Journal
SCIENCE
Volume 372, Issue 6546, Pages 1108-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abg5268
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Funding
- Military Infectious Diseases Research Program [14066041]
- NIH [P41-GM103311]
- University of Texas College of Natural Sciences
- Cancer Prevention and Research Institute of Texas (CPRIT) [RR160023]
- Clayton Foundation
- National Institutes of Health (NIH)-National Institute of Allergy and Infectious Diseases (NIAID) [R01-AI127521]
- Welch Foundation [F-0003-19620604, F-1016]
- NIH NCI COVID-19 SeroNet grant [U54-CA260543]
- UT System Proteomics Network pilot funding
- NIH NIAID [75N93019C00050]
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The study found that in convalescent individuals from COVID-19, the IgG antibodies primarily target epitopes outside the receptor binding domain (RBD) in the spike glycoprotein. It also revealed a protective NTD antibody and an NTD epitope that is recurrently mutated in emerging SARS-CoV-2 variants.
The molecular composition and binding epitopes of the immunoglobulin G (IgG) antibodies that circulate in blood plasma after severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection are unknown. Proteomic deconvolution of the IgG repertoire to the spike glycoprotein in convalescent subjects revealed that the response is directed predominantly (>80%) against epitopes residing outside the receptor binding domain (RBD). In one subject, just four IgG lineages accounted for 93.5% of the response, including an amino (N)-terminal domain (NTD)-directed antibody that was protective against lethal viral challenge. Genetic, structural, and functional characterization of a multidonor class of public antibodies revealed an NTD epitope that is recurrently mutated among emerging SARS-CoV-2 variants of concern. These data show that public NTD-directed and other non-RBD plasma antibodies are prevalent and have implications for SARS-CoV-2 protection and antibody escape.
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