SrasV1, PascalFrancis, Corpus, bibRecord, 000048

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 : 000048 ( PascalFrancis/Corpus ); précédent : 000047; suivant : 000049

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 ; Marco Axmann ; Susanne Pfefferle ; Christian Drosten ; Bernd Meyer

Source :

Antiviral research [ 0166-3542 ] ; 2012.

RBID : Pascal:12-0375796

Descripteurs français

Pascal (Inist)
- Récepteur biologique, Virus syndrome respiratoire aigu sévère, Protéine, In vitro, Cellule, Homme, Multiplication cellulaire, Criblage, Dépistage, Angiotensin converting enzyme 2, Inhibiteur d'entrée.

English descriptors

KwdEn :
- Biological receptor, Cell, Cell proliferation, Entry inhibitor, Human, In vitro, Medical screening, Protein, Screening, Severe acute respiratory syndrome virus.

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.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A11	`01`	`1`		`@1 STRUCK (Anna-Winona)`
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A11	`05`	`1`		`@1 MEYER (Bernd)`
A14	`01`			`@1 Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6 @2 20146 Hamburg @3 DEU @Z 1 aut. @Z 2 aut. @Z 5 aut.`
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C01	`01`		`ENG`	@0 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.
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Format Inist (serveur)

NO :	PASCAL 12-0375796 INIST
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 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.
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

Links to Exploration step

Pascal:12-0375796

Le 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>
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<fC01 i1="01" l="ENG"><s0>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>
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 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>
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<s4>INC</s4>
<s5>86</s5>
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<s4>CD</s4>
<s5>96</s5>
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<fC03 i1="11" i2="X" l="ENG"><s0>Entry inhibitor</s0>
<s4>CD</s4>
<s5>96</s5>
</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Inhibidor de entrada</s0>
<s4>CD</s4>
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<fC07 i1="01" i2="X" l="SPA"><s0>Coronavirus</s0>
<s2>NW</s2>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NW</s2>
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<fC07 i1="03" i2="X" l="SPA"><s0>Nidovirales</s0>
<s2>NW</s2>
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<fC07 i1="04" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
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<fC07 i1="04" i2="X" l="ENG"><s0>Virus</s0>
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<fC07 i1="04" i2="X" l="SPA"><s0>Virus</s0>
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<fN21><s1>289</s1>
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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>
<SO>Antiviral research; ISSN 0166-3542; Coden ARSRDR; Royaume-Uni; Da. 2012; Vol. 94; No. 3; Pp. 288-296; Bibl. 3/4 p.</SO>
<LA>Anglais</LA>
<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>
<CC>002B02S05</CC>
<FD>Récepteur biologique; Virus syndrome respiratoire aigu sévère; Protéine; In vitro; Cellule; Homme; Multiplication cellulaire; Criblage; Dépistage; Angiotensin converting enzyme 2; Inhibiteur d'entrée</FD>
<FG>Coronavirus; Coronaviridae; Nidovirales; Virus</FG>
<ED>Biological receptor; Severe acute respiratory syndrome virus; Protein; In vitro; Cell; Human; Cell proliferation; Screening; Medical screening; Entry inhibitor</ED>
<EG>Coronavirus; Coronaviridae; Nidovirales; Virus</EG>
<SD>Receptor biológico; Severe acute respiratory syndrome virus; Proteína; In vitro; Célula; Hombre; Multiplicación celular; Cernido; Descubrimiento; Inhibidor de entrada</SD>
<LO>INIST-18839.354000505222760100</LO>
<ID>12-0375796</ID>
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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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