drug development.
Lectins are a class of proteins or glycoproteins of non-immune origin that specifically recognize and bind to pairs of sugars and their complexes (Damme, e.j.m. v., peumans, w.j., barre, a.).&Rougé, P. Plant Lectins: A Composite of Several Distinct Families of Structurally and Evolutionary RelatedProteins with Diverse Biological Roles.Critical Reviews in Plant Sciences17, 575-692), polygonatum sibiricum lectinPolygonatum cyrtonemaHua, lectin, PCL) is a Lectin (An, J) specifically recognizing binding mannose and sialic acid isolated by the inventors from traditional chinese herbal medicines in our country.et al.Anti-HIV I/II activity and molecular cloning of a novel mannose/sialic acid-binding lectin from rhizome of Polygonatum cyrtonema Hua.Acta biochimica et biophysica Sinica38, 70-78）。
The invention detects the S protein binding activity and the SRAS-CoV-2 antiviral activity of the rhizoma polygonati lectin (PCL), discovers that the rhizoma polygonati lectin can specifically and efficiently bind to the S protein sugar chain, can also effectively bind to the peptide chain skeleton of the S protein, and shows the double binding property of the sugar chain and the peptide chain.
The antiviral activity experiment shows that the rhizoma polygonati lectin protein can effectively block the infection of the novel coronavirus to the VERO cells, and the antiviral capability of the lectin protein is greatly reduced or even lost after mannose is added to seal the mannose binding site of the rhizoma polygonati lectin protein. Therefore, the rhizoma polygonati lectin protein can be used as an active ingredient for preparing medicines for resisting novel coronaviruses. The invention provides possibility for a novel blocking method for blocking SRAS-CoV-2 invasion infection by utilizing the rhizoma polygonati lectin protein so as to achieve the effect of blocking and preventing virus infection.
Disclosure of Invention
The invention aims to provide a novel blocking method for blocking SRAS-CoV-2 invasive infection by utilizing rhizoma polygonati lectin protein.
It is still another object of the present invention to provide the use of the above novel blocking method for SRAS-CoV-2 invasive infection using a lectin protein of Polygonatum sibiricum.
Description of the embodiments
The aim of the invention is achieved by the following experimental scheme:
1) Obtaining an antiviral activity test substance, namely rhizoma polygonati lectin protein:
polygonatum sibiricum lectinPolygonatum cyrtonema，Preparation of the hua. Lectin, abbreviated PCL protein preparation and detection (An, J) were performed according to the method prior to the inventors' laboratory.et al.Anti-HIV I/II activity and molecular cloning of a novel mannose/sialic acid-binding lectin from rhizome of Polygonatum cyrtonema Hua.Acta biochimica et biophysica Sinica38, 70-78）。
2) The virus TCID50 (tissue half-infection) assay was performed to examine the antiviral activity of the protein sample rhizoma Polygonati lectin to be tested in step 1).
The invention has the beneficial effects that: the rhizoma polygonati raw materials and rhizoma polygonati lectin protein samples are easy to obtain, and compared with the cost required by research and development of neutralizing antibodies, recombinant vaccines, small molecular drugs and the like, the large amount of research and development time is reduced; can specifically target and bind to a plurality of oligosaccharide mannose type, high mannose type and mannose complex type sugar chains on the surface of coronavirus. The problems of virus immunogenicity inhibition and innate/acquired immune response escape caused by breaking through a large amount of sugar chains attached to the surface, antigen shielding and the like are not required to be considered in the research and the development of traditional vaccines and targeted drugs. Thereby sealing the glycoprotein chain or host cell on the surface of the virus with high efficiency, blocking the recognition and combination of the virus and the host cell, and further preventing the infection of the novel coronavirus.
Drawings
FIG. 1, (a) normal cell control, (b) SARS-CoV-2 inoculation, (c) glycoprotein addition.
FIG. 2 PCL and SARS-CoV-2 neutralization titration curves.
Detailed Description
The present invention will be described in further detail with reference to examples, but embodiments of the present invention are not limited thereto.
