Yunjiao Zhou, Zezhong Liu, Shibo Li, Wei Xu, Qianqian Zhang, I. T. Silva, C. Li, Y. Wu, Qingling Jiang, Zhenmi Liu, Qiujing Wang, Yu Guo, Jianbo Wu, C. Gu, Xia Cai, D. Qu, C. T. Mayer, X. Wang, Shibo Jiang, T. Ying, Zhenghong Yuan, Youhua Xie, Y. Wen, L. Lu, Qiao Wang
Cell Reports, 2021
Several potent neutralizing antibodies against SARS-CoV-2 virus have been identified. However, antibody-dependent enhancement (ADE) has not been comprehensively studied for SARS-CoV-2, and the relationship between enhancing versus neutralizing activities and antibody epitopes remains unknown. Here, we select a convalescent individual with potent IgG neutralizing activity and characterize his antibody response. Monoclonal antibodies isolated from memory B cells target four groups of five non-overlapping receptor-binding domain (RBD) epitopes. Antibodies to one group of these RBD epitopes mediate ADE of entry in Raji cells via an Fcγ receptor-dependent mechanism. In contrast, antibodies targeting two other distinct epitope groups neutralize SARS-CoV-2 without ADE, while antibodies against the fourth epitope group are poorly neutralizing. One antibody, XG014, potently cross-neutralizes SARS-CoV-2 variants as well as SARS-CoV-1 with respective IC50 values as low as 5.1 ng/ml and 23.7 ng/ml, while not exhibiting ADE. Therefore, neutralization and ADE of human SARS-CoV-2 antibodies correlate with non-overlapping RBD epitopes.
Cited by 24 publications.
Field of study: Medicine