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| Item Type: | Article |
|---|---|
| Title: | SARS-CoV-2 Beta variant infection elicits potent lineage-specific and cross-reactive antibodies |
| Creators Name: | Reincke, S.M., Yuan, M., Kornau, H.C., Corman, V.M., van Hoof, S., Sánchez-Sendin, E., Ramberger, M., Yu, W., Hua, Y., Tien, H., Schmidt, M.L., Schwarz, T., Jeworowski, L.M., Brandl, S.E., Rasmussen, H.F., Homeyer, M.A., Stöffler, L., Barner, M., Kunkel, D., Huo, S., Horler, J., von Wardenburg, N., Kroidl, I., Eser, T.M., Wieser, A., Geldmacher, C., Hoelscher, M., Gänzer, H., Weiss, G., Schmitz, D., Drosten, C., Prüss, H., Wilson, I.A. and Kreye, J. |
| Abstract: | SARS-CoV-2 Beta variant of concern (VOC) resists neutralization by major classes of antibodies from COVID-19 patients and vaccinated individuals. Here, serum of Beta-infected patients revealed reduced cross-neutralization of wildtype virus. From these patients, we isolated Beta-specific and cross-reactive receptor-binding domain (RBD) antibodies. The Beta-specificity results from recruitment of VOC-specific clonotypes and accommodation of mutations present in Beta and Omicron into a major antibody class that is normally sensitive to these mutations. The Beta-elicited cross-reactive antibodies share genetic and structural features with wildtype-elicited antibodies, including a public VH1-58 clonotype targeting the RBD ridge. These findings advance our understanding of the antibody response to SARS-CoV-2 shaped by antigenic drift with implications for design of next-generation vaccines and therapeutics. |
| Keywords: | Neutralizing Antibodies, Viral Antibodies, Antigenic Drift and Shift, COVID-19, Cross Reactions, Neutralization Tests, Protein Binding, Protein Domains, Protein Interaction Domains and Motifs, SARS-CoV-2, Coronavirus Spike Glycoprotein, Coronavirus Spike Coronavirus / Metabolism |
| Source: | Science |
| ISSN: | 0036-8075 |
| Publisher: | American Association for the Advancement of Science |
| Volume: | 375 |
| Number: | 6582 |
| Page Range: | 782-787 |
| Date: | 18 February 2022 |
| Official Publication: | https://doi.org/10.1126/science.abm5835 |
| PubMed: | View item in PubMed |
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