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Cell Rep Med . An updated atlas of antibody evasion by SARS-CoV-2 Omicron sub-variants including BQ.1.1 and XBB

tetano

Editor, Senior Moderator
Cell Rep Med


. 2023 Mar 21;100991.
doi: 10.1016/j.xcrm.2023.100991. Online ahead of print.
An updated atlas of antibody evasion by SARS-CoV-2 Omicron sub-variants including BQ.1.1 and XBB


Qingwen He[SUP] 1 [/SUP], Lili Wu[SUP] 2 [/SUP], Zepeng Xu[SUP] 3 [/SUP], Xiaoyun Wang[SUP] 3 [/SUP], Yufeng Xie[SUP] 4 [/SUP], Yan Chai[SUP] 2 [/SUP], Anqi Zheng[SUP] 2 [/SUP], Jianjie Zhou[SUP] 2 [/SUP], Shitong Qiao[SUP] 2 [/SUP], Min Huang[SUP] 5 [/SUP], Guijun Shang[SUP] 6 [/SUP], Xin Zhao[SUP] 2 [/SUP], Youjun Feng[SUP] 7 [/SUP], Jianxun Qi[SUP] 8 [/SUP], George Fu Gao[SUP] 9 [/SUP], Qihui Wang[SUP] 10 [/SUP]



Affiliations

Abstract

Emerging Omicron sub-variants are causing global concerns, and their immune evasion should be monitored continuously. We previously evaluated the escape of Omicron BA.1, BA.1.1, BA.2, and BA.3 from an atlas of 50 monoclonal antibodies (mAbs), covering seven epitope classes of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) receptor-binding domain (RBD). Here, we update the atlas of totally 77 mAbs against emerging sub-variants including BQ.1.1 and XBB and find that BA.4/5, BQ.1.1, and XBB display further evasion. Besides, investigation into the correlation of binding and neutralization of mAbs reveals the important role of antigenic conformation in mAb functioning. Moreover, the complex structures of BA.2 RBD/BD-604/S304 and BA.4/5 RBD/BD-604/S304/S309 further elucidate the molecular mechanism of antibody evasion by these sub-variants. By focusing on the identified broadly potent mAbs, we find a general hotspot epitope on the RBD, which could guide the design of vaccines and calls for new broad-spectrum countermeasures against COVID-19.

Keywords: BA.2.13; BA.2.75; BA.4; BA.5; BQ.1.1; Omicron BA.2.12.1; SARS-CoV-2; XBB; human neutralizing antibodies; immune escape.
 
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