Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular Basis of Mink ACE2 Binding to SARS-CoV-2 and Its Mink-Derived Variants.
Journal, issue, pages	J Virol, Vol. 96, Issue 17, Page e0081422, Year 2022
Publish date	Sep 14, 2022
Authors	Chao Su / Juanhua He / Pengcheng Han / Bin Bai / Dedong Li / Jian Cao / Mingxiong Tian / Yu Hu / Anqi Zheng / Sheng Niu / Qian Chen / Xiaoyu Rong / Yanfang Zhang / Weiwei Li / Jianxun Qi / Xin Zhao / Mengsu Yang / Qihui Wang / George Fu Gao /
PubMed Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is transmitted between humans and minks, and some mutations in the spike (S) protein, especially in the receptor-binding domain (RBD), ...Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is transmitted between humans and minks, and some mutations in the spike (S) protein, especially in the receptor-binding domain (RBD), have been identified in mink-derived viruses. Here, we examined binding of the mink angiotensin-converting enzyme 2 (ACE2) receptor to mink-derived and important human-originating variants, and we demonstrated that most of the RBD variants increased the binding affinities to mink ACE2 (mkACE2). Cryo-electron microscopy structures of the mkACE2-RBD Y453F (with a Y-to-F change at position 453) and mkACE2-RBD F486L complexes helped identify the key residues that facilitate changes in mkACE2 binding affinity. Additionally, the data indicated that the Y453F and F486L mutations reduced the binding affinities to some human monoclonal antibodies, and human vaccinated sera efficiently prevented infection of human cells by pseudoviruses expressing Y453F, F486L, or N501T RBD. Our findings provide an important molecular mechanism for the rapid adaptation of SARS-CoV-2 in minks and highlight the potential influence of the main mink-originating variants for humans. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a broad range of hosts. Mink-derived SARS-CoV-2 can transmit back to humans. There is an urgent need to understand the binding mechanism of mink-derived SARS-CoV-2 variants to mink receptor. In this study, we identified all mutations in the receptor-binding domain (RBD) of spike (S) protein from mink-derived SARS-CoV-2, and we demonstrated the enhanced binding affinity of mink angiotensin-converting enzyme 2 (ACE2) to most of the mink-derived RBD variants as well as important human-originating RBD variants. Cryo-electron microscopy structures revealed that the Y453F and F486L mutations enhanced the binding forces in the interaction interface. In addition, Y453F and F486L mutations reduced the binding affinities to some human monoclonal antibodies, and the SARS-CoV-2 pseudoviruses with Y453F, F486L, or N501T mutations were neutralized by human vaccinated sera. Therefore, our results provide valuable information for understanding the cross-species transmission mechanism of SARS-CoV-2.
External links	J Virol / PubMed:36000849 / PubMed Central
Methods	EM (single particle)
Resolution	2.85 - 2.9 Å
Structure data	32358 7w8s EMDB-32358, PDB-7w8s: Structure of SARS-CoV-2 spike receptor-binding domain Y453F mutation complexed with American mink ACE2 Method: EM (single particle) / Resolution: 2.85 Å 32379 7wa1 EMDB-32379, PDB-7wa1: Structure of SARS-CoV-2 spike receptor-binding domain F486L mutation complexed with American mink ACE2 Method: EM (single particle) / Resolution: 2.9 Å
Chemicals	ChemComp-ZN: Unknown entry
Source	homo sapiens (human) severe acute respiratory syndrome coronavirus 2
Keywords	VIRAL PROTEIN