Example 1: separation and purification of natural rhizoma polygonati lectin (PCL)
The separation and purification method of rhizoma Polygonati lectin is disclosed in literature (Bao Jinku, zeng Zhongkui, zhouhong. Rhizoma Polygonati lectin II purification and partial property research).Journal of biochemistry, 165-170,1996). The method comprises the following steps:
1. taking fresh Polygonatum cyrtonema Fabricius tuberous stems, crushing by a high-speed tissue triturator, extracting and filtering by using normal saline, centrifuging (4 ℃ C., 45000r/min,30 min), adding ammonium sulfate into supernatant to reach 30% saturation, precipitating overnight, and centrifuging at 4 ℃ C., 6000r/min for 30min.
2. Collecting supernatant, adding ammonium sulfate to reach 80% saturation, centrifuging at 4deg.C at 6000r/min for 30min, collecting precipitate, dissolving in water, dialyzing with water, and freeze drying to obtain PCL crude product.
3. Dissolving the PCL crude product with 0.14M NaCl, performing equilibrium dialysis, centrifuging to remove insoluble substances, loading the supernatant to a porcine thyroglobulin-Sepharose 4B column (2.6X40 cm) for affinity chromatography, washing the supernatant with 0.14M NaCl until the absorbance of the effluent liquid is 280nm to be less than 0.02, eluting with 0.2M acetic acid solution at a flow rate of 20ml/h, collecting the fraction, detecting by a rabbit hemagglutination experiment, collecting the fraction with agglutination activity, dialyzing and freeze-drying.
4. PCL sample obtained by affinity chromatography is dissolved in pH4.4 and 0.02M NaAc buffer solution, and after equilibrium dialysis, the PCL sample is applied to CM-Sepharose fast column (2.6X28 CM), washed by NaAc buffer solution, subjected to linear gradient elution by NaAc buffer solution containing 0.6M NaCl, pressurized by peristaltic pump and flow rate of 3ml/min, and the fraction with agglutination activity is collected and lyophilized.
5. The above lyophilized sample was dissolved and equilibrated with Sephadex G-100 (1.6X100 cm) using 0.14M NaCl, followed by molecular sieve chromatographic purification of PCL. The flow rate is 12ml/h, the II activity peak is collected after the detection of the ultraviolet and the coagulation activity, and the PCL pure product is obtained after dialysis and desalination and freeze drying.
Example 2: virus infection experiment of Vero cells
1. Cell preparation: 100 μl Vero E6 cells were seeded in 96-well plates, with a cell number of about 8×103 to 1×104 per well. 97% MEM medium (GIBCO, cat. No. 12800017, naHCO3 added at 1.5 g/L); 3% fetal bovine serum; 5% CO 2 The method comprises the steps of carrying out a first treatment on the surface of the Culturing at 37 ℃. The cells were plated in a monolayer per well, approximately 60% abundance to inoculate the virus.
2. Preparation of diluted virus liquid: the dilution fold was determined based on the approximate titer of the virus. Viral stock was diluted in an EP tube to X concentrations (10 -1 ，10 -2 …10 -10 Etc.).
3. Inoculating: the cell culture plates were removed, the culture medium in the 96-well plates was aspirated with a lance, the incubation was gently applied once per well, and then the incubation was aspirated (this step was aimed at removing serum, as serum could interfere with virus adsorption). 100 μl of virus dilution was added per well, 3 replicates of each concentration, and two additional rows of no virus added were left as negative controls. 37 ℃,5% CO 2 The incubator was incubated for 3 days. Incubation is carried out for 1h in a CO2 incubator at 37 ℃, the 96-well plate is taken out to suck the virus liquid, and the culture is continued in the incubator for 3 days after 200 mu l of culture medium is added.
4. Measurement results
The plates were removed and cytopathic effect was observed under a microscope, with normal cells shown in FIG. 1 (a), and infected cells shown in Table 1 and FIG. 1 (b).
