Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.
Identifieur interne : 000E63 ( Main/Exploration ); précédent : 000E62; suivant : 000E64Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.
Auteurs : Kazuya Shirato [Japon] ; Kazuhiko Kanou [Japon] ; Miyuki Kawase [Japon] ; Shutoku Matsuyama [Japon]Source :
- Journal of virology [ 1098-5514 ] ; 2017.
Descripteurs français
- KwdFr :
- Alignement de séquences, Cathepsine L (antagonistes et inhibiteurs), Cathepsine L (génétique), Cathepsine L (immunologie), Cellules HeLa, Cellules épithéliales (), Cellules épithéliales (immunologie), Cellules épithéliales (virologie), Coronavirus humain 229E (génétique), Coronavirus humain 229E (métabolisme), Endocytose, Endosomes (), Endosomes (immunologie), Endosomes (virologie), Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Infections à coronavirus (immunologie), Infections à coronavirus (virologie), Inhibiteurs de protéases (pharmacologie), Membrane cellulaire (immunologie), Membrane cellulaire (virologie), Muqueuse respiratoire (), Muqueuse respiratoire (immunologie), Muqueuse respiratoire (virologie), Mutation, Pénétration virale, Rhume banal (immunologie), Rhume banal (virologie), Serine endopeptidases (génétique), Serine endopeptidases (immunologie), Substitution d'acide aminé, Séquence d'acides aminés, Échappement immunitaire, Évolution biologique.
- MESH :
- antagonistes et inhibiteurs : Cathepsine L.
- génétique : Cathepsine L, Coronavirus humain 229E, Glycoprotéine de spicule des coronavirus, Serine endopeptidases.
- immunologie : Cathepsine L, Cellules épithéliales, Endosomes, Infections à coronavirus, Membrane cellulaire, Muqueuse respiratoire, Rhume banal, Serine endopeptidases.
- métabolisme : Coronavirus humain 229E, Glycoprotéine de spicule des coronavirus.
- pharmacologie : Inhibiteurs de protéases.
- virologie : Cellules épithéliales, Endosomes, Infections à coronavirus, Membrane cellulaire, Muqueuse respiratoire, Rhume banal.
- Alignement de séquences, Cellules HeLa, Cellules épithéliales, Endocytose, Endosomes, Humains, Muqueuse respiratoire, Mutation, Pénétration virale, Substitution d'acide aminé, Séquence d'acides aminés, Échappement immunitaire, Évolution biologique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Biological Evolution, Cathepsin L (antagonists & inhibitors), Cathepsin L (genetics), Cathepsin L (immunology), Cell Membrane (immunology), Cell Membrane (virology), Common Cold (immunology), Common Cold (virology), Coronavirus 229E, Human (genetics), Coronavirus 229E, Human (metabolism), Coronavirus Infections (immunology), Coronavirus Infections (virology), Endocytosis, Endosomes (drug effects), Endosomes (immunology), Endosomes (virology), Epithelial Cells (drug effects), Epithelial Cells (immunology), Epithelial Cells (virology), HeLa Cells, Humans, Immune Evasion, Mutation, Protease Inhibitors (pharmacology), Respiratory Mucosa (drug effects), Respiratory Mucosa (immunology), Respiratory Mucosa (virology), Sequence Alignment, Serine Endopeptidases (genetics), Serine Endopeptidases (immunology), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Virus Internalization.
- MESH :
- chemical , antagonists & inhibitors : Cathepsin L.
- chemical , genetics : Cathepsin L, Serine Endopeptidases, Spike Glycoprotein, Coronavirus.
- chemical , immunology : Cathepsin L, Serine Endopeptidases.
- drug effects : Endosomes, Epithelial Cells, Respiratory Mucosa.
- genetics : Coronavirus 229E, Human.
- immunology : Cell Membrane, Common Cold, Coronavirus Infections, Endosomes, Epithelial Cells, Respiratory Mucosa.
- metabolism : Coronavirus 229E, Human, Spike Glycoprotein, Coronavirus.
- chemical , pharmacology : Protease Inhibitors.
- virology : Cell Membrane, Common Cold, Coronavirus Infections, Endosomes, Epithelial Cells, Respiratory Mucosa.
