A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2
Identifieur interne : 002443 ( Ncbi/Merge ); précédent : 002442; suivant : 002444A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2
Auteurs : Anna-Winona Struck [Allemagne] ; Marco Axmann [Allemagne] ; Susanne Pfefferle [Allemagne] ; Christian Drosten [Allemagne] ; Bernd Meyer [Allemagne]Source :
- Antiviral Research [ 0166-3542 ] ; 2012.
Descripteurs français
- KwdFr :
- Antiviraux (pharmacologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (pharmacologie), Humains, Liaison aux protéines, Peptides (génétique), Peptides (pharmacologie), Peptidyl-Dipeptidase A (métabolisme), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (pharmacologie), Pénétration virale (), Récepteurs viraux (métabolisme), Résonance plasmonique de surface, Virus du SRAS (), Virus du SRAS (croissance et développement), Virus du SRAS (physiologie).
- MESH :
- croissance et développement : Virus du SRAS.
- génétique : Glycoprotéines membranaires, Peptides, Protéines de l'enveloppe virale.
- métabolisme : Peptidyl-Dipeptidase A, Récepteurs viraux.
- pharmacologie : Antiviraux, Glycoprotéines membranaires, Peptides, Protéines de l'enveloppe virale.
- physiologie : Virus du SRAS.
- Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Pénétration virale, Résonance plasmonique de surface, Virus du SRAS.
English descriptors
- KwdEn :
- Antiviral Agents (pharmacology), Humans, Membrane Glycoproteins (genetics), Membrane Glycoproteins (pharmacology), Peptides (genetics), Peptides (pharmacology), Peptidyl-Dipeptidase A (metabolism), Protein Binding, Receptors, Virus (metabolism), SARS Virus (drug effects), SARS Virus (growth & development), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Surface Plasmon Resonance, Viral Envelope Proteins (genetics), Viral Envelope Proteins (pharmacology), Virus Internalization (drug effects).
- MESH :
- chemical , genetics : Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- chemical , metabolism : Peptidyl-Dipeptidase A, Receptors, Virus.
- chemical , pharmacology : Antiviral Agents, Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- drug effects : SARS Virus, Virus Internalization.
- growth & development : SARS Virus.
- physiology : SARS Virus.
- Humans, Protein Binding, Spike Glycoprotein, Coronavirus, Surface Plasmon Resonance.
Abstract
► Hexapeptide YKYRYL specifically inhibits SARS infection in cells. ► Assessment of peptide libraries by SPR screening and virus proliferation assays. ► Hexapeptide YKYRYL is minimal binding epitope of SARS spike protein to ACE2. ► Characterization by SPR, STD and molecular dynamics of the binding mode of the hexapeptide.
Url:
DOI: 10.1016/j.antiviral.2011.12.012
PubMed: 22265858
PubMed Central: 7114193
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Links to Exploration step
PMC:7114193Le document en format XML
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(pharmacology)</term><term>Virus Internalization (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antiviraux (pharmacologie)</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (pharmacologie)</term><term>Humains</term><term>Liaison aux protéines</term><term>Peptides (génétique)</term><term>Peptides (pharmacologie)</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (pharmacologie)</term><term>Pénétration virale ()</term><term>Récepteurs viraux (métabolisme)</term><term>Résonance plasmonique de surface</term><term>Virus du SRAS ()</term><term>Virus du SRAS (croissance et développement)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptides</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Membrane Glycoproteins</term><term>Peptides</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Peptides</term><term>Protéines de l'enveloppe virale</term></keywords><keywords 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SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Graphical abstract</title><p><fig id="f0040" position="anchor"><graphic xlink:href="fx1"></graphic></fig></p></sec><sec><title>Highlights</title><p>► Hexapeptide YKYRYL specifically inhibits SARS infection in cells. ► Assessment of peptide libraries by SPR screening and virus proliferation assays. ► Hexapeptide YKYRYL is minimal binding epitope of SARS spike protein to ACE2. ► Characterization by SPR, STD and molecular dynamics of the binding mode of the hexapeptide.