Structure-based analyses of neutralization antibodies interacting with naturally occurring SARS-CoV-2 RBD variants
Dear Editor,
SARS-CoV-2 variants are developing rapidly among COVID-19 patients,likely resulting in higher transmissibility at the population level.1-5 Mutations in the spike proteins (S proteins) of these variants are supposed to be related with receptor binding and virus invasion.Examples of these prevalent variants include the B.1.1.7 lineage that emerged in the United Kingdom (UK),the B.1.351 lineage (also termed 501Y.V2) in South Africa (SA),and the P.1 and P.2 lineages in Brazil,etc.Many S protein alterations,especially in the receptor binding domain (RBD),characterize these variants,e.g.,the N501Y mutation in B.1.351 and the K417N (or T)/E484K/N501Y co-mutation in the SA and Brazil variant.2,3,s The RBD is responsible for interacting with mammalian receptor angiotensin-converting enzyme 2 (ACE2) to mediate the viral infection of host cells.It is also concentrated with epitopes for neutralizing antibodies (NAbs),thus playing a vital role in the study of prophylactics and therapeutics for COVID-19.6-10 Whether those RBD mutations may alter virus-host cell interactions and gain resistance to NAbs needs to be addressed.
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We thank the National Center for Protein Sciences at Peking University in Beijing,China,for assistance with SPR assay;We thank the staff of the Shanghai Synchrotron Radiation Facility ;We thank the KEK Photon Factory ;We thank the Core Facilities at the School of Life Sciences,Peking University,for help with negative-staining EM;This project was supported by the Ministry of Science and Technology of China ;This project was also supported by the Beijing Science and Technology Project ;the National Natural Science Foundation of China ;Special thanks to Drs;Sunney Xie,Junyu Xiao,Yunlong Cao for providing plasmids and IgG samples of the antibodies
2021-11-11（万方平台首次上网日期，不代表论文的发表时间）
共4页
1126-1129