- Amino Acid Sequence, Amino Acid Substitution, Biological Evolution, Endocytosis, HeLa Cells, Humans, Immune Evasion, Mutation, Sequence Alignment, Virus Internalization.
Abstract
Human coronavirus 229E (HCoV-229E), a causative agent of the common cold, enters host cells via two distinct pathways: one is mediated by cell surface proteases, particularly transmembrane protease serine 2 (TMPRSS2), and the other by endosomal cathepsin L. Thus, specific inhibitors of these proteases block virus infection. However, it is unclear which of these pathways is actually utilized by HCoV-229E in the human respiratory tract. Here, we examined the mechanism of cell entry used by a pseudotyped virus bearing the HCoV-229E spike (S) protein in the presence or absence of protease inhibitors. We found that, compared with a laboratory strain isolated in 1966 and passaged for a half century, clinical isolates of HCoV-229E were less likely to utilize cathepsin L; rather, they showed a preference for TMPRSS2. Two amino acid substitutions (R642M and N714K) in the S protein of HCoV-229E clinical isolates altered their sensitivity to a cathepsin L inhibitor, suggesting that these amino acids were responsible for cathepsin L use. After 20 passages in HeLa cells, the ability of the isolate to use cathepsin increased so that it was equal to that of the laboratory strain; this increase was caused by an amino acid substitution (I577S) in the S protein. The passaged virus showed a reduced ability to replicate in differentiated airway epithelial cells cultured at an air-liquid interface. These results suggest that the endosomal pathway is disadvantageous for HCoV-229E infection of human airway epithelial cells; therefore, clinical isolates are less able to use cathepsin.
DOI: 10.1128/JVI.01387-16
PubMed: 27733646
Affiliations:
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xml:lang="en">Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.</title><author><name sortKey="Shirato, Kazuya" sort="Shirato, Kazuya" uniqKey="Shirato K" first="Kazuya" last="Shirato">Kazuya Shirato</name><affiliation wicri:level="3"><nlm:affiliation>Laboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Kanou, Kazuhiko" sort="Kanou, Kazuhiko" uniqKey="Kanou K" first="Kazuhiko" last="Kanou">Kazuhiko Kanou</name><affiliation wicri:level="3"><nlm:affiliation>Infectious Disease Surveillance Center, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Infectious Disease Surveillance Center, National Institute of Infectious Diseases, Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Kawase, Miyuki" sort="Kawase, Miyuki" uniqKey="Kawase M" first="Miyuki" last="Kawase">Miyuki Kawase</name><affiliation wicri:level="3"><nlm:affiliation>Laboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name><affiliation wicri:level="3"><nlm:affiliation>Laboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan matuyama@nih.go.jp.</nlm:affiliation><country wicri:rule="url">Japon</country><wicri:regionArea>Laboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Biological Evolution</term><term>Cathepsin L (antagonists & inhibitors)</term><term>Cathepsin L (genetics)</term><term>Cathepsin L (immunology)</term><term>Cell Membrane (immunology)</term><term>Cell Membrane (virology)</term><term>Common Cold (immunology)</term><term>Common Cold (virology)</term><term>Coronavirus 229E, Human (genetics)</term><term>Coronavirus 229E, Human (metabolism)</term><term>Coronavirus Infections (immunology)</term><term>Coronavirus Infections (virology)</term><term>Endocytosis</term><term>Endosomes (drug effects)</term><term>Endosomes (immunology)</term><term>Endosomes (virology)</term><term>Epithelial Cells (drug effects)</term><term>Epithelial Cells (immunology)</term><term>Epithelial Cells (virology)</term><term>HeLa Cells</term><term>Humans</term><term>Immune Evasion</term><term>Mutation</term><term>Protease Inhibitors (pharmacology)</term><term>Respiratory Mucosa (drug effects)</term><term>Respiratory Mucosa (immunology)</term><term>Respiratory Mucosa (virology)</term><term>Sequence Alignment</term><term>Serine Endopeptidases (genetics)</term><term>Serine Endopeptidases (immunology)</term><term>Spike Glycoprotein, Coronavirus (genetics)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term><term>Cathepsine L (antagonistes et inhibiteurs)</term><term>Cathepsine L (génétique)</term><term>Cathepsine L (immunologie)</term><term>Cellules HeLa</term><term>Cellules épithéliales ()</term><term>Cellules épithéliales (immunologie)</term><term>Cellules épithéliales (virologie)</term><term>Coronavirus humain 229E (génétique)</term><term>Coronavirus humain 229E (métabolisme)</term><term>Endocytose</term><term>Endosomes ()</term><term>Endosomes (immunologie)</term><term>Endosomes (virologie)</term><term>Glycoprotéine