| First Author | Liu C | Year | 2022 |
| Journal | Cell Host Microbe | Volume | 30 |
| Issue | 1 | Pages | 53-68.e12 |
| PubMed ID | 34921776 | Mgi Jnum | J:335926 |
| Mgi Id | MGI:6874722 | Doi | 10.1016/j.chom.2021.11.013 |
| Citation | Liu C, et al. (2022) The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants. Cell Host Microbe 30(1):53-68.e12 |
| abstractText | 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. |
