期刊
CELL REPORTS
卷 33, 期 3, 页码 -出版社
CELL PRESS
DOI: 10.1016/j.celrep.2020.108274
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资金
- NIH [R00 AI139445]
- Bill and Melinda Gates Foundation [OPP1170236, OPP1111923, OPP1132237, INV-002022]
- NIH HIV Vaccine Research and Design (HIVRAD) grant [P01 AI110657]
- AMC Fellowship
- Vici grant from the Netherlands Organisation for Scientific Research (NWO)
- U.S. Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences [DE-AC0276SF00515]
- DOE Office of Biological and Environmental Research
- NIH National Institute of General Medical Sciences [P41GM103393]
- Bill and Melinda Gates Foundation [OPP1111923, INV-002022] Funding Source: Bill and Melinda Gates Foundation
IGHV3-53-encoded neutralizing antibodies are commonly elicited during SARS-CoV-2 infection and target the receptor-binding domain (RBD) of the spike (S) protein. Such IGHV3-53 antibodies generally have a short CDR H3 because of structural constraints in binding the RBD (mode A). However, a small subset of IGHV3-53 antibodies to the RBD contain a longer CDR H3. Crystal structures of two IGHV3-53 neutralizing antibodies here demonstrate that a longer CDR H3 can be accommodated in a different binding mode (mode B). These two classes of IGHV3-53 antibodies both target the ACE2 receptor binding site, but with very different angles of approach and molecular interactions. Overall, these findings emphasize the versatility of IGHV3-53 in this common anti- body response to SARS-CoV-2, where conserved IGHV3-53 germline-encoded features can be combined with very different CDR H3 lengths and light chains for SARS-CoV-2 RBD recognition and virus neutralization.
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