Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors
Identifieur interne : 001D83 ( Ncbi/Merge ); précédent : 001D82; suivant : 001D84Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors
Auteurs : I-Jung Liu [Taïwan] ; Chuan-Liang Kao [Taïwan] ; Szu-Chia Hsieh [Taïwan] ; Ming-Tsair Wey [Taïwan] ; Lon-Sing Kan [Taïwan] ; Wei-Kung Wang [Taïwan]Source :
- Antiviral Research [ 0166-3542 ] ; 2008.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Cellules Vero, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Glycoprotéines membranaires (pharmacologie), Humains, Peptides (), Peptides (pharmacologie), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines de l'enveloppe virale (pharmacologie), Pénétration virale (), Structure secondaire des protéines, Syndrome respiratoire aigu sévère (traitement médicamenteux), Syndrome respiratoire aigu sévère (virologie), Séquence d'acides aminés, Virus du SRAS (), Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus du SRAS.
- pharmacologie : Glycoprotéines membranaires, Peptides, Protéines de l'enveloppe virale.
- traitement médicamenteux : Syndrome respiratoire aigu sévère.
- virologie : Syndrome respiratoire aigu sévère.
- Alignement de séquences, Animaux, Cellules Vero, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Peptides, Protéines de l'enveloppe virale, Pénétration virale, Structure secondaire des protéines, Séquence d'acides aminés, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Chlorocebus aethiops, Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Membrane Glycoproteins (pharmacology), Molecular Sequence Data, Peptides (chemistry), Peptides (pharmacology), Protein Structure, Secondary, SARS Virus (chemistry), SARS Virus (drug effects), SARS Virus (genetics), SARS Virus (metabolism), Sequence Alignment, Severe Acute Respiratory Syndrome (drug therapy), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Viral Envelope Proteins (pharmacology), Virus Internalization (drug effects).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , pharmacology : Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- chemistry : SARS Virus.
- drug effects : SARS Virus, Virus Internalization.
- drug therapy : Severe Acute Respiratory Syndrome.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Animals, Chlorocebus aethiops, Humans, Molecular Sequence Data, Protein Structure, Secondary, Sequence Alignment, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
The heptad repeats (HR1 and HR2) of the spike protein of SARS-CoV are highly conserved regions forming a critical 6-helix bundle during the fusion step of virus entry and are attractive targets of entry inhibitors. In this study, we report that a minimal HR2 peptide, P6 of 23-mer, can block the fusion of SARS-CoV with an IC50 of 1.04 ± 0.22 μM. This finding supports the structural prediction of the deep groove of HR1 trimer as a target for fusion inhibitors, and suggests P6 as a potential lead peptide for future drug development. Moreover, combination of an HR-1 peptide, N46, and its mutated version, N46eg, shows synergistic inhibition with an IC50 of 1.39 ± 0.05 μM and combination index of 0.75 ± 0.15, suggesting a common strategy to achieve promising inhibition by HR1 peptide for other class I envelope viruses.
Url:
DOI: 10.1016/j.antiviral.2008.10.001
PubMed: 18983873
PubMed Central: 7114320
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PMC:7114320Le document en format XML
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<term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>Humans</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Membrane Glycoproteins (pharmacology)</term>
<term>Molecular Sequence Data</term>
<term>Peptides (chemistry)</term>
<term>Peptides (pharmacology)</term>
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<term>SARS Virus (drug effects)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
<term>Sequence Alignment</term>
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<term>Vero Cells</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
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<term>Virus Internalization (drug effects)</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
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<front><div type="abstract" xml:lang="en"><p>The heptad repeats (HR1 and HR2) of the spike protein of SARS-CoV are highly conserved regions forming a critical 6-helix bundle during the fusion step of virus entry and are attractive targets of entry inhibitors. In this study, we report that a minimal HR2 peptide, P6 of 23-mer, can block the fusion of SARS-CoV with an IC<sub>50</sub>
of 1.04 ± 0.22 μM. This finding supports the structural prediction of the deep groove of HR1 trimer as a target for fusion inhibitors, and suggests P6 as a potential lead peptide for future drug development. Moreover, combination of an HR-1 peptide, N46, and its mutated version, N46eg, shows synergistic inhibition with an IC<sub>50</sub>
of 1.39 ± 0.05 μM and combination index of 0.75 ± 0.15, suggesting a common strategy to achieve promising inhibition by HR1 peptide for other class I envelope viruses.</p>
</div>
</front>
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<author><name sortKey="Liu, I Jung" sort="Liu, I Jung" uniqKey="Liu I" first="I-Jung" last="Liu">I-Jung Liu</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff2">Cardinal Tien College of Healthcare and Management, Hsin-Tien, Taipei County, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Cardinal Tien College of Healthcare and Management, Hsin-Tien, Taipei County</wicri:regionArea>
