SrasV1, Main, Curation, bibRecord, 001F95

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 : 001F95 ( Main/Curation ); précédent : 001F94; suivant : 001F96

A 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.

RBID : Pascal:12-0375796

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.
Pascal (Inist)
- Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Pénétration virale, Récepteur biologique, Résonance plasmonique de surface, Virus du SRAS, Virus syndrome respiratoire aigu sévère, Protéine, In vitro, Cellule, Homme, Multiplication cellulaire, Criblage, Dépistage, Angiotensin converting enzyme 2, Inhibiteur d'entrée.
Wicri :
- topic : Homme.

English descriptors

KwdEn :
- Antiviral Agents (pharmacology), Biological receptor, Cell, Cell proliferation, Entry inhibitor, Human, Humans, In vitro, Medical screening, Membrane Glycoproteins (genetics), Membrane Glycoproteins (pharmacology), Peptides (genetics), Peptides (pharmacology), Peptidyl-Dipeptidase A (metabolism), Protein, Protein Binding, Receptors, Virus (metabolism), SARS Virus (drug effects), SARS Virus (growth & development), SARS Virus (physiology), Screening, Severe acute respiratory syndrome virus, 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

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 ⁴³⁸YKYRYL⁴⁴³ 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. ⁴³⁸YKYRYL⁴⁴³ 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.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114193

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Pascal:12-0375796

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiviral Agents (pharmacology)</term>
<term>Biological receptor</term>
<term>Cell</term>
<term>Cell proliferation</term>
<term>Entry inhibitor</term>
<term>Human</term>
<term>Humans</term>
<term>In vitro</term>
<term>Medical screening</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</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>Screening</term>
<term>Severe acute respiratory syndrome virus</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="Pascal" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Pénétration virale</term>
<term>Récepteur biologique</term>
<term>Résonance plasmonique de surface</term>
<term>Virus du SRAS</term>
<term>Virus syndrome respiratoire aigu sévère</term>
<term>Protéine</term>
<term>In vitro</term>
<term>Cellule</term>
<term>Homme</term>
<term>Multiplication cellulaire</term>
<term>Criblage</term>
<term>Dépistage</term>
<term>Angiotensin converting enzyme 2</term>
<term>Inhibiteur d'entrée</term>
</keywords>
<keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Homme</term>
</keywords>
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<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 <sup>438</sup>
YKYRYL<sup>443</sup>
 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. <sup>438</sup>
YKYRYL<sup>443</sup>
 carries the dominant binding epitope and binds to ACE2 with K<sub>D</sub>
 = 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>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">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"><inist:fA14 i1="01"><s1>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6</s1>
<s2>20146 Hamburg</s2>
<s3>DEU</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
<country>Allemagne</country>
<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"><inist:fA14 i1="01"><s1>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6</s1>
<s2>20146 Hamburg</s2>
<s3>DEU</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
<country>Allemagne</country>
<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>
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<s2>20359 Hamburg</s2>
<s3>DEU</s3>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
</inist:fA14>
<country>Allemagne</country>
<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"><inist:fA14 i1="02"><s1>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74</s1>
<s2>20359 Hamburg</s2>
<s3>DEU</s3>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
</inist:fA14>
<country>Allemagne</country>
<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"><inist:fA14 i1="01"><s1>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6</s1>
<s2>20146 Hamburg</s2>
<s3>DEU</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
<country>Allemagne</country>
<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" type="main">Antiviral research</title>
<title level="j" type="abbreviated">Antivir. res.</title>
<idno type="ISSN">0166-3542</idno>
<imprint><date when="2012">2012</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><title level="j" type="main">Antiviral research</title>
<title level="j" type="abbreviated">Antivir. res.</title>
<idno type="ISSN">0166-3542</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biological receptor</term>
<term>Cell</term>
<term>Cell proliferation</term>
<term>Entry inhibitor</term>
<term>Human</term>
<term>In vitro</term>
<term>Medical screening</term>
<term>Protein</term>
<term>Screening</term>
<term>Severe acute respiratory syndrome virus</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Récepteur biologique</term>
<term>Virus syndrome respiratoire aigu sévère</term>
<term>Protéine</term>
<term>In vitro</term>
<term>Cellule</term>
<term>Homme</term>
<term>Multiplication cellulaire</term>
<term>Criblage</term>
<term>Dépistage</term>
<term>Angiotensin converting enzyme 2</term>
<term>Inhibiteur d'entrée</term>
</keywords>
<keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Homme</term>
</keywords>
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<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 <sup>438</sup>
YKYRYL<sup>443</sup>
 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. <sup>438</sup>
YKYRYL<sup>443</sup>
 carries the dominant binding epitope and binds to ACE2 with K<sub>D</sub>
 = 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>
</INIST>
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<country xml:lang="fr">Allemagne</country>
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<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>
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</placeName>
</affiliation>
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<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>
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<author><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name>
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<country xml:lang="fr">Allemagne</country>
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<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>
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<wicri:noRegion>20359 Hamburg</wicri:noRegion>
<placeName><settlement type="city">Hambourg</settlement>
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</placeName>
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<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>
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<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>
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<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>
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A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2

A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2

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