Autor: |
Amin Addetia, Young-Jun Park, Tyler Starr, Allison J. Greaney, Kaitlin R. Sprouse, John E. Bowen, Sasha W. Tiles, Wesley C. Van Voorhis, Jesse D. Bloom, Davide Corti, Alexandra C. Walls, David Veesler |
Jazyk: |
angličtina |
Rok vydání: |
2023 |
Předmět: |
|
Zdroj: |
Cell Reports, Vol 42, Iss 6, Pp 112621- (2023) |
Druh dokumentu: |
article |
ISSN: |
2211-1247 |
DOI: |
10.1016/j.celrep.2023.112621 |
Popis: |
Summary: Continued evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is eroding antibody responses elicited by prior vaccination and infection. The SARS-CoV-2 receptor-binding domain (RBD) E406W mutation abrogates neutralization mediated by the REGEN-COV therapeutic monoclonal antibody (mAb) COVID-19 cocktail and the AZD1061 (COV2-2130) mAb. Here, we show that this mutation remodels the receptor-binding site allosterically, thereby altering the epitopes recognized by these three mAbs and vaccine-elicited neutralizing antibodies while remaining functional. Our results demonstrate the spectacular structural and functional plasticity of the SARS-CoV-2 RBD, which is continuously evolving in emerging SARS-CoV-2 variants, including currently circulating strains that are accumulating mutations in the antigenic sites remodeled by the E406W substitution. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
|