The calculation method comprises the following steps:
1) Spearman-Karber method
LgCCID50 /0.2ml= - （X0 - d/2 + d×∑R1/N1）
X0=log of lowest dilution of total lesions
d = logarithm of dilution factor
N1=number of wells per dilution
R1=lesion number
Sigma = product and
LgCCID50 /ml = LgCCID50 /0.2ml +0.7
2) Reed-Muench method
CPE (cytopathic effect) was observed to find the dilution of virus that caused half of the cell flask/well infections and the TCID50 of the virus solution was calculated according to the formula, see table 1:
TABLE 1 VERO cell CPE after virus infection
(example)
Distance ratio = (percentage of disease rate higher than 50%)/(percentage of disease rate higher than 50% below 50% disease rate)
lgtcid50=distance ratio X log of dilution+log tcid50=10-X/0.1 ml of dilution above 50% disease rate
Meaning: 50% of the cells were diseased by 10X dilution and 100. Mu.l inoculation of the virus.
3) Decision criterion
The cell control was lesion-free and the number of experiments should be increased to reduce errors in the absence of standard.
Example 3: polygonatum sibiricum lectin covd-19 Virus neutralization assay
1. Cell preparation: 1 day before experiment, vero cells with good state are taken, digested and counted by pancreatin, and then are used up
Whole medium diluted cells were arranged to 1.5X10 5 Cell suspension with concentration of/mL, 100 mu L of cell suspension is added to each well of a 96-well cell culture plate, the plate is placed in a CO2 incubator for culture overnight, and before the infection experiment, the cell state is observed, if the cell state is good, the plate is washed 2-3 times with PBS, and 100 mu L of maintenance solution is added to each well.
2. PCL purity was diluted to 8. Mu.g/mL with PBS as initial concentration.
3. Sample dilution: the samples are diluted according to the double ratio, and at least two repetitions of each sample are needed in a 96-well U-shaped plate, so that each well to be measured after dilution has a volume of 40 mu L of the sample to be measured.
4. Incubation of virus with PCL samples: the virus with known TCID50 titer is diluted to 100 TCID50/35 mu L (which can be adjusted according to the experiment requirement and is partially 200 TCID50/35 mu L) by using a maintenance solution, then 35 mu L of virus dilution solution is added into each PCL sample hole, the PCL sample holes are placed in a safety cabinet for room temperature incubation for 2 h, during the period, vero cell plates are prepared, the Vero cell plates are washed twice by PBS, after the incubation is completed, the incubation mixture of the virus and the sample is measured according to 35 mu L/hole, the cells are added according to the corresponding hole, and the PCL sample holes are placed in a CO2 incubator for incubation for 2 h at 37 ℃.
5. 120 mu L of virus maintenance solution is added into each cell culture hole, and the cells are placed in a cell culture box for 3-5 days at 37 ℃ for culture, and cell CPE is observed, and the result is shown in FIG. 1 (C); plasma/serum neutralization titers, or antibody IC50 values, were calculated and the results are shown in figure 2.
