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Yin, Wanchao; Xu, Youwei; Xu, Peiyu; Cao, Xiaodan; Wu, Canrong; Gu, Chunyin; He, Xinheng; Wang, Xiaoxi; Huang, Sijie; Yuan, Qingning; Wu, Kai; Hu, Wen; Huang, Zifu; Liu, Jia; Wang, Zongda; Jia, Fangfang; Xia, Kaiwen; Liu, Peipei; Wang, Xueping; Song, Bin; Zheng, Jie; Jiang, Hualiang; Cheng, Xi; Jiang, Yi; Deng, Su-Jun; Xu, H Eric
Science, 03/2022, Volume: 375, Issue: 6584Journal Article
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant has become the dominant infective strain. We report the structures of the Omicron spike trimer on its own and in complex with angiotensin-converting enzyme 2 (ACE2) or an anti-Omicron antibody. Most Omicron mutations are located on the surface of the spike protein and change binding epitopes to many current antibodies. In the ACE2-binding site, compensating mutations strengthen receptor binding domain (RBD) binding to ACE2. Both the RBD and the apo form of the Omicron spike trimer are thermodynamically unstable. An unusual RBD-RBD interaction in the ACE2-spike complex supports the open conformation and further reinforces ACE2 binding to the spike trimer. A broad-spectrum therapeutic antibody, JMB2002, which has completed a phase 1 clinical trial, maintains neutralizing activity against Omicron. JMB2002 binds to RBD differently from other characterized antibodies and inhibits ACE2 binding.
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