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Babcock, G J" uniqKey="Babcock G">G.J. Babcock</name></author><author><name sortKey="Esshaki, D J" uniqKey="Esshaki D">D.J. Esshaki</name></author><author><name sortKey="Thomas, W D J" uniqKey="Thomas W">W.D.J. Thomas</name></author><author><name sortKey="Ambrosino, D M" uniqKey="Ambrosino D">D.M. Ambrosino</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Dimitrov, D S" uniqKey="Dimitrov D">D.S. Dimitrov</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Drosten, C" uniqKey="Drosten C">C. Drosten</name></author><author><name sortKey="Chiu, L L" uniqKey="Chiu L">L.L. Chiu</name></author><author><name sortKey="Panning, M" uniqKey="Panning M">M. Panning</name></author><author><name sortKey="Leong, H N" uniqKey="Leong H">H.N. Leong</name></author><author><name sortKey="Preiser, W" uniqKey="Preiser W">W. Preiser</name></author><author><name sortKey="Tam, J S" uniqKey="Tam J">J.S. Tam</name></author><author><name sortKey="Gunther, S" uniqKey="Gunther S">S. 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nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Axmann, Marco" sort="Axmann, Marco" uniqKey="Axmann M" first="Marco" last="Axmann">Marco Axmann</name><affiliation wicri:level="1"><nlm:aff id="aff1">Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg</wicri:regionArea><wicri:noRegion>20359 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg</wicri:regionArea><wicri:noRegion>20359 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Meyer, Bernd" sort="Meyer, Bernd" uniqKey="Meyer B" first="Bernd" last="Meyer">Bernd Meyer</name><affiliation wicri:level="1"><nlm:aff id="aff1">Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22265858</idno><idno type="pmc">7114193</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114193</idno><idno type="RBID">PMC:7114193</idno><idno type="doi">10.1016/j.antiviral.2011.12.012</idno><date when="2012">2012</date><idno type="wicri:Area/Pmc/Corpus">000D92</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000D92</idno><idno type="wicri:Area/Pmc/Curation">000D92</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000D92</idno><idno type="wicri:Area/Pmc/Checkpoint">000A95</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000A95</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2</title><author><name sortKey="Struck, Anna Winona" sort="Struck, Anna Winona" uniqKey="Struck A" first="Anna-Winona" last="Struck">Anna-Winona Struck</name><affiliation wicri:level="1"><nlm:aff id="aff1">Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Axmann, Marco" sort="Axmann, Marco" uniqKey="Axmann M" first="Marco" last="Axmann">Marco Axmann</name><affiliation wicri:level="1"><nlm:aff id="aff1">Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg</wicri:regionArea><wicri:noRegion>20359 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg</wicri:regionArea><wicri:noRegion>20359 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Meyer, Bernd" sort="Meyer, Bernd" uniqKey="Meyer B" first="Bernd" last="Meyer">Bernd Meyer</name><affiliation wicri:level="1"><nlm:aff id="aff1">Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author></analytic><series><title level="j">Antiviral Research</title><idno type="ISSN">0166-3542</idno><idno type="eISSN">1872-9096</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Graphical abstract</title><p><fig id="f0040" position="anchor"><graphic xlink:href="fx1"></graphic></fig></p></sec><sec><title>Highlights</title><p>► Hexapeptide YKYRYL specifically inhibits SARS infection in cells. ► Assessment of peptide libraries by SPR screening and virus proliferation assays. ► Hexapeptide YKYRYL is minimal binding epitope of SARS spike protein to ACE2. ► Characterization by SPR, STD and molecular dynamics of the binding mode of the hexapeptide.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Babcock, G J" uniqKey="Babcock G">G.J. 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Huang</name></author></analytic></biblStruct></listBibl></div1></back></TEI></pmc><pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2.