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 : 000004 ( PascalFrancis/Corpus ); précédent : 000003; suivant : 000005A 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 ; Marco Axmann ; Susanne Pfefferle ; Christian Drosten ; Bernd MeyerSource :
- Antiviral research [ 0166-3542 ] ; 2012.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
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 KD = 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.
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Format Inist (serveur)
NO : | PASCAL 12-0375796 INIST |
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ET : | A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2 |
AU : | STRUCK (Anna-Winona); AXMANN (Marco); PFEFFERLE (Susanne); DROSTEN (Christian); MEYER (Bernd) |
AF : | Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6/20146 Hamburg/Allemagne (1 aut., 2 aut., 5 aut.); Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74/20359 Hamburg/Allemagne (3 aut., 4 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Antiviral research; ISSN 0166-3542; Coden ARSRDR; Royaume-Uni; Da. 2012; Vol. 94; No. 3; Pp. 288-296; Bibl. 3/4 p. |
LA : | Anglais |
EA : | 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 KD = 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. |
CC : | 002B02S05 |
FD : | Récepteur biologique; Virus syndrome respiratoire aigu sévère; Protéine; In vitro; Cellule; Homme; Multiplication cellulaire; Criblage; Dépistage; Angiotensin converting enzyme 2; Inhibiteur d'entrée |
FG : | Coronavirus; Coronaviridae; Nidovirales; Virus |
ED : | Biological receptor; Severe acute respiratory syndrome virus; Protein; In vitro; Cell; Human; Cell proliferation; Screening; Medical screening; Entry inhibitor |
EG : | Coronavirus; Coronaviridae; Nidovirales; Virus |
SD : | Receptor biológico; Severe acute respiratory syndrome virus; Proteína; In vitro; Célula; Hombre; Multiplicación celular; Cernido; Descubrimiento; Inhibidor de entrada |
LO : | INIST-18839.354000505222760100 |
ID : | 12-0375796 |
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Pascal:12-0375796Le document en format XML
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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>
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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>
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<server><NO>PASCAL 12-0375796 INIST</NO>
<ET>A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2</ET>
<AU>STRUCK (Anna-Winona); AXMANN (Marco); PFEFFERLE (Susanne); DROSTEN (Christian); MEYER (Bernd)</AU>
<AF>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6/20146 Hamburg/Allemagne (1 aut., 2 aut., 5 aut.); Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74/20359 Hamburg/Allemagne (3 aut., 4 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
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<EA>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.</EA>
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</record>
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