National Natural Science Foundation of China (NSFC)
32022037
China
National Natural Science Foundation of China (NSFC)
81803429
China
Citation
Journal: Signal Transduct Target Ther / Year: 2022 Title: Broadly neutralizing antibodies against Omicron-included SARS-CoV-2 variants induced by vaccination. Authors: Xiangyang Chi / Yingying Guo / Guanying Zhang / Hancong Sun / Jun Zhang / Min Li / Zhengshan Chen / Jin Han / Yuanyuan Zhang / Xinghai Zhang / Pengfei Fan / Zhe Zhang / Busen Wang / Xiaodong ...Authors: Xiangyang Chi / Yingying Guo / Guanying Zhang / Hancong Sun / Jun Zhang / Min Li / Zhengshan Chen / Jin Han / Yuanyuan Zhang / Xinghai Zhang / Pengfei Fan / Zhe Zhang / Busen Wang / Xiaodong Zai / Xuelian Han / Meng Hao / Ting Fang / Jinghan Xu / Shipo Wu / Yi Chen / Yingying Fang / Yunzhu Dong / Bingjie Sun / Jinlong Zhang / Jianmin Li / Guangyu Zhao / Changming Yu / Qiang Zhou / Wei Chen / Abstract: The SARS-CoV-2 Omicron variant shows substantial resistance to neutralization by infection- and vaccination-induced antibodies, highlighting the demands for research on the continuing discovery of ...The SARS-CoV-2 Omicron variant shows substantial resistance to neutralization by infection- and vaccination-induced antibodies, highlighting the demands for research on the continuing discovery of broadly neutralizing antibodies (bnAbs). Here, we developed a panel of bnAbs against Omicron and other variants of concern (VOCs) elicited by vaccination of adenovirus-vectored COVID-19 vaccine (Ad5-nCoV). We also investigated the human longitudinal antibody responses following vaccination and demonstrated how the bnAbs evolved over time. A monoclonal antibody (mAb), named ZWD12, exhibited potent and broad neutralization against SARS-CoV-2 variants Alpha, Beta, Gamma, Kappa, Delta, and Omicron by blocking the spike protein binding to the angiotensin-converting enzyme 2 (ACE2) and provided complete protection in the challenged prophylactic and therapeutic K18-hACE2 transgenic mouse model. We defined the ZWD12 epitope by determining its structure in complex with the spike (S) protein via cryo-electron microscopy. This study affords the potential to develop broadly therapeutic mAb drugs and suggests that the RBD epitope bound by ZWD12 is a rational target for the design of a broad spectrum of vaccines.
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