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Structural insights into the binding of SARS-CoV-2, SARS-CoV, and hCoV-NL63 spike receptor-binding domain to horse ACE2

Structure. 2022-08; 
Jun Lan, Peng Chen, Weiming Liu, Wenlin Ren, Linqi Zhang, Qiang Ding, Qi Zhang, Xinquan Wang, Jiwan Ge
Products/Services Used Details Operation
Gene Synthesis … This special case reminds us that in addition to the direct interacting regions, attention … The cDNA of ACE2 orthologs, each with a C-terminal FLAG-tag, were synthesized by GenScript Get A Quote

摘要

Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV-2, and human coronavirus (hCoV)-NL63 utilize ACE2 as the functional receptor for cell entry, which leads to zoonotic infection. Horses (Equus caballus) attracted our attention because the spike protein receptor-binding domains (RBDs) of SARS-CoV-2 and SARS-CoV-2-related coronaviruses bind equine ACE2 (eACE2) with high affinity. Here we show that eACE2 binds the RBDs of these three coronaviruses and also SARS-CoV-2 variants but with lower affinities compared with human ACE2 (hACE2). Structural analysis and mutation assays indicated that eACE2-H41 accounts for the lower binding affinity of eACE2 to the RBDs of SARS-CoV-2 variants (Alpha, Beta, and... More

关键词

ACE2, SARS-CoV, SARS-CoV-2, complex structure, hCoV-NL63, horse, pseudovirus infection, receptor binding domain