Abstract：Abstract: The spike glycoprotein (S protein) on the surface of the severe acute respiratory syndrome coro-navirus 2 (SARS-CoV-2) recognizes and binds to the host cell surface receptor angiotensin-converting en-zyme 2 (ACE2) through its receptor binding domain (RBD), but the effect of mutations in the S protein RBD on its interaction with the receptor is unclear. Through molecular docking and protein binding analysis of S protein and ACE2, this study found that, compared with the wild-type, the strains of both 501Y and B.1.617 lineages displayed more stable receptor-binding ability. Among the variants, 501Y.V1 was proved to be the most stable strain. At the RBD-ACE2 binding interface, 18% of single amino acid mutations in RBD could enhance the stability of the RBD-ACE2 complex. Knowing about the receptor-binding information of SARS-CoV-2 spike variants would be helpful in designing neutralizing antibodies and vaccines against the viral infection.
引用本文:
马学婧, 李俊甫, 张兆英, 白 静, 李 末. SARS-CoV-2刺突糖蛋白突变体与血管紧张素转化酶2结合的热点残基分析[J]. 生命科学研究, 2022, 26(2): 131-138.
MA Xue-jing, LI Jun-fu, ZHANG Zhao-ying, BAI Jing, LI Mo. Analysis of Effects of Spike Hotspot Residues on Binding Stability of SARS-CoV-2 Variants with ACE2. Life Science Research, 2022, 26(2): 131-138.
