The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants
Issued Date
2022-01-12
Resource Type
ISSN
19313128
eISSN
19346069
Scopus ID
2-s2.0-85121345277
Pubmed ID
34921776
Journal Title
Cell Host and Microbe
Volume
30
Issue
1
Start Page
53
End Page
68.e12
Rights Holder(s)
SCOPUS
Bibliographic Citation
Cell Host and Microbe Vol.30 No.1 (2022) , 53-68.e12
Suggested Citation
Liu C., Zhou D., Nutalai R., Duyvesteyn H.M.E., Tuekprakhon A., Ginn H.M., Dejnirattisai W., Supasa P., Mentzer A.J., Wang B., Case J.B., Zhao Y., Skelly D.T., Chen R.E., Johnson S.A., Ritter T.G., Mason C., Malik T., Temperton N., Paterson N.G., Williams M.A., Hall D.R., Clare D.K., Howe A., Goulder P.J.R., Fry E.E., Diamond M.S., Mongkolsapaya J., Ren J., Stuart D.I., Screaton G.R. The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants. Cell Host and Microbe Vol.30 No.1 (2022) , 53-68.e12. 68.e12. doi:10.1016/j.chom.2021.11.013 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/87534
Title
The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants
Author(s)
Liu C.
Zhou D.
Nutalai R.
Duyvesteyn H.M.E.
Tuekprakhon A.
Ginn H.M.
Dejnirattisai W.
Supasa P.
Mentzer A.J.
Wang B.
Case J.B.
Zhao Y.
Skelly D.T.
Chen R.E.
Johnson S.A.
Ritter T.G.
Mason C.
Malik T.
Temperton N.
Paterson N.G.
Williams M.A.
Hall D.R.
Clare D.K.
Howe A.
Goulder P.J.R.
Fry E.E.
Diamond M.S.
Mongkolsapaya J.
Ren J.
Stuart D.I.
Screaton G.R.
Zhou D.
Nutalai R.
Duyvesteyn H.M.E.
Tuekprakhon A.
Ginn H.M.
Dejnirattisai W.
Supasa P.
Mentzer A.J.
Wang B.
Case J.B.
Zhao Y.
Skelly D.T.
Chen R.E.
Johnson S.A.
Ritter T.G.
Mason C.
Malik T.
Temperton N.
Paterson N.G.
Williams M.A.
Hall D.R.
Clare D.K.
Howe A.
Goulder P.J.R.
Fry E.E.
Diamond M.S.
Mongkolsapaya J.
Ren J.
Stuart D.I.
Screaton G.R.
Author's Affiliation
Other Contributor(s)
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 recognize a neutralizing epitope conserved between SARS-CoV-1 and -2, while 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.