SrasV1, PascalFrancis, Corpus, bibRecord, 000059

Simultaneous Treatment of Human Bronchial Epithelial Cells with Serine and Cysteine Protease Inhibitors Prevents Severe Acute Respiratory Syndrome Coronavirus Entry

Identifieur interne : 000059 ( PascalFrancis/Corpus ); précédent : 000058; suivant : 000060

Simultaneous Treatment of Human Bronchial Epithelial Cells with Serine and Cysteine Protease Inhibitors Prevents Severe Acute Respiratory Syndrome Coronavirus Entry

Auteurs : Miyuki Kawase ; Kazuya Shirato ; Lia Van Der Hoek ; Fumihiro Taguchi ; Shutoku Matsuyama

Source :

Journal of virology [ 0022-538X ] ; 2012.

RBID : Pascal:12-0269207

Descripteurs français

Pascal (Inist)
- Homme, Coronavirus, Traitement, Cellule épithéliale, Cysteine endopeptidases, Syndrome respiratoire aigu sévère, Sérine, Inhibiteur protease, Antiviral.

English descriptors

KwdEn :
- Antiviral, Coronavirus, Cysteine endopeptidases, Epithelial cell, Human, Protease inhibitor, Serine, Severe acute respiratory syndrome, Treatment.

Abstract

The type II transmembrane protease TMPRSS2 activates the spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) on the cell surface following receptor binding during viral entry into cells. In the absence of TMPRSS2, SARS-CoV achieves cell entry via an endosomal pathway in which cathepsin L may play an important role, i.e., the activation of spike protein fusogenicity. This study shows that a commercial serine protease inhibitor (camostat) partially blocked infection by SARS-CoV and human coronavirus NL63 (HCoV-NL63) in HeLa cells expressing the receptor angiotensin-converting enzyme 2 (ACE2) and TMPRSS2. Simultaneous treatment of the cells with camostat and EST [(23,25)trans-epoarysuccinyl-L-leurylamindo-3-methylbutane ethyl ester], a cathepsin inhibitor, efficiently prevented both cell entry and the multistep growth of SARS-CoV in human Calu-3 airway epithelial cells. This efficient inhibition could be attributed to the dual blockade of entry from the cell surface and through the endosomal pathway. These observations suggest camostat as a candidate antiviral drug to prevent or depress TMPRSS2-dependent infection by SARS-CoV.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A11	`02`	`1`		`@1 SHIRATO (Kazuya)`
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A11	`05`	`1`		`@1 MATSUYAMA (Shutoku)`
A14	`01`			`@1 Department of Virology III, National Institute of Infectious Diseases, Murayama Branch, Gakuen Musashi-Murayama @2 Tokyo @3 JPN @Z 1 aut. @Z 2 aut. @Z 5 aut.`
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C01	`01`		`ENG`	@0 The type II transmembrane protease TMPRSS2 activates the spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) on the cell surface following receptor binding during viral entry into cells. In the absence of TMPRSS2, SARS-CoV achieves cell entry via an endosomal pathway in which cathepsin L may play an important role, i.e., the activation of spike protein fusogenicity. This study shows that a commercial serine protease inhibitor (camostat) partially blocked infection by SARS-CoV and human coronavirus NL63 (HCoV-NL63) in HeLa cells expressing the receptor angiotensin-converting enzyme 2 (ACE2) and TMPRSS2. Simultaneous treatment of the cells with camostat and EST [(23,25)trans-epoarysuccinyl-L-leurylamindo-3-methylbutane ethyl ester], a cathepsin inhibitor, efficiently prevented both cell entry and the multistep growth of SARS-CoV in human Calu-3 airway epithelial cells. This efficient inhibition could be attributed to the dual blockade of entry from the cell surface and through the endosomal pathway. These observations suggest camostat as a candidate antiviral drug to prevent or depress TMPRSS2-dependent infection by SARS-CoV.
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Format Inist (serveur)

