文章基本信息

标题：The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike
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作者：Yu Li ; Ziding Zhang ; Li Yang 等
期刊名称：iScience
印刷版ISSN：2589-0042
出版年度：2020
卷号：23
期号：6
页码：1-15
DOI：10.1016/j.isci.2020.101160
语种：English
出版社：Elsevier
摘要：SummaryThe ongoing outbreak of the novel coronavirus pneumonia COVID-19 has caused great number of cases and deaths, but our understanding about the pathogen SARS-CoV-2 remains largely unclear. The attachment of the virus with the cell-surface receptor and a cofactor is the first step for the infection. Here, bioinformatics approaches combining human-virus protein interaction prediction and protein docking based on crystal structures have revealed the high affinity between human dipeptidylpeptidase 4 (DPP4) and the spike (S) receptor-binding domain of SARS-CoV-2. Intriguingly, the crucial binding residues of DPP4 are identical to those that are bound to the MERS-CoV-S. Moreover, E484 insertion and adjacent substitutions should be most essential for this DPP4-binding ability acquirement of SARS-CoV-2-S compared with SARS-CoV-S. This potential utilization of DPP4 as a binding target for SARS-CoV-2 may offer novel insight into the viral pathogenesis and help the surveillance and therapeutics strategy for meeting the challenge of COVID-19.Graphical AbstractDisplay OmittedHighlights•SARS-CoV-2 spike receptor-binding domain has a potentially high affinity to DPP4•SARS-CoV-2-S/DPP4 binding shares key DPP4 residues with that of MERS-CoV-S/DPP4•E484 and adjacent mutations are critical for the DPP4-binding ability of SARS-CoV-2-SVirology; Molecular Structure; Crystallography