Characterization of neutralizing antibodies from a SARS-CoV-2 infected individual

B cells specific for the SARS-CoV-2 S envelope glycoprotein spike were isolated from a COVID-19-infected subject using a stabilized spike-derived ectodomain (S2P) twenty-one days post-infection. Forty-four S2P-specific monoclonal antibodies were generated, three of which bound to the receptor bindin...

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Published inbioRxiv
Main Authors Seydoux, Emilie, Homad, Leah J, MacCamy, Anna J, Parks, K Rachael, Hurlburt, Nicholas K, Jennewein, Madeleine F, Akins, Nicholas R, Stuart, Andrew B, Wan, Yu-Hsin, Feng, Junli, Nelson, Rachael E, Singh, Suruchi, Cohen, Kristen W, McElrath, M Juliana, Englund, Janet A, Chu, Helen Y, Pancera, Marie, McGuire, Andrew T, Stamatatos, Leonidas
Format Journal Article Paper
LanguageEnglish
Published United States Cold Spring Harbor Laboratory 12.05.2020
Edition1.1
Subjects
Immunology
COVID-19
receptor binding domain
SARS-CoV-2
antibody
neutralization
spike protein
SARS
B cells
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Summary:B cells specific for the SARS-CoV-2 S envelope glycoprotein spike were isolated from a COVID-19-infected subject using a stabilized spike-derived ectodomain (S2P) twenty-one days post-infection. Forty-four S2P-specific monoclonal antibodies were generated, three of which bound to the receptor binding domain (RBD). The antibodies were minimally mutated from germline and were derived from different B cell lineages. Only two antibodies displayed neutralizing activity against SARS-CoV-2 pseudo-virus. The most potent antibody bound the RBD in a manner that prevented binding to the ACE2 receptor, while the other bound outside the RBD. Our study indicates that the majority of antibodies against the viral envelope spike that were generated during the first weeks of COVID-19 infection are non-neutralizing and target epitopes outside the RBD. Antibodies that disrupt the SARS-CoV-2 spike-ACE2 interaction can potently neutralize the virus without undergoing extensive maturation. Such antibodies have potential preventive/therapeutic potential and can serve as templates for vaccine-design.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Working Paper/Pre-Print-1
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Competing Interest Statement: The authors have declared no competing interest.
ISSN:2692-8205
2692-8205
DOI:10.1101/2020.05.12.091298