NO :	PASCAL 12-0269207 INIST
ET :	Simultaneous Treatment of Human Bronchial Epithelial Cells with Serine and Cysteine Protease Inhibitors Prevents Severe Acute Respiratory Syndrome Coronavirus Entry
AU :	KAWASE (Miyuki); SHIRATO (Kazuya); DER HOEK (Lia Van); TAGUCHI (Fumihiro); MATSUYAMA (Shutoku)
AF :	Department of Virology III, National Institute of Infectious Diseases, Murayama Branch, Gakuen Musashi-Murayama/Tokyo/Japon (1 aut., 2 aut., 5 aut.); Faculty of Veterinary Medicine, Nippon Veterinary and Life Science University, Kyonan-cho/Musashino, Tokyo/Japon (4 aut.); Department of Medical Microbiology, University of Amsterdam, Faculty of Earth and Life Sciences/Amsterdam/Pays-Bas (3 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2012; Vol. 86; No. 12; Pp. 6537-6545; Bibl. 34 ref.
LA :	Anglais
EA :	The type II transmembrane protease TMPRSS2 activates the spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) on the cell surface following receptor binding during viral entry into cells. In the absence of TMPRSS2, SARS-CoV achieves cell entry via an endosomal pathway in which cathepsin L may play an important role, i.e., the activation of spike protein fusogenicity. This study shows that a commercial serine protease inhibitor (camostat) partially blocked infection by SARS-CoV and human coronavirus NL63 (HCoV-NL63) in HeLa cells expressing the receptor angiotensin-converting enzyme 2 (ACE2) and TMPRSS2. Simultaneous treatment of the cells with camostat and EST [(23,25)trans-epoarysuccinyl-L-leurylamindo-3-methylbutane ethyl ester], a cathepsin inhibitor, efficiently prevented both cell entry and the multistep growth of SARS-CoV in human Calu-3 airway epithelial cells. This efficient inhibition could be attributed to the dual blockade of entry from the cell surface and through the endosomal pathway. These observations suggest camostat as a candidate antiviral drug to prevent or depress TMPRSS2-dependent infection by SARS-CoV.
CC :	002A05C10
FD :	Homme; Coronavirus; Traitement; Cellule épithéliale; Cysteine endopeptidases; Syndrome respiratoire aigu sévère; Sérine; Inhibiteur protease; Antiviral
FG :	Coronaviridae; Nidovirales; Virus; Peptidases; Hydrolases; Enzyme; Virose; Infection; Pathologie de l'appareil respiratoire; Pathologie des poumons
ED :	Human; Coronavirus; Treatment; Epithelial cell; Cysteine endopeptidases; Severe acute respiratory syndrome; Serine; Protease inhibitor; Antiviral
EG :	Coronaviridae; Nidovirales; Virus; Peptidases; Hydrolases; Enzyme; Viral disease; Infection; Respiratory disease; Lung disease
SD :	Hombre; Coronavirus; Tratamiento; Célula epitelial; Cysteine endopeptidases; Síndrome respiratorio agudo severo; Serina; Inhibidor proteasa; Antiviral
LO :	INIST-13592.354000508304970150
ID :	12-0269207

