Human antibody recognition and neutralization mode on the NTD and RBD domains of SARS-CoV-2 spike protein.

Humans Spike Glycoprotein, Coronavirus / chemistry COVID-19 Leukocytes, Mononuclear Antibodies, Viral SARS-CoV-2 Antibodies, Neutralizing Antibodies, Monoclonal

Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
22 11 2022
Historique:
received: 08 08 2022
accepted: 18 11 2022
entrez: 23 11 2022
pubmed: 24 11 2022
medline: 26 11 2022
Statut: epublish

Résumé

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes coronavirus disease 2019 (COVID-19). Variants of concern (VOCs) such as Delta and Omicron have developed, which continue to spread the pandemic. It has been reported that these VOCs reduce vaccine efficacy and evade many neutralizing monoclonal antibodies (mAbs) that target the receptor binding domain (RBD) of the glycosylated spike (S) protein, which consists of the S1 and S2 subunits. Therefore, identification of optimal target regions is required to obtain neutralizing antibodies that can counter VOCs. Such regions have not been identified to date. We obtained 2 mAbs, NIBIC-71 and 7G7, using peripheral blood mononuclear cells derived from volunteers who recovered from COVID-19. Both mAbs had neutralizing activity against wild-type SARS-CoV-2 and Delta, but not Omicron. NIBIC-71 binds to the RBD, whereas 7G7 recognizes the N-terminal domain of the S1. In particular, 7G7 inhibited S1/S2 cleavage but not the interaction between the S protein and angiotensin-converting enzyme 2; it suppressed viral entry. Thus, the efficacy of a neutralizing mAb targeting inhibition of S1/2 cleavage was demonstrated. These results suggest that neutralizing mAbs targeting blockade of S1/S2 cleavage are likely to be cross-reactive against various VOCs.

Identifiants

DOI: 10.1038/s41598-022-24730-4 PMID: 36418391 PMC: PMC9684487
pubmed: 36418391
doi: 10.1038/s41598-022-24730-4
pii: 10.1038/s41598-022-24730-4
pmc: PMC9684487
doi:

Substances chimiques

spike protein, SARS-CoV-2 0
Spike Glycoprotein, Coronavirus 0
Antibodies, Viral 0
Antibodies, Neutralizing 0
Antibodies, Monoclonal 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

20120

Subventions

Organisme : Ministry of Health, Labour and Welfare
ID : 19HA1003
Organisme : Japan Society for the Promotion of Science
ID : JP20K22630
Organisme : Japan Society for the Promotion of Science
ID : JP25000013
Organisme : Japan Society for the Promotion of Science
ID : 22K07850
Organisme : Platform Project for Supporting Drug Discovery and Life Science Research (BINDS) from AMED
ID : JP21am0101117
Organisme : Cyclic Innovation for Clinical Empowerment (CiCLE) from AMED
ID : JP17pc0101020
Organisme : Moonshot Research and Development Program
ID : JPMJMS2025
Organisme : Jappan Agency for Medical Research and Development
ID : 22ek0109579s0101

Informations de copyright

© 2022. The Author(s).