<wicri:noRegion>Taipei County</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kao, Chuan Liang" sort="Kao, Chuan Liang" uniqKey="Kao C" first="Chuan-Liang" last="Kao">Chuan-Liang Kao</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">Institute of Medical Technology, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Medical Technology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Hsieh, Szu Chia" sort="Hsieh, Szu Chia" uniqKey="Hsieh S" first="Szu-Chia" last="Hsieh">Szu-Chia Hsieh</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Wey, Ming Tsair" sort="Wey, Ming Tsair" uniqKey="Wey M" first="Ming-Tsair" last="Wey">Ming-Tsair Wey</name>
<affiliation wicri:level="1"><nlm:aff id="aff4">Institute of Chemistry, Academia Sinica, Taipei 11529, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Chemistry, Academia Sinica, Taipei 11529</wicri:regionArea>
<wicri:noRegion>Taipei 11529</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kan, Lon Sing" sort="Kan, Lon Sing" uniqKey="Kan L" first="Lon-Sing" last="Kan">Lon-Sing Kan</name>
<affiliation wicri:level="1"><nlm:aff id="aff4">Institute of Chemistry, Academia Sinica, Taipei 11529, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Chemistry, Academia Sinica, Taipei 11529</wicri:regionArea>
<wicri:noRegion>Taipei 11529</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Wang, Wei Kung" sort="Wang, Wei Kung" uniqKey="Wang W" first="Wei-Kung" last="Wang">Wei-Kung Wang</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff5">Department of Internal Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Department of Internal Medicine, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors</title>
<author><name sortKey="Liu, I Jung" sort="Liu, I Jung" uniqKey="Liu I" first="I-Jung" last="Liu">I-Jung Liu</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff2">Cardinal Tien College of Healthcare and Management, Hsin-Tien, Taipei County, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Cardinal Tien College of Healthcare and Management, Hsin-Tien, Taipei County</wicri:regionArea>
<wicri:noRegion>Taipei County</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kao, Chuan Liang" sort="Kao, Chuan Liang" uniqKey="Kao C" first="Chuan-Liang" last="Kao">Chuan-Liang Kao</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">Institute of Medical Technology, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Medical Technology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Hsieh, Szu Chia" sort="Hsieh, Szu Chia" uniqKey="Hsieh S" first="Szu-Chia" last="Hsieh">Szu-Chia Hsieh</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Wey, Ming Tsair" sort="Wey, Ming Tsair" uniqKey="Wey M" first="Ming-Tsair" last="Wey">Ming-Tsair Wey</name>
<affiliation wicri:level="1"><nlm:aff id="aff4">Institute of Chemistry, Academia Sinica, Taipei 11529, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Chemistry, Academia Sinica, Taipei 11529</wicri:regionArea>
<wicri:noRegion>Taipei 11529</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kan, Lon Sing" sort="Kan, Lon Sing" uniqKey="Kan L" first="Lon-Sing" last="Kan">Lon-Sing Kan</name>
<affiliation wicri:level="1"><nlm:aff id="aff4">Institute of Chemistry, Academia Sinica, Taipei 11529, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Chemistry, Academia Sinica, Taipei 11529</wicri:regionArea>
<wicri:noRegion>Taipei 11529</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Wang, Wei Kung" sort="Wang, Wei Kung" uniqKey="Wang W" first="Wei-Kung" last="Wang">Wei-Kung Wang</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff5">Department of Internal Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan</nlm:aff>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Department of Internal Medicine, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</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="2008">2008</date>
</imprint>
</series>
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<profileDesc><textClass></textClass>
</profileDesc>
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<front><div type="abstract" xml:lang="en"><p>The heptad repeats (HR1 and HR2) of the spike protein of SARS-CoV are highly conserved regions forming a critical 6-helix bundle during the fusion step of virus entry and are attractive targets of entry inhibitors. In this study, we report that a minimal HR2 peptide, P6 of 23-mer, can block the fusion of SARS-CoV with an IC<sub>50</sub>
of 1.04 ± 0.22 μM. This finding supports the structural prediction of the deep groove of HR1 trimer as a target for fusion inhibitors, and suggests P6 as a potential lead peptide for future drug development. Moreover, combination of an HR-1 peptide, N46, and its mutated version, N46eg, shows synergistic inhibition with an IC<sub>50</sub>
of 1.39 ± 0.05 μM and combination index of 0.75 ± 0.15, suggesting a common strategy to achieve promising inhibition by HR1 peptide for other class I envelope viruses.</p>
</div>
</front>
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</pmc>
<pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors.</title>
<author><name sortKey="Liu, I Jung" sort="Liu, I Jung" uniqKey="Liu I" first="I-Jung" last="Liu">I-Jung Liu</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100, Taiwan.</nlm:affiliation>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kao, Chuan Liang" sort="Kao, Chuan Liang" uniqKey="Kao C" first="Chuan-Liang" last="Kao">Chuan-Liang Kao</name>