Links to Exploration step

Pascal:12-0269207

Le document en format XML

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<front><div type="abstract" xml:lang="en">The type II transmembrane protease TMPRSS2 activates the spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) on the cell surface following receptor binding during viral entry into cells. In the absence of TMPRSS2, SARS-CoV achieves cell entry via an endosomal pathway in which cathepsin L may play an important role, i.e., the activation of spike protein fusogenicity. This study shows that a commercial serine protease inhibitor (camostat) partially blocked infection by SARS-CoV and human coronavirus NL63 (HCoV-NL63) in HeLa cells expressing the receptor angiotensin-converting enzyme 2 (ACE2) and TMPRSS2. Simultaneous treatment of the cells with camostat and EST [(23,25)trans-epoarysuccinyl-L-leurylamindo-3-methylbutane ethyl ester], a cathepsin inhibitor, efficiently prevented both cell entry and the multistep growth of SARS-CoV in human Calu-3 airway epithelial cells. This efficient inhibition could be attributed to the dual blockade of entry from the cell surface and through the endosomal pathway. These observations suggest camostat as a candidate antiviral drug to prevent or depress TMPRSS2-dependent infection by SARS-CoV.</div>
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<fC01 i1="01" l="ENG"><s0>The type II transmembrane protease TMPRSS2 activates the spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) on the cell surface following receptor binding during viral entry into cells. In the absence of TMPRSS2, SARS-CoV achieves cell entry via an endosomal pathway in which cathepsin L may play an important role, i.e., the activation of spike protein fusogenicity. This study shows that a commercial serine protease inhibitor (camostat) partially blocked infection by SARS-CoV and human coronavirus NL63 (HCoV-NL63) in HeLa cells expressing the receptor angiotensin-converting enzyme 2 (ACE2) and TMPRSS2. Simultaneous treatment of the cells with camostat and EST [(23,25)trans-epoarysuccinyl-L-leurylamindo-3-methylbutane ethyl ester], a cathepsin inhibitor, efficiently prevented both cell entry and the multistep growth of SARS-CoV in human Calu-3 airway epithelial cells. This efficient inhibition could be attributed to the dual blockade of entry from the cell surface and through the endosomal pathway. These observations suggest camostat as a candidate antiviral drug to prevent or depress TMPRSS2-dependent infection by SARS-CoV.</s0>
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<fC03 i1="01" i2="X" l="ENG"><s0>Human</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Hombre</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Traitement</s0>
<s5>05</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Treatment</s0>
<s5>05</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Tratamiento</s0>
<s5>05</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Cellule épithéliale</s0>
<s5>06</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Epithelial cell</s0>
<s5>06</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Célula epitelial</s0>
<s5>06</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Cysteine endopeptidases</s0>
<s2>FE</s2>
<s5>07</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Cysteine endopeptidases</s0>
<s2>FE</s2>
<s5>07</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Cysteine endopeptidases</s0>
<s2>FE</s2>
<s5>07</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Syndrome respiratoire aigu sévère</s0>
<s2>NM</s2>
<s5>08</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Severe acute respiratory syndrome</s0>
<s2>NM</s2>
<s5>08</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Síndrome respiratorio agudo severo</s0>
<s2>NM</s2>
<s5>08</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Sérine</s0>
<s2>NK</s2>
<s2>FR</s2>
<s5>14</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Serine</s0>
<s2>NK</s2>
<s2>FR</s2>
<s5>14</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Serina</s0>
<s2>NK</s2>
<s2>FR</s2>
<s5>14</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Inhibiteur protease</s0>
<s2>FR</s2>
<s5>15</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Protease inhibitor</s0>
<s2>FR</s2>
<s5>15</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Inhibidor proteasa</s0>
<s2>FR</s2>
<s5>15</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Antiviral</s0>
