Polymorphisms in dipeptidyl peptidase 4 reduce host cell entry of Middle East respiratory syndrome coronavirus.
Identifieur interne : 000279 ( PubMed/Corpus ); précédent : 000278; suivant : 000280Polymorphisms in dipeptidyl peptidase 4 reduce host cell entry of Middle East respiratory syndrome coronavirus.
Auteurs : Hannah Kleine-Weber ; Simon Schroeder ; Nadine Krüger ; Alexander Prokscha ; Hassan Y. Naim ; Marcel A. Müller ; Christian Drosten ; Stefan Pöhlmann ; Markus HoffmannSource :
- Emerging microbes & infections [ 2222-1751 ] ; 2020.
Abstract
Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) causes a severe respiratory disease in humans. The MERS-CoV spike (S) glycoprotein mediates viral entry into target cells. For this, MERS-CoV S engages the host cell protein dipeptidyl peptidase 4 (DPP4, CD26) and the interface between MERS-CoV S and DPP4 has been resolved on the atomic level. Here, we asked whether naturally-occurring polymorphisms in DPP4, that alter amino acid residues required for MERS-CoV S binding, influence cellular entry of MERS-CoV. By screening of public databases, we identified fourteen such polymorphisms. Introduction of the respective mutations into DPP4 revealed that all except one (Δ346-348) were compatible with robust DPP4 expression. Four polymorphisms (K267E, K267N, A291P and Δ346-348) strongly reduced binding of MERS-CoV S to DPP4 and S protein-driven host cell entry, as determined using soluble S protein and S protein bearing rhabdoviral vectors, respectively. Two polymorphisms (K267E and A291P) were analyzed in the context of authentic MERS-CoV and were found to attenuate viral replication. Collectively, we identified naturally-occurring polymorphisms in DPP4 that negatively impact cellular entry of MERS-CoV and might thus modulate MERS development in infected patients.
DOI: 10.1080/22221751.2020.1713705
PubMed: 31964246
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Naim</name><affiliation><nlm:affiliation>Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Hannover, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Muller, Marcel A" sort="Muller, Marcel A" uniqKey="Muller M" first="Marcel A" last="Müller">Marcel A. Müller</name><affiliation><nlm:affiliation>Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Institute of Virology, Berlin, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><affiliation><nlm:affiliation>Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Institute of Virology, Berlin, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name><affiliation><nlm:affiliation>Infection Biology Unit, German Primate Center, Göttingen, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Hoffmann, Markus" sort="Hoffmann, Markus" uniqKey="Hoffmann M" first="Markus" last="Hoffmann">Markus Hoffmann</name><affiliation><nlm:affiliation>Infection Biology Unit, German Primate Center, Göttingen, Germany.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Emerging microbes & infections</title><idno type="eISSN">2222-1751</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) causes a severe respiratory disease in humans. The MERS-CoV spike (S) glycoprotein mediates viral entry into target cells. For this, MERS-CoV S engages the host cell protein dipeptidyl peptidase 4 (DPP4, CD26) and the interface between MERS-CoV S and DPP4 has been resolved on the atomic level. Here, we asked whether naturally-occurring polymorphisms in DPP4, that alter amino acid residues required for MERS-CoV S binding, influence cellular entry of MERS-CoV. By screening of public databases, we identified fourteen such polymorphisms. Introduction of the respective mutations into DPP4 revealed that all except one (Δ346-348) were compatible with robust DPP4 expression. Four polymorphisms (K267E, K267N, A291P and Δ346-348) strongly reduced binding of MERS-CoV S to DPP4 and S protein-driven host cell entry, as determined using soluble S protein and S protein bearing rhabdoviral vectors, respectively. Two polymorphisms (K267E and A291P) were analyzed in the context of authentic MERS-CoV and were found to attenuate viral replication. Collectively, we identified naturally-occurring polymorphisms in DPP4 that negatively impact cellular entry of MERS-CoV and might thus modulate MERS development in infected patients.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">31964246</PMID><DateRevised><Year>2020</Year><Month>03</Month><Day>23</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">2222-1751</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>1</Issue><PubDate><Year>2020</Year></PubDate></JournalIssue><Title>Emerging microbes & infections</Title><ISOAbbreviation>Emerg Microbes Infect</ISOAbbreviation></Journal><ArticleTitle>Polymorphisms in dipeptidyl peptidase 4 reduce host cell entry of Middle East respiratory syndrome coronavirus.