A Fusion Peptide in the Spike Protein of MERS Coronavirus
Identifieur interne : 000744 ( Main/Exploration ); précédent : 000743; suivant : 000745A Fusion Peptide in the Spike Protein of MERS Coronavirus
Auteurs : Entedar A. J. Alsaadi [Royaume-Uni] ; Benjamin W. Neuman [États-Unis] ; Ian M. Jones [Royaume-Uni]Source :
- Viruses [ 1999-4915 ] ; 2019.
Abstract
Coronaviruses represent current and emerging threats for many species, including humans. Middle East respiratory syndrome-related coronavirus (MERS-CoV) is responsible for sporadic infections in mostly Middle Eastern countries, with occasional transfer elsewhere. A key step in the MERS-CoV replication cycle is the fusion of the virus and host cell membranes mediated by the virus spike protein, S. The location of the fusion peptide within the MERS S protein has not been precisely mapped. We used isolated peptides and giant unilamellar vesicles (GUV) to demonstrate membrane binding for a peptide located near the N-terminus of the S2 domain. Key residues required for activity were mapped by amino acid replacement and their relevance in vitro tested by their introduction into recombinant MERS S protein expressed in mammalian cells. Mutations preventing membrane binding in vitro also abolished S-mediated syncytium formation consistent with the identified peptide acting as the fusion peptide for the S protein of MERS-CoV.
Url:
DOI: 10.3390/v11090825
PubMed: 31491938
PubMed Central: 6784214
Affiliations:
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J." last="Alsaadi">Entedar A. J. Alsaadi</name><affiliation wicri:level="1"><nlm:aff id="af1-viruses-11-00825">School of Biological Sciences, University of Reading, Reading RG6 6AJ, UK</nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Reading, Reading RG6 6AJ</wicri:regionArea><wicri:noRegion>Reading RG6 6AJ</wicri:noRegion></affiliation></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W." last="Neuman">Benjamin W. Neuman</name><affiliation wicri:level="2"><nlm:aff id="af2-viruses-11-00825">Biology Department, CASE, Texas A&M University, Texarkana, TX 75503, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biology Department, CASE, Texas A&M University, Texarkana, TX 75503</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author><author><name sortKey="Jones, Ian M" sort="Jones, Ian M" uniqKey="Jones I" first="Ian M." last="Jones">Ian M. Jones</name><affiliation wicri:level="1"><nlm:aff id="af1-viruses-11-00825">School of Biological Sciences, University of Reading, Reading RG6 6AJ, UK</nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Reading, Reading RG6 6AJ</wicri:regionArea><wicri:noRegion>Reading RG6 6AJ</wicri:noRegion></affiliation></author></analytic><series><title level="j">Viruses</title><idno type="eISSN">1999-4915</idno><imprint><date when="2019">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Coronaviruses represent current and emerging threats for many species, including humans. Middle East respiratory syndrome-related coronavirus (MERS-CoV) is responsible for sporadic infections in mostly Middle Eastern countries, with occasional transfer elsewhere. A key step in the MERS-CoV replication cycle is the fusion of the virus and host cell membranes mediated by the virus spike protein, S. The location of the fusion peptide within the MERS S protein has not been precisely mapped. We used isolated peptides and giant unilamellar vesicles (GUV) to demonstrate membrane binding for a peptide located near the N-terminus of the S2 domain. Key residues required for activity were mapped by amino acid replacement and their relevance in vitro tested by their introduction into recombinant MERS S protein expressed in mammalian cells. Mutations preventing membrane binding in vitro also abolished S-mediated syncytium formation consistent with the identified peptide acting as the fusion peptide for the S protein of MERS-CoV.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Coleman, C M" uniqKey="Coleman C">C.M. Coleman</name></author><author><name sortKey="Frieman, M B" uniqKey="Frieman M">M.B. 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