</title><author><name sortKey="Struck, Anna Winona" sort="Struck, Anna Winona" uniqKey="Struck A" first="Anna-Winona" last="Struck">Anna-Winona Struck</name><affiliation wicri:level="1"><nlm:affiliation>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Axmann, Marco" sort="Axmann, Marco" uniqKey="Axmann M" first="Marco" last="Axmann">Marco Axmann</name></author><author><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name></author><author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name></author><author><name sortKey="Meyer, Bernd" sort="Meyer, Bernd" uniqKey="Meyer B" first="Bernd" last="Meyer">Bernd Meyer</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22265858</idno><idno type="pmid">22265858</idno><idno type="doi">10.1016/j.antiviral.2011.12.012</idno><idno type="wicri:Area/PubMed/Corpus">001414</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001414</idno><idno type="wicri:Area/PubMed/Curation">001414</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001414</idno><idno type="wicri:Area/PubMed/Checkpoint">001393</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001393</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2.</title><author><name sortKey="Struck, Anna Winona" sort="Struck, Anna Winona" uniqKey="Struck A" first="Anna-Winona" last="Struck">Anna-Winona Struck</name><affiliation wicri:level="1"><nlm:affiliation>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Axmann, Marco" sort="Axmann, Marco" uniqKey="Axmann M" first="Marco" last="Axmann">Marco Axmann</name></author><author><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name></author><author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name></author><author><name sortKey="Meyer, Bernd" sort="Meyer, Bernd" uniqKey="Meyer B" first="Bernd" last="Meyer">Bernd Meyer</name></author></analytic><series><title level="j">Antiviral research</title><idno type="eISSN">1872-9096</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiviral Agents (pharmacology)</term><term>Humans</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (pharmacology)</term><term>Peptides (genetics)</term><term>Peptides (pharmacology)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Protein Binding</term><term>Receptors, Virus (metabolism)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (growth & development)</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Surface Plasmon Resonance</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (pharmacology)</term><term>Virus Internalization (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antiviraux (pharmacologie)</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (pharmacologie)</term><term>Humains</term><term>Liaison aux protéines</term><term>Peptides (génétique)</term><term>Peptides (pharmacologie)</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (pharmacologie)</term><term>Pénétration virale ()</term><term>Récepteurs viraux (métabolisme)</term><term>Résonance plasmonique de surface</term><term>Virus du SRAS ()</term><term>Virus du SRAS (croissance et développement)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptides</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Membrane Glycoproteins</term><term>Peptides</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Peptides</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term><term>Glycoprotéines membranaires</term><term>Peptides</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Protein Binding</term><term>Spike Glycoprotein, Coronavirus</term><term>Surface Plasmon Resonance</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Liaison aux protéines</term><term>Pénétration virale</term><term>Résonance plasmonique de surface</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In vitro infection of Vero E6 cells by SARS coronavirus (SARS-CoV) is blocked by hexapeptide Tyr-Lys-Tyr-Arg-Tyr-Leu. The peptide also inhibits proliferation of coronavirus NL63. On human cells both viruses utilize angiotensin-converting enzyme 2 (ACE2) as entry receptor. Blocking the viral entry is specific as alpha virus Sindbis shows no reduction in infectivity. Peptide (438)YKYRYL(443) is part of the receptor-binding domain (RBD) of the spike protein of SARS-CoV. Peptide libraries were screened by surface plasmon resonance (SPR) to identify RBD binding epitopes. (438)YKYRYL(443) carries the dominant binding epitope and binds to ACE2 with K(D)=46 μM. The binding mode was further characterized by saturation transfer difference (STD) NMR spectroscopy and molecular dynamic simulations. Based on this information the peptide can be used as lead structure to design potential entry inhibitors against SARS-CoV and related viruses.</div></front></TEI></pubmed></double></record>Pour manipuler ce document sous Unix (Dilib)
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