EMD-35063
The complex structure of Omicron BA.4 RBD with BD604, S309, and S304
EMD-35063
Single-particle2.36 Å
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Map released: 06/12/2023
Last modified: 23/10/2024
Sample Organism:
Homo sapiens,
Severe acute respiratory syndrome coronavirus 2
Sample: Omicron BA.4/5 RBD in complex with Fabs of BD-604, S304 and S309
Fitted models: 8hws (Avg. Q-score: 0.472)
Deposition Authors: He QW, Xu ZP, Xie YF
Sample: Omicron BA.4/5 RBD in complex with Fabs of BD-604, S304 and S309
Fitted models: 8hws (Avg. Q-score: 0.472)
Deposition Authors: He QW, Xu ZP, Xie YF
An updated atlas of antibody evasion by SARS-CoV-2 Omicron sub-variants including BQ.1.1 and XBB.
He Q,
Wu L,
Xu Z,
Wang X,
Xie Y,
Chai Y,
Zheng A,
Zhou J,
Qiao S,
Huang M,
Shang G,
Zhao X,
Feng Y,
Qi J,
Gao GF,
Wang Q
(2023) Cell Rep Med , 4 , 100991 - 100991
(2023) Cell Rep Med , 4 , 100991 - 100991
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.
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.