</ArticleTitle><Pagination><MedlinePgn>155-168</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/22221751.2020.1713705</ELocationID><Abstract><AbstractText>Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) causes a severe respiratory disease in humans. The MERS-CoV spike (S) glycoprotein mediates viral entry into target cells. For this, MERS-CoV S engages the host cell protein dipeptidyl peptidase 4 (DPP4, CD26) and the interface between MERS-CoV S and DPP4 has been resolved on the atomic level. Here, we asked whether naturally-occurring polymorphisms in DPP4, that alter amino acid residues required for MERS-CoV S binding, influence cellular entry of MERS-CoV. By screening of public databases, we identified fourteen such polymorphisms. Introduction of the respective mutations into DPP4 revealed that all except one (Δ346-348) were compatible with robust DPP4 expression. Four polymorphisms (K267E, K267N, A291P and Δ346-348) strongly reduced binding of MERS-CoV S to DPP4 and S protein-driven host cell entry, as determined using soluble S protein and S protein bearing rhabdoviral vectors, respectively. Two polymorphisms (K267E and A291P) were analyzed in the context of authentic MERS-CoV and were found to attenuate viral replication. Collectively, we identified naturally-occurring polymorphisms in DPP4 that negatively impact cellular entry of MERS-CoV and might thus modulate MERS development in infected patients.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kleine-Weber</LastName><ForeName>Hannah</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Infection Biology Unit, German Primate Center, Göttingen, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Faculty of Biology and Psychology, University Göttingen, Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schroeder</LastName><ForeName>Simon</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Institute of Virology, Berlin, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Krüger</LastName><ForeName>Nadine</ForeName><Initials>N</Initials><Identifier Source="ORCID">0000-0002-4413-8699</Identifier><AffiliationInfo><Affiliation>Institute of Virology, University of Veterinary Medicine Hannover, Hannover, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Research Center for Emerging Infections and Zoonoses, University of Veterinary Medicine Hannover, Hannover, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prokscha</LastName><ForeName>Alexander</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Hannover, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Naim</LastName><ForeName>Hassan Y</ForeName><Initials>HY</Initials><Identifier Source="ORCID">0000-0003-4884-8425</Identifier><AffiliationInfo><Affiliation>Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Hannover, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Müller</LastName><ForeName>Marcel A</ForeName><Initials>MA</Initials><Identifier Source="ORCID">0000-0003-2242-5117</Identifier><AffiliationInfo><Affiliation>Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Institute of Virology, Berlin, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>German Centre for Infection Research, associated partner Charité, Berlin, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Martsinovsky Institute of Medical Parasitology, Tropical and Vector Borne Diseases, Sechenov University, Moscow, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Drosten</LastName><ForeName>Christian</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Institute of Virology, Berlin, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>German Centre for Infection Research, associated partner Charité, Berlin, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pöhlmann</LastName><ForeName>Stefan</ForeName><Initials>S</Initials><Identifier Source="ORCID">0000-0001-6086-9136</Identifier><AffiliationInfo><Affiliation>Infection Biology Unit, German Primate Center, Göttingen, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Faculty of Biology and Psychology, University Göttingen, Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hoffmann</LastName><ForeName>Markus</ForeName><Initials>M</Initials><Identifier Source="ORCID">0000-0003-4603-7696</Identifier><AffiliationInfo><Affiliation>Infection Biology Unit, German Primate Center, 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