Références

Signal Transduct Target Ther. 2022 Feb 9;7(1):43
pubmed: 35140198
Cell Rep. 2022 May 17;39(7):110812
pubmed: 35568025
Nature. 2022 Feb;602(7898):671-675
pubmed: 35016199
Proc Natl Acad Sci U S A. 2012 Jun 5;109(23):9047-52
pubmed: 22615367
Protein Sci. 2021 Jan;30(1):70-82
pubmed: 32881101
Cell Mol Immunol. 2020 Jun;17(6):647-649
pubmed: 32313207
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
pubmed: 20383002
Nat Protoc. 2006;1(6):2856-60
pubmed: 17406544
Biomed Pharmacother. 2020 Sep;129:110337
pubmed: 32534226
Nat Methods. 2017 Apr;14(4):331-332
pubmed: 28250466
Nature. 2014 May 1;509(7498):55-62
pubmed: 24590074
Science. 2020 Dec 18;370(6523):1464-1468
pubmed: 33184236
Life Sci Alliance. 2020 Jul 23;3(9):
pubmed: 32703818
J Hum Genet. 2020 Dec;65(12):1075-1082
pubmed: 32699345
Cell Mol Immunol. 2021 Jun;18(6):1562-1564
pubmed: 33958745
Inflamm Res. 2020 Nov;69(11):1077-1085
pubmed: 32767095
Nat Med. 2022 Jun;28(6):1297-1302
pubmed: 35322239
Commun Biol. 2022 Jul 6;5(1):669
pubmed: 35794202
Sci Rep. 2021 Jun 9;11(1):12134
pubmed: 34108521
Nature. 2020 Jul;583(7815):290-295
pubmed: 32422645
Mol Cell. 2020 May 21;78(4):779-784.e5
pubmed: 32362314
J Comput Chem. 2004 Oct;25(13):1605-12
pubmed: 15264254
PLoS One. 2017 Dec 11;12(12):e0189453
pubmed: 29228045
J Struct Biol. 2015 Nov;192(2):216-21
pubmed: 26278980
Cell. 2021 Apr 29;184(9):2316-2331.e15
pubmed: 33773105
Commun Biol. 2021 Sep 7;4(1):1044
pubmed: 34493805
Bioinformatics. 2020 Mar 1;36(6):1731-1739
pubmed: 31873728
Nat Methods. 2015 May;12(5):380-1
pubmed: 25924071
Pharmacol Ther. 2022 Jun 20;240:108233
pubmed: 35738431
Sci Rep. 2021 Nov 16;11(1):22341
pubmed: 34785706
J Struct Biol. 2005 Oct;152(1):36-51
pubmed: 16182563
Vaccines (Basel). 2021 Mar 05;9(3):
pubmed: 33807818
Cell. 2021 Jun 24;184(13):3452-3466.e18
pubmed: 34139176
Nucleic Acids Res. 2018 Jul 2;46(W1):W296-W303
pubmed: 29788355
Biochem J. 2021 Dec 22;478(24):4169-4185
pubmed: 34783343
Signal Transduct Target Ther. 2021 Jun 9;6(1):226
pubmed: 34108440

Auteurs

Ryota Otsubo (R)

Laboratory of Infectious Diseases and Immunity, Center for Vaccine and Adjuvant Research (CVAR), National Institutes of Biomedical Innovation, Health and Nutrition (NIBIOHN), 7-6-8 Saito-Asagi, Ibaraki, Osaka, 567-0085, Japan.

Takeharu Minamitani (T)

Laboratory of Infectious Diseases and Immunity, Center for Vaccine and Adjuvant Research (CVAR), National Institutes of Biomedical Innovation, Health and Nutrition (NIBIOHN), 7-6-8 Saito-Asagi, Ibaraki, Osaka, 567-0085, Japan.
Toyama Prefectural Institute for Pharmaceutical Research, 17-1 Nakataikoyama, Imizu, Toyama, 939-0363, Japan.

Kouji Kobiyama (K)

Division of Vaccine Science, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo, 108-8639, Japan.
Laboratory of Adjuvant Innovation, CVAR, NIBIOHN, 7-6-8 Saito-Asagi, Ibaraki, Osaka, 567-0085, Japan.

Junso Fujita (J)

Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka, 565-0871, Japan.

Toshihiro Ito (T)

Laboratory of Proteome Research, NIBIOHN, 7-6-8 Saito-Asagi, Ibaraki, Osaka, 567-0085, Japan.
Laboratory of Experimental Immunology, Department of Regeneration Science and Engineering, Institute for Life and Medical Sciences, Kyoto University, 53 Shogoin Kawahara-cho, Sakyo-ku, Kyoto, 606-8507, Japan.

