The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike

The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike

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Summary: The 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 infe...

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Main Authors: Yu Li, Ziding Zhang, Li Yang, Xianyi Lian, Yan Xie, Shen Li, Shuyu Xin, Pengfei Cao, Jianhong Lu
Format: Article
Language:English
Published: Elsevier 2020-06-01
Series:iScience
Subjects:
Virology
Molecular Structure
Crystallography
Online Access:http://www.sciencedirect.com/science/article/pii/S258900422030345X
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spelling doaj-a6e48d446cf542be81e848bc1580d9c52020-11-25T03:05:49ZengElsevieriScience2589-00422020-06-01236101160The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 SpikeYu Li0Ziding Zhang1Li Yang2Xianyi Lian3Yan Xie4Shen Li5Shuyu Xin6Pengfei Cao7Jianhong Lu8State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing 100193, ChinaState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing 100193, ChinaDepartment of Hematology, Xiangya Hospital, Central South University, Changsha 410080, China; Department of Microbiology, School of Basic Medical Science, Central South University, Changsha 410078, China; China-Africa Research Center of Infectious Diseases, Central South University, Changsha 410013, ChinaState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing 100193, ChinaDepartment of Hematology, Xiangya Hospital, Central South University, Changsha 410080, China; Department of Microbiology, School of Basic Medical Science, Central South University, Changsha 410078, ChinaDepartment of Hematology, Xiangya Hospital, Central South University, Changsha 410080, China; Department of Microbiology, School of Basic Medical Science, Central South University, Changsha 410078, ChinaDepartment of Hematology, Xiangya Hospital, Central South University, Changsha 410080, China; Department of Microbiology, School of Basic Medical Science, Central South University, Changsha 410078, China; China-Africa Research Center of Infectious Diseases, Central South University, Changsha 410013, ChinaDepartment of Hematology, Xiangya Hospital, Central South University, Changsha 410080, ChinaDepartment of Hematology, Xiangya Hospital, Central South University, Changsha 410080, China; Department of Microbiology, School of Basic Medical Science, Central South University, Changsha 410078, China; China-Africa Research Center of Infectious Diseases, Central South University, Changsha 410013, China; Corresponding authorSummary: The 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.http://www.sciencedirect.com/science/article/pii/S258900422030345XVirologyMolecular StructureCrystallography
collection DOAJ
language English
format Article
sources DOAJ
author Yu Li
Ziding Zhang
Li Yang
Xianyi Lian
Yan Xie
Shen Li
Shuyu Xin
Pengfei Cao
Jianhong Lu
spellingShingle Yu Li
Ziding Zhang
Li Yang
Xianyi Lian
Yan Xie
Shen Li
Shuyu Xin
Pengfei Cao
Jianhong Lu
The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike
iScience
Virology
Molecular Structure
Crystallography
author_facet Yu Li
Ziding Zhang
Li Yang
Xianyi Lian
Yan Xie
Shen Li
Shuyu Xin
Pengfei Cao
Jianhong Lu
author_sort Yu Li
title The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike
title_short The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike
title_full The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike
title_fullStr The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike
title_full_unstemmed The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike
title_sort mers-cov receptor dpp4 as a candidate binding target of the sars-cov-2 spike
publisher Elsevier
series iScience
issn 2589-0042
publishDate 2020-06-01
description Summary: The 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.
topic Virology
Molecular Structure
Crystallography
url http://www.sciencedirect.com/science/article/pii/S258900422030345X
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