Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein
Identifieur interne : 001458 ( Ncbi/Checkpoint ); précédent : 001457; suivant : 001459Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein
Auteurs : Bruno Sainz [États-Unis] ; Eric C. Mossel [États-Unis] ; William R. Gallaher [États-Unis] ; William C. Wimley [États-Unis] ; C. J. Peters [États-Unis] ; Russell B. Wilson [États-Unis] ; Robert F. Garry [États-Unis]Source :
- Virus Research [ 0168-1702 ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Hémagglutinines (), Hémagglutinines virales (), Lignée cellulaire, Méthode des plages virales, Peptides (génétique), Peptides (pharmacologie), Peptides (synthèse chimique), Protéines de l'enveloppe virale (), Relation dose-effet des médicaments, Sous-unités de protéines (génétique), Sous-unités de protéines (pharmacologie), Sous-unités de protéines (synthèse chimique), Séquence d'acides aminés, Virulence (), Virus de l'hépatite murine (), Virus du SRAS (), Virus du SRAS (croissance et développement), Virus du SRAS (pathogénicité).
- MESH :
- croissance et développement : Virus du SRAS.
- génétique : Peptides, Sous-unités de protéines.
- pathogénicité : Virus du SRAS.
- pharmacologie : Peptides, Sous-unités de protéines.
- synthèse chimique : Peptides, Sous-unités de protéines.
- Animaux, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Hémagglutinines, Hémagglutinines virales, Lignée cellulaire, Méthode des plages virales, Protéines de l'enveloppe virale, Relation dose-effet des médicaments, Séquence d'acides aminés, Virulence, Virus de l'hépatite murine, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cell Line, Dose-Response Relationship, Drug, Hemagglutinins (chemistry), Hemagglutinins, Viral (chemistry), Membrane Glycoproteins (chemistry), Molecular Sequence Data, Murine hepatitis virus (chemistry), Peptides (chemical synthesis), Peptides (genetics), Peptides (pharmacology), Protein Subunits (chemical synthesis), Protein Subunits (genetics), Protein Subunits (pharmacology), SARS Virus (drug effects), SARS Virus (growth & development), SARS Virus (pathogenicity), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Plaque Assay, Virulence (drug effects).
- MESH :
- chemical , chemical synthesis : Peptides, Protein Subunits.
- chemical , chemistry : Hemagglutinins, Hemagglutinins, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- chemistry : Murine hepatitis virus.
- drug effects : SARS Virus, Virulence.
- chemical , genetics : Peptides, Protein Subunits.
- growth & development : SARS Virus.
- pathogenicity : SARS Virus.
- chemical , pharmacology : Peptides, Protein Subunits.
- Amino Acid Sequence, Animals, Cell Line, Dose-Response Relationship, Drug, Molecular Sequence Data, Spike Glycoprotein, Coronavirus, Viral Plaque Assay.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the cause of an atypical pneumonia that affected Asia, North America and Europe in 2002–2003. The viral spike (S) glycoprotein is responsible for mediating receptor binding and membrane fusion. Recent studies have proposed that the carboxyl terminal portion (S2 subunit) of the S protein is a class I viral fusion protein. The Wimley and White interfacial hydrophobicity scale was used to identify regions within the CoV S2 subunit that may preferentially associate with lipid membranes with the premise that peptides analogous to these regions may function as inhibitors of viral infectivity. Five regions of high interfacial hydrophobicity spanning the length of the S2 subunit of SARS-CoV and murine hepatitis virus (MHV) were identified. Peptides analogous to regions of the N-terminus or the pre-transmembrane domain of the S2 subunit inhibited SARS-CoV plaque formation by 40–70% at concentrations of 15–30 μM. Interestingly, peptides analogous to the SARS-CoV or MHV loop region inhibited viral plaque formation by >80% at similar concentrations. The observed effects were dose-dependent (IC50 values of 2–4 μM) and not a result of peptide-mediated cell cytotoxicity. The antiviral activity of the CoV peptides tested provides an attractive basis for the development of new fusion peptide inhibitors corresponding to regions outside the fusion protein heptad repeat regions.
