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 : 000B93 ( Main/Exploration ); précédent : 000B92; suivant : 000B94A 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 ; Susanne Pfefferle ; Christian Drosten ; Bernd MeyerSource :
- Antiviral research [ 1872-9096 ] ; 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
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.
DOI: 10.1016/j.antiviral.2011.12.012
PubMed: 22265858
Affiliations:
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Le document en format XML
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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><affiliations><list><country><li>Allemagne</li></country><region><li>Hambourg</li></region><settlement><li>Hambourg</li></settlement></list><tree><noCountry><name sortKey="Axmann, Marco" sort="Axmann, Marco" uniqKey="Axmann M" first="Marco" last="Axmann">Marco Axmann</name><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><name sortKey="Meyer, Bernd" sort="Meyer, Bernd" uniqKey="Meyer B" first="Bernd" last="Meyer">Bernd Meyer</name><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name></noCountry><country name="Allemagne"><region name="Hambourg"><name sortKey="Struck, Anna Winona" sort="Struck, Anna Winona" uniqKey="Struck A" first="Anna-Winona" last="Struck">Anna-Winona Struck</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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