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<author><name sortKey="Hsieh, Szu Chia" sort="Hsieh, Szu Chia" uniqKey="Hsieh S" first="Szu-Chia" last="Hsieh">Szu-Chia Hsieh</name>
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<author><name sortKey="Wey, Ming Tsair" sort="Wey, Ming Tsair" uniqKey="Wey M" first="Ming-Tsair" last="Wey">Ming-Tsair Wey</name>
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<author><name sortKey="Kan, Lon Sing" sort="Kan, Lon Sing" uniqKey="Kan L" first="Lon-Sing" last="Kan">Lon-Sing Kan</name>
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<author><name sortKey="Wang, Wei Kung" sort="Wang, Wei Kung" uniqKey="Wang W" first="Wei-Kung" last="Wang">Wei-Kung Wang</name>
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</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2009">2009</date>
<idno type="RBID">pubmed:18983873</idno>
<idno type="pmid">18983873</idno>
<idno type="doi">10.1016/j.antiviral.2008.10.001</idno>
<idno type="wicri:Area/PubMed/Corpus">001A35</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001A35</idno>
<idno type="wicri:Area/PubMed/Curation">001A35</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001A35</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001865</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001865</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors.</title>
<author><name sortKey="Liu, I Jung" sort="Liu, I Jung" uniqKey="Liu I" first="I-Jung" last="Liu">I-Jung Liu</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100, Taiwan.</nlm:affiliation>
<country xml:lang="fr">Taïwan</country>
<wicri:regionArea>Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 100</wicri:regionArea>
<wicri:noRegion>Taipei 100</wicri:noRegion>
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<series><title level="j">Antiviral research</title>
<idno type="eISSN">1872-9096</idno>
<imprint><date when="2009" type="published">2009</date>
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</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>Humans</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Membrane Glycoproteins (pharmacology)</term>
<term>Molecular Sequence Data</term>
<term>Peptides (chemistry)</term>
<term>Peptides (pharmacology)</term>
<term>Protein Structure, Secondary</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (drug effects)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
<term>Sequence Alignment</term>
<term>Severe Acute Respiratory Syndrome (drug therapy)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Vero Cells</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Viral Envelope Proteins (pharmacology)</term>
<term>Virus Internalization (drug effects)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term>
<term>Animaux</term>
<term>Cellules Vero</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Glycoprotéines membranaires (pharmacologie)</term>
<term>Humains</term>
<term>Peptides ()</term>
<term>Peptides (pharmacologie)</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Protéines de l'enveloppe virale (pharmacologie)</term>
<term>Pénétration virale ()</term>
<term>Structure secondaire des protéines</term>
<term>Syndrome respiratoire aigu sévère (traitement médicamenteux)</term>
<term>Syndrome respiratoire aigu sévère (virologie)</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Peptides</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Peptides</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term>
<term>Virus Internalization</term>
</keywords>
<keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Virus du SRAS</term>
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</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Peptides</term>
<term>Protéines de l'enveloppe virale</term>
</keywords>
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</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Protein Structure, Secondary</term>
<term>Sequence Alignment</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Vero Cells</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term>
<term>Animaux</term>
<term>Cellules Vero</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Humains</term>
<term>Peptides</term>
<term>Protéines de l'enveloppe virale</term>
<term>Pénétration virale</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS</term>
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<front><div type="abstract" xml:lang="en">The heptad repeats (HR1 and HR2) of the spike protein of SARS-CoV are highly conserved regions forming a critical 6-helix bundle during the fusion step of virus entry and are attractive targets of entry inhibitors. In this study, we report that a minimal HR2 peptide, P6 of 23-mer, can block the fusion of SARS-CoV with an IC(50) of 1.04+/-0.22 microM. This finding supports the structural prediction of the deep groove of HR1 trimer as a target for fusion inhibitors, and suggests P6 as a potential lead peptide for future drug development. Moreover, combination of an HR-1 peptide, N46, and its mutated version, N46eg, shows synergistic inhibition with an IC(50) of 1.39+/-0.05 microM and combination index of 0.75+/-0.15, suggesting a common strategy to achieve promising inhibition by HR1 peptide for other class I envelope viruses.</div>
</front>
</TEI>
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