Url:
DOI: 10.1016/j.virusres.2006.03.001
PubMed: 16616792
PubMed Central: 2582734
Affiliations:
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PMC:2582734Le document en format XML
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<series><title level="j">Virus Research</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Cell Line</term>
<term>Dose-Response Relationship, Drug</term>
<term>Hemagglutinins (chemistry)</term>
<term>Hemagglutinins, Viral (chemistry)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Molecular Sequence Data</term>
<term>Murine hepatitis virus (chemistry)</term>
<term>Peptides (chemical synthesis)</term>
<term>Peptides (genetics)</term>
<term>Peptides (pharmacology)</term>
<term>Protein Subunits (chemical synthesis)</term>
<term>Protein Subunits (genetics)</term>
<term>Protein Subunits (pharmacology)</term>
<term>SARS Virus (drug effects)</term>
<term>SARS Virus (growth & development)</term>
<term>SARS Virus (pathogenicity)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Plaque Assay</term>
<term>Virulence (drug effects)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Hémagglutinines ()</term>
<term>Hémagglutinines virales ()</term>
<term>Lignée cellulaire</term>
<term>Méthode des plages virales</term>
<term>Peptides (génétique)</term>
<term>Peptides (pharmacologie)</term>
<term>Peptides (synthèse chimique)</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Relation dose-effet des médicaments</term>
<term>Sous-unités de protéines (génétique)</term>
<term>Sous-unités de protéines (pharmacologie)</term>
<term>Sous-unités de protéines (synthèse chimique)</term>
<term>Séquence d'acides aminés</term>
<term>Virulence ()</term>
<term>Virus de l'hépatite murine ()</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (croissance et développement)</term>
<term>Virus du SRAS (pathogénicité)</term>
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<term>Protein Subunits</term>
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<term>Hemagglutinins, Viral</term>
<term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Murine hepatitis virus</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>Virulence</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptides</term>
<term>Protein Subunits</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>Peptides</term>
<term>Sous-unités de protéines</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Peptides</term>
<term>Sous-unités de protéines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Peptides</term>
<term>Protein Subunits</term>
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<keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Peptides</term>
<term>Sous-unités de protéines</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Cell Line</term>
<term>Dose-Response Relationship, Drug</term>
<term>Molecular Sequence Data</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Plaque Assay</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Hémagglutinines</term>
<term>Hémagglutinines virales</term>
<term>Lignée cellulaire</term>
<term>Méthode des plages virales</term>
<term>Protéines de l'enveloppe virale</term>
<term>Relation dose-effet des médicaments</term>
<term>Séquence d'acides aminés</term>
<term>Virulence</term>
<term>Virus de l'hépatite murine</term>
<term>Virus du SRAS</term>
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<front><div type="abstract" xml:lang="en"><p>Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the cause of an atypical pneumonia that affected Asia, North America and Europe in 2002–2003. The viral spike (S) glycoprotein is responsible for mediating receptor binding and membrane fusion. Recent studies have proposed that the carboxyl terminal portion (S2 subunit) of the S protein is a class I viral fusion protein. The Wimley and White interfacial hydrophobicity scale was used to identify regions within the CoV S2 subunit that may preferentially associate with lipid membranes with the premise that peptides analogous to these regions may function as inhibitors of viral infectivity. Five regions of high interfacial hydrophobicity spanning the length of the S2 subunit of SARS-CoV and murine hepatitis virus (MHV) were identified. Peptides analogous to regions of the N-terminus or the pre-transmembrane domain of the S2 subunit inhibited SARS-CoV plaque formation by 40–70% at concentrations of 15–30 μM. Interestingly, peptides analogous to the SARS-CoV or MHV loop region inhibited viral plaque formation by >80% at similar concentrations. The observed effects were dose-dependent (IC50 values of 2–4 μM) and not a result of peptide-mediated cell cytotoxicity. The antiviral activity of the CoV peptides tested provides an attractive basis for the development of new fusion peptide inhibitors corresponding to regions outside the fusion protein heptad repeat regions.</p>
</div>
</front>
<back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Bergeron, E" uniqKey="Bergeron E">E. Bergeron</name>
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</div1>
</back>
</TEI>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Louisiane</li>
<li>Texas</li>
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</affiliations>
</record>
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