<s5>45</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Antiviral</s0>
<s5>45</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Antiviral</s0>
<s5>45</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="07" i2="X" l="FRE"><s0>Virose</s0>
</fC07>
<fC07 i1="07" i2="X" l="ENG"><s0>Viral disease</s0>
</fC07>
<fC07 i1="07" i2="X" l="SPA"><s0>Virosis</s0>
</fC07>
<fC07 i1="08" i2="X" l="FRE"><s0>Infection</s0>
</fC07>
<fC07 i1="08" i2="X" l="ENG"><s0>Infection</s0>
</fC07>
<fC07 i1="08" i2="X" l="SPA"><s0>Infección</s0>
</fC07>
<fC07 i1="09" i2="X" l="FRE"><s0>Pathologie de l'appareil respiratoire</s0>
<s5>13</s5>
</fC07>
<fC07 i1="09" i2="X" l="ENG"><s0>Respiratory disease</s0>
<s5>13</s5>
</fC07>
<fC07 i1="09" i2="X" l="SPA"><s0>Aparato respiratorio patología</s0>
<s5>13</s5>
</fC07>
<fC07 i1="10" i2="X" l="FRE"><s0>Pathologie des poumons</s0>
<s5>16</s5>
</fC07>
<fC07 i1="10" i2="X" l="ENG"><s0>Lung disease</s0>
<s5>16</s5>
</fC07>
<fC07 i1="10" i2="X" l="SPA"><s0>Pulmón patología</s0>
<s5>16</s5>
</fC07>
<fN21><s1>205</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
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<server><NO>PASCAL 12-0269207 INIST</NO>
<ET>Simultaneous Treatment of Human Bronchial Epithelial Cells with Serine and Cysteine Protease Inhibitors Prevents Severe Acute Respiratory Syndrome Coronavirus Entry</ET>
<AU>KAWASE (Miyuki); SHIRATO (Kazuya); DER HOEK (Lia Van); TAGUCHI (Fumihiro); MATSUYAMA (Shutoku)</AU>
<AF>Department of Virology III, National Institute of Infectious Diseases, Murayama Branch, Gakuen Musashi-Murayama/Tokyo/Japon (1 aut., 2 aut., 5 aut.); Faculty of Veterinary Medicine, Nippon Veterinary and Life Science University, Kyonan-cho/Musashino, Tokyo/Japon (4 aut.); Department of Medical Microbiology, University of Amsterdam, Faculty of Earth and Life Sciences/Amsterdam/Pays-Bas (3 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2012; Vol. 86; No. 12; Pp. 6537-6545; Bibl. 34 ref.</SO>
<LA>Anglais</LA>
<EA>The type II transmembrane protease TMPRSS2 activates the spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) on the cell surface following receptor binding during viral entry into cells. In the absence of TMPRSS2, SARS-CoV achieves cell entry via an endosomal pathway in which cathepsin L may play an important role, i.e., the activation of spike protein fusogenicity. This study shows that a commercial serine protease inhibitor (camostat) partially blocked infection by SARS-CoV and human coronavirus NL63 (HCoV-NL63) in HeLa cells expressing the receptor angiotensin-converting enzyme 2 (ACE2) and TMPRSS2. Simultaneous treatment of the cells with camostat and EST [(23,25)trans-epoarysuccinyl-L-leurylamindo-3-methylbutane ethyl ester], a cathepsin inhibitor, efficiently prevented both cell entry and the multistep growth of SARS-CoV in human Calu-3 airway epithelial cells. This efficient inhibition could be attributed to the dual blockade of entry from the cell surface and through the endosomal pathway. These observations suggest camostat as a candidate antiviral drug to prevent or depress TMPRSS2-dependent infection by SARS-CoV.</EA>
<CC>002A05C10</CC>
<FD>Homme; Coronavirus; Traitement; Cellule épithéliale; Cysteine endopeptidases; Syndrome respiratoire aigu sévère; Sérine; Inhibiteur protease; Antiviral</FD>
<FG>Coronaviridae; Nidovirales; Virus; Peptidases; Hydrolases; Enzyme; Virose; Infection; Pathologie de l'appareil respiratoire; Pathologie des poumons</FG>
<ED>Human; Coronavirus; Treatment; Epithelial cell; Cysteine endopeptidases; Severe acute respiratory syndrome; Serine; Protease inhibitor; Antiviral</ED>
<EG>Coronaviridae; Nidovirales; Virus; Peptidases; Hydrolases; Enzyme; Viral disease; Infection; Respiratory disease; Lung disease</EG>
<SD>Hombre; Coronavirus; Tratamiento; Célula epitelial; Cysteine endopeptidases; Síndrome respiratorio agudo severo; Serina; Inhibidor proteasa; Antiviral</SD>
<LO>INIST-13592.354000508304970150</LO>
<ID>12-0269207</ID>
</server>
</inist>
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Simultaneous Treatment of Human Bronchial Epithelial Cells with Serine and Cysteine Protease Inhibitors Prevents Severe Acute Respiratory Syndrome Coronavirus Entry

Simultaneous Treatment of Human Bronchial Epithelial Cells with Serine and Cysteine Protease Inhibitors Prevents Severe Acute Respiratory Syndrome Coronavirus Entry

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