Sequence listing
<110> university of Sichuan
<120> Effect of Polygonatum sibiricum lectin on blocking novel coronavirus invasion and infection
<160> 2
<170> SIPOSequenceListing 1.0
<210> 1
<211> 160
<212> PRT
<213> Polygonatum sibiricum (Polygonatum cyrtonema)
<400> 1
Met Ala Ala Ser Ser Ser Pro Ile Leu Leu Leu Met Ala Thr Ile Ala
1 5 10 15
Ile Phe Gly Leu Met Val Ala Ser Pro Cys Ala Ala Val Asn Ser Leu
20 25 30
Ser Ser Pro Asn Ser Leu Phe Thr Gly His Ser Leu Glu Val Gly Pro
35 40 45
Ser Tyr Arg Leu Ile Met Pro Gly Asp Cys Asn Phe Val Leu Tyr Asp
50 55 60
Ser Gly Lys Pro Val Trp Ala Ser Asn Thr Gly Gly Leu Gly Ser Gly
65 70 75 80
Cys Arg Leu Thr Leu His Asn Asn Gly Asn Leu Val Ile Tyr Asp Gln
85 90 95
Ser Asn Arg Val Ile Trp Gln Thr Lys Thr Asn Gly Lys Glu Asp His
100 105 110
Tyr Val Leu Val Leu Gln Gln Asp Arg Asn Val Val Ile Tyr Gly Pro
115 120 125
Val Val Trp Ala Thr Gly Ser Gly Pro Ala Val Gly Leu Thr Leu Ile
130 135 140
Pro His Asn Ala Thr Asp Ile Val His Ala Thr Pro Met Leu Asn Glu
145 150 155 160
<210> 2
<211> 396
<212> DNA
<213> Polygonatum sibiricum (Polygonatum cyrtonema)
<400> 2
gtcaattctc tgtcttcccc caacagcctc ttcaccggcc attccctcga ggtggggccc 60
tcttaccgtc tcattatgcc gggagactgc aactttgtgt tgtacgactc aggcaaacct 120
gtttgggcgt ccaacaccgg cgggctcggc agtggctgcc gcttgacgtt gcacaacaac 180
gggaacctcg tcatctacga tcagagcaac cgtgtgattt ggcagaccaa gacgaacggg 240
aaggaggacc attacgtgct ggtgctgcag caagaccgca atgtggtcat ctacggccct 300
gtagtttggg ccacaggctc tggaccggcc gtcggactca cccttattcc gcataacgct 360
actgatattg ttcatgctac accgatgctt aatgag 396
Claims (1)
1. The application of natural plant protein in preparing medicine for resisting coronavirus SARS-CoV-2 is characterized in that the protein is rhizoma polygonati lectin Polygonatum cyrtonema Hua Lectin from plant rhizoma polygonati Polygonatum cyrtonema Hua, and the nucleotide sequence of the rhizoma polygonati lectin is shown in SEQ ID NO: 2.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202110342884.9A CN115137806B (en) | 2021-03-30 | 2021-03-30 | Use of rhizoma Polygonati lectin in blocking invasion and infection of novel coronavirus |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202110342884.9A CN115137806B (en) | 2021-03-30 | 2021-03-30 | Use of rhizoma Polygonati lectin in blocking invasion and infection of novel coronavirus |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN115137806A CN115137806A (en) | 2022-10-04 |
| CN115137806B true CN115137806B (en) | 2023-07-07 |
Family
ID=83404577
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202110342884.9A Active CN115137806B (en) | 2021-03-30 | 2021-03-30 | Use of rhizoma Polygonati lectin in blocking invasion and infection of novel coronavirus |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN115137806B (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2023245415A1 (en) * | 2022-06-21 | 2023-12-28 | 四川大学 | Use of polygonatum cyrtonema hua. lectin in blocking invasion and infection of novel coronavirus |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1562351A (en) * | 2004-04-20 | 2005-01-12 | 四川大学 | Application of agglutinin II protein of rhizome of manyflower solmonaeal in pharmacy |
| CN1840174A (en) * | 2004-04-20 | 2006-10-04 | 四川大学 | Application of polygonatum cyrtonema Hua. Lectin II protein in medicine preparation for treating or preventing AIDS |
| KR100885671B1 (en) * | 2007-10-24 | 2009-02-25 | (주)풍국면 | A method for encapsulation of anti-diabetes herb mixtures |
| CN111803608A (en) * | 2020-06-01 | 2020-10-23 | 北京中医药大学 | A Chinese medicinal composition with antiviral effect |
-
2021
- 2021-03-30 CN CN202110342884.9A patent/CN115137806B/en active Active
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1562351A (en) * | 2004-04-20 | 2005-01-12 | 四川大学 | Application of agglutinin II protein of rhizome of manyflower solmonaeal in pharmacy |