Shiori Ueno (S)

Department of Infectious Diseases and Host Defense, Graduate School of Medicine, Gunma University, 3-39-22 Syowa-cho, Maebashi, Gunma, 371-8511, Japan.

Itsuki Anzai (I)

Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.

Hiroki Tanino (H)

Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka, 565-0871, Japan.

Hiroshi Aoyama (H)

Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka, 565-0871, Japan.

Yoshiharu Matsuura (Y)

Centre for Infectious Disease Education and Research, Osaka University, 2-8 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Laboratory of Virus Control, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.

Keiichi Namba (K)

Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
JEOL YOKOGUSHI Research Alliance Laboratories, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
RIKEN SPring-8 Center, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.

Ken-Ichi Imadome (KI)

Department of Advanced Medicine for Infections, National Center for Child Health and Development (NCCHD), 2-10-1 Okura, Setagaya-ku, Tokyo, 157-8535, Japan.

Ken J Ishii (KJ)

Division of Vaccine Science, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo, 108-8639, Japan.
Laboratory of Adjuvant Innovation, CVAR, NIBIOHN, 7-6-8 Saito-Asagi, Ibaraki, Osaka, 567-0085, Japan.

Kouhei Tsumoto (K)

Center for Drug Discovery Research (CDDR), National Institutes of Biomedical Innovation, Health and Nutrition (NIBIOHN), 7-6-8 Saito-Asagi, Ibaraki, Osaka, 567-0085, Japan.
Department of Bioengineering, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8656, Japan.
Medical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo, 108-8639, Japan.

Wataru Kamitani (W)

Department of Infectious Diseases and Host Defense, Graduate School of Medicine, Gunma University, 3-39-22 Syowa-cho, Maebashi, Gunma, 371-8511, Japan.

Teruhito Yasui (T)

Laboratory of Infectious Diseases and Immunity, Center for Vaccine and Adjuvant Research (CVAR), National Institutes of Biomedical Innovation, Health and Nutrition (NIBIOHN), 7-6-8 Saito-Asagi, Ibaraki, Osaka, 567-0085, Japan. tyasui@nibiohn.go.jp.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female

Evaluation of Low-Value Services Across Major Medicare Advantage Insurers and Traditional Medicare.

Ciara Duggan, Adam L Beckman, Ishani Ganguli et al.
1.00
Humans United States Aged Cross-Sectional Studies Medicare Part C

Effectiveness of Virtual Yoga for Chronic Low Back Pain: A Randomized Clinical Trial.

Hallie Tankha, Devyn Gaskins, Amanda Shallcross et al.
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH

Recherchemedicale.com › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Human antibody recognition and neutralization...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Protéines virales › Protéines virales structurales › Protéines de l'enveloppe virale › Protéines de fusion virale › Glycoprotéine de spicule des coronavirus › Human antibody recognition and neutralization...
Recherchemedicale.com › Maladies de l'appareil respiratoire › Infections de l'appareil respiratoire › Pneumopathie infectieuse › Pneumopathie virale › COVID-19 › Human antibody recognition and neutralization...
Recherchemedicale.com › Systèmes sanguin et immunitaire › Système immunitaire › Leucocytes › Agranulocytes › Human antibody recognition and neutralization...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Globulines › Sérum-globulines › Immunoglobulines › Anticorps › Anticorps antiviraux › Human antibody recognition and neutralization...
Recherchemedicale.com › Virus › Virus à ARN › Virus à ARN à brin positif › Nidovirales › Coronaviridae › Coronavirus › Betacoronavirus › Virus du SRAS › SARS-CoV-2 › Human antibody recognition and neutralization...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Globulines › Sérum-globulines › Immunoglobulines › Anticorps › Anticorps neutralisants › Human antibody recognition and neutralization...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Globulines › Sérum-globulines › Immunoglobulines › Anticorps › Anticorps monoclonaux › Human antibody recognition and neutralization...