Liu, Chang, Zhou, Daming, Nutalai, Rungtiwa, Duyvesteyn, Helen M.E., Tuekprakhon, Aekkachai, Ginn, Helen M., Dejnirattisai, Wanwisa, Supasa, Piyada, Mentzer, Alexander J., Wang, Beibei, and others. (2021) The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants. Cell Host & Microbe, . ISSN 1931-3128. E-ISSN 1934-6069. (doi:10.1016/j.chom.2021.11.013) (KAR id:91956)
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Official URL: https://doi.org/10.1016/j.chom.2021.11.013 |
Abstract
Alpha-B.1.1.7, Beta-B.1.351, Gamma-P.1 and Delta-B.1.617.2 variants of SARS-CoV-2 express multiple mutations in the spike protein (S). These may alter the antigenic structure of S, causing escape from natural or vaccine-induced immunity. Beta is particularly difficult to neutralize using serum induced by early pandemic SARS-CoV-2 strains and is most antigenically separated from Delta. To understand this, we generated 674 mAbs from Beta infected individuals and performed a detailed structure-function analysis of the 27 most potent mAbs: one binding the spike N-terminal domain (NTD), the rest the receptor binding domain (RBD). Two of these RBD-binding mAbs recognise a neutralizing epitope conserved between SARS-CoV-1 and -2, whilst 18 target mutated residues in Beta: K417N, E484K, and N501Y. There is a major response to N501Y including a public IgVH4-39 sequence, with E484K and K417N also targeted. Recognition of these key residues underscores why serum from Beta cases poorly neutralizes early pandemic and Delta viruses.
Item Type: | Article |
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DOI/Identification number: | 10.1016/j.chom.2021.11.013 |
Subjects: | Q Science > QR Microbiology > QR355 Virology |
Divisions: | Divisions > Division of Natural Sciences > Medway School of Pharmacy |
Depositing User: | Nigel Temperton |
Date Deposited: | 02 Dec 2021 22:26 UTC |
Last Modified: | 03 Dec 2021 11:45 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/91956 (The current URI for this page, for reference purposes) |
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