Simultaneous Treatment of Human Bronchial Epithelial Cells with Serine and Cysteine Protease Inhibitors Prevents Severe Acute Respiratory Syndrome Coronavirus Entry
Identifieur interne : 001F62 ( Main/Exploration ); précédent : 001F61; suivant : 001F63Simultaneous Treatment of Human Bronchial Epithelial Cells with Serine and Cysteine Protease Inhibitors Prevents Severe Acute Respiratory Syndrome Coronavirus Entry
Auteurs : Miyuki Kawase [Japon] ; Kazuya Shirato [Japon] ; Lia Van Der Hoek [Pays-Bas] ; Fumihiro Taguchi [Japon] ; Shutoku Matsuyama [Japon]Source :
- Journal of virology [ 0022-538X ] ; 2012.
Descripteurs français
- KwdFr :
- Bronches (cytologie), Bronches (virologie), Cellules épithéliales (), Cellules épithéliales (virologie), Humains, Inhibiteurs de la cystéine protéinase (pharmacologie), Inhibiteurs de la sérine protéinase (pharmacologie), Pénétration virale (), Régulation négative (), Syndrome respiratoire aigu sévère (traitement médicamenteux), Syndrome respiratoire aigu sévère (virologie), Virus du SRAS (), Virus du SRAS (physiologie).
- MESH :
- cytologie : Bronches.
- pharmacologie : Inhibiteurs de la cystéine protéinase, Inhibiteurs de la sérine protéinase.
- physiologie : Virus du SRAS.
- traitement médicamenteux : Syndrome respiratoire aigu sévère.
- virologie : Bronches, Cellules épithéliales, Syndrome respiratoire aigu sévère.
- Pascal (Inist)
- Wicri :
- topic : Homme.
English descriptors
- KwdEn :
- Antiviral, Bronchi (cytology), Bronchi (virology), Coronavirus, Cysteine Proteinase Inhibitors (pharmacology), Cysteine endopeptidases, Down-Regulation (drug effects), Epithelial Cells (drug effects), Epithelial Cells (virology), Epithelial cell, Human, Humans, Protease inhibitor, SARS Virus (drug effects), SARS Virus (physiology), Serine, Serine Proteinase Inhibitors (pharmacology), Severe Acute Respiratory Syndrome (drug therapy), Severe Acute Respiratory Syndrome (virology), Severe acute respiratory syndrome, Treatment, Virus Internalization (drug effects).
- MESH :
- chemical , pharmacology : Cysteine Proteinase Inhibitors, Serine Proteinase Inhibitors.
- cytology : Bronchi.
- drug effects : Down-Regulation, Epithelial Cells, SARS Virus, Virus Internalization.
- drug therapy : Severe Acute Respiratory Syndrome.
- physiology : SARS Virus.
- virology : Bronchi, Epithelial Cells, Severe Acute Respiratory Syndrome.
- Humans.
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.
Url:
Affiliations:
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Le document en format XML
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sortKey="Shirato, Kazuya" sort="Shirato, Kazuya" uniqKey="Shirato K" first="Kazuya" last="Shirato">Kazuya Shirato</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Department of Virology III, National Institute of Infectious Diseases, Murayama Branch, Gakuen Musashi-Murayama</s1><s2>Tokyo</s2><s3>JPN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Japon</country><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Der Hoek, Lia Van" sort="Der Hoek, Lia Van" uniqKey="Der Hoek L" first="Lia Van" last="Der Hoek">Lia Van Der Hoek</name><affiliation wicri:level="4"><inist:fA14 i1="03"><s1>Department of Medical Microbiology, University of Amsterdam, Faculty of Earth and Life Sciences</s1><s2>Amsterdam</s2><s3>NLD</s3><sZ>3 aut.</sZ></inist:fA14><country>Pays-Bas</country><placeName><settlement type="city">Amsterdam</settlement><region nuts="2" 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Musashi-Murayama</s1><s2>Tokyo</s2><s3>JPN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Japon</country><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author></analytic><series><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiviral</term><term>Bronchi (cytology)</term><term>Bronchi (virology)</term><term>Coronavirus</term><term>Cysteine Proteinase Inhibitors (pharmacology)</term><term>Cysteine endopeptidases</term><term>Down-Regulation (drug effects)</term><term>Epithelial Cells (drug effects)</term><term>Epithelial Cells (virology)</term><term>Epithelial cell</term><term>Human</term><term>Humans</term><term>Protease inhibitor</term><term>SARS Virus (drug effects)</term><term>SARS Virus (physiology)</term><term>Serine</term><term>Serine Proteinase Inhibitors (pharmacology)</term><term>Severe Acute Respiratory Syndrome (drug therapy)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Severe acute respiratory syndrome</term><term>Treatment</term><term>Virus Internalization (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bronches (cytologie)</term><term>Bronches (virologie)</term><term>Cellules épithéliales ()</term><term>Cellules épithéliales (virologie)</term><term>Humains</term><term>Inhibiteurs de la cystéine protéinase (pharmacologie)</term><term>Inhibiteurs de la sérine protéinase (pharmacologie)</term><term>Pénétration virale ()</term><term>Régulation négative ()</term><term>Syndrome respiratoire aigu sévère (traitement médicamenteux)</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Virus du SRAS ()</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cysteine Proteinase Inhibitors</term><term>Serine Proteinase Inhibitors</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Bronches</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Bronchi</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Down-Regulation</term><term>Epithelial Cells</term><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="pharmacologie" xml:lang="fr"><term>Inhibiteurs de la cystéine protéinase</term><term>Inhibiteurs de la sérine protéinase</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Bronches</term><term>Cellules épithéliales</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Bronchi</term><term>Epithelial Cells</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Cellules épithéliales</term><term>Homme</term><term>Coronavirus</term><term>Humains</term><term>Pénétration virale</term><term>Régulation négative</term><term>Traitement</term><term>Cellule épithéliale</term><term>Cysteine endopeptidases</term><term>Syndrome respiratoire aigu sévère</term><term>Sérine</term><term>Inhibiteur protease</term><term>Antiviral</term><term>Virus du SRAS</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Homme</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>Japon</li><li>Pays-Bas</li></country><region><li>Hollande-Septentrionale</li><li>Région de Kantō</li></region><settlement><li>Amsterdam</li><li>Tokyo</li></settlement><orgName><li>Université d'Amsterdam</li></orgName></list><tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Kawase, Miyuki" sort="Kawase, Miyuki" uniqKey="Kawase M" first="Miyuki" last="Kawase">Miyuki Kawase</name></region><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name><name sortKey="Shirato, Kazuya" sort="Shirato, Kazuya" uniqKey="Shirato K" first="Kazuya" last="Shirato">Kazuya Shirato</name><name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name></country><country name="Pays-Bas"><region name="Hollande-Septentrionale"><name sortKey="Der Hoek, Lia Van" sort="Der Hoek, Lia Van" uniqKey="Der Hoek L" first="Lia Van" last="Der Hoek">Lia Van Der Hoek</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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