| CN1840174A (en) * | 2004-04-20 | 2006-10-04 | 四川大学 | Application of polygonatum cyrtonema Hua. Lectin II protein in medicine preparation for treating or preventing AIDS |
| KR100885671B1 (en) * | 2007-10-24 | 2009-02-25 | (주)풍국면 | A method for encapsulation of anti-diabetes herb mixtures |
| CN111803608A (en) * | 2020-06-01 | 2020-10-23 | 北京中医药大学 | A Chinese medicinal composition with antiviral effect |
Non-Patent Citations (2)
| Title |
|---|
| Anita Gupta等.Status of mannose‑binding lectin (MBL) and complement system in COVID‑19 patients and therapeutic applications of antiviral plant MBLs.《Molecular and Cellular Biochemistry》.2021,第第476卷卷(第第476卷期),2917-2942页. * |
| Jie AN等.Anti-HIV I/II Activity and Molecular Cloning of a Novel Mannose/Sialic Acidbinding Lectin from Rhizome of Polygonatum cyrtonema Hua.《Acta Biochimica et Biophysica Sinica》.2006,第第38卷卷(第第38卷期),70 - 78 页. * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN115137806A (en) | 2022-10-04 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN111560074B (en) | Novel coronavirus S protein single-region subunit nano vaccine based on helicobacter pylori ferritin | |
| US20230080694A1 (en) | Method for improving antigen immunogenicity, coronavirus antigen, use thereof, recombinant vector, expression kit, transgenic cell line, recombinant bacterium, coronavirus vaccine, preparation method of antigen and nucleotide sequence | |
| CN111647048B (en) | Application of interference polypeptide in preparing anti-SARS-CoV-2 medicine | |
| Gondim et al. | Potent antiviral activity of carbohydrate-specific algal and leguminous lectins from the Brazilian biodiversity | |
| CN113512096B (en) | Weever rhabdovirus recombinant G2 protein and application thereof | |
| CN113521265B (en) | Perch rhabdovirus subunit vaccine and preparation method thereof | |
| CN115137806B (en) | Use of rhizoma Polygonati lectin in blocking invasion and infection of novel coronavirus | |
| CN113769080B (en) | Polypeptide immunoconjugates and uses thereof | |
| CN101367879A (en) | Gastrodia elata polysaccharide, its sulfating derivant, preparation and application thereof | |
| CN113372459B (en) | Oroxylum indicum polysaccharide, preparation method and application thereof | |
| CN115282259A (en) | Oral spray preparation based on virus blocking agent and application thereof | |
| CN102533677B (en) | Malaria vaccine and preparation method thereof | |
| Loffredo et al. | Antimicrobial peptides for novel antiviral strategies in the current post‐COVID‐19 pandemic | |
| Van Damme et al. | Molecular cloning of the lectin and a lectin-related protein from common Solomon's seal (Polygonatum multiflorum) | |
| CA2257943A1 (en) | Viral peptides with structural homology to protein g of respiratory syncytial virus | |
| CN116769048A (en) | Polymeric molecules, single and multiple structures including the same | |
| CN105012935A (en) | Application of IFITM3 protein loaded exosome in preparation of anti-dengue virus interferon antagonism strain infection drugs | |
| CN111073861A (en) | Human respiratory syncytial virus strain, application, antibody or hybridoma cell or antiserum | |
| CN108676074A (en) | A kind of active peptides of hepatic cell growth promotion | |
| CN102516394B (en) | CMG 2mutant and Fc fusion protein, its encoding gene and its application | |
| US12076364B2 (en) | Use of interference peptide in preparation of anti-SARS-CoV-2 medicament | |
| CN1256349C (en) | Prepn and use of curcuma oligosaccharide sulfate derivative | |
| CN115300608B (en) | Method for blocking new coronavirus infection by mannose-binding lectin | |
| CN101948439A (en) | Extraction method and application to medicine of active alkaloid compounds in cervus nippon temminck | |
| US20220323537A1 (en) | USE OF INTERFERENCE PEPTIDE IN PREPARATION OF ANTI-SARS-CoV-2 MEDICAMENT |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |