| Literature DB >> 33910569 |
Lin Cheng1, Shuo Song1, Bing Zhou1, Xiangyang Ge1, Jiazhen Yu1, Mingxia Zhang1, Bin Ju2,3,4,5, Zheng Zhang6,7,8,9.
Abstract
The emergence and rapid spread of the B.1.1.7 lineage (VOC-202012/01) SARS-CoV-2 variant has aroused global concern. The N501Y substitution is the only mutation in the interface between the RBD of B.1.1.7 and ACE2, raising concerns that its recognition by neutralizing antibodies may be affected. Here, we assessed the neutralizing activity and binding affinity of a panel of 12 monoclonal antibodies against the wild type and N501Y mutant SARS-CoV-2 pseudovirus and RBD protein, respectively. We found that the neutralization activity and binding affinity of most detected antibodies (10 out of 12) were unaffected, although the N501Y substitution decreased the neutralizing and binding activities of CB6 and increased that of BD-23. These findings could be of value in the development of therapeutic antibodies.Entities:
Keywords: Binding kinetics; Monoclonal neutralizing antibody; N501Y variant; Neutralizing activity; SARS-CoV-2
Year: 2021 PMID: 33910569 DOI: 10.1186/s12985-021-01554-8
Source DB: PubMed Journal: Virol J ISSN: 1743-422X Impact factor: 4.099