de spicule des coronavirus (génétique)</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Humains</term><term>Infections à coronavirus (immunologie)</term><term>Infections à coronavirus (virologie)</term><term>Inhibiteurs de protéases (pharmacologie)</term><term>Membrane cellulaire (immunologie)</term><term>Membrane cellulaire (virologie)</term><term>Muqueuse respiratoire ()</term><term>Muqueuse respiratoire (immunologie)</term><term>Muqueuse respiratoire (virologie)</term><term>Mutation</term><term>Pénétration virale</term><term>Rhume banal (immunologie)</term><term>Rhume banal (virologie)</term><term>Serine endopeptidases (génétique)</term><term>Serine endopeptidases (immunologie)</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term><term>Échappement immunitaire</term><term>Évolution biologique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Cathepsin L</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cathepsin L</term><term>Serine Endopeptidases</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Cathepsin L</term><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Cathepsine L</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Endosomes</term><term>Epithelial Cells</term><term>Respiratory Mucosa</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coronavirus 229E, Human</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cathepsine L</term><term>Coronavirus humain 229E</term><term>Glycoprotéine de spicule des coronavirus</term><term>Serine endopeptidases</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Cathepsine L</term><term>Cellules épithéliales</term><term>Endosomes</term><term>Infections à coronavirus</term><term>Membrane cellulaire</term><term>Muqueuse respiratoire</term><term>Rhume banal</term><term>Serine endopeptidases</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Cell Membrane</term><term>Common Cold</term><term>Coronavirus Infections</term><term>Endosomes</term><term>Epithelial Cells</term><term>Respiratory Mucosa</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus 229E, Human</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus humain 229E</term><term>Glycoprotéine de spicule des coronavirus</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de protéases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Cellules épithéliales</term><term>Endosomes</term><term>Infections à coronavirus</term><term>Membrane cellulaire</term><term>Muqueuse respiratoire</term><term>Rhume banal</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Cell Membrane</term><term>Common Cold</term><term>Coronavirus Infections</term><term>Endosomes</term><term>Epithelial Cells</term><term>Respiratory Mucosa</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Biological Evolution</term><term>Endocytosis</term><term>HeLa Cells</term><term>Humans</term><term>Immune Evasion</term><term>Mutation</term><term>Sequence Alignment</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Cellules HeLa</term><term>Cellules épithéliales</term><term>Endocytose</term><term>Endosomes</term><term>Humains</term><term>Muqueuse respiratoire</term><term>Mutation</term><term>Pénétration virale</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term><term>Échappement immunitaire</term><term>Évolution biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human coronavirus 229E (HCoV-229E), a causative agent of the common cold, enters host cells via two distinct pathways: one is mediated by cell surface proteases, particularly transmembrane protease serine 2 (TMPRSS2), and the other by endosomal cathepsin L. Thus, specific inhibitors of these proteases block virus infection. However, it is unclear which of these pathways is actually utilized by HCoV-229E in the human respiratory tract. Here, we examined the mechanism of cell entry used by a pseudotyped virus bearing the HCoV-229E spike (S) protein in the presence or absence of protease inhibitors. We found that, compared with a laboratory strain isolated in 1966 and passaged for a half century, clinical isolates of HCoV-229E were less likely to utilize cathepsin L; rather, they showed a preference for TMPRSS2. Two amino acid substitutions (R642M and N714K) in the S protein of HCoV-229E clinical isolates altered their sensitivity to a cathepsin L inhibitor, suggesting that these amino acids were responsible for cathepsin L use. After 20 passages in HeLa cells, the ability of the isolate to use cathepsin increased so that it was equal to that of the laboratory strain; this increase was caused by an amino acid substitution (I577S) in the S protein. The passaged virus showed a reduced ability to replicate in differentiated airway epithelial cells cultured at an air-liquid interface. These results suggest that the endosomal pathway is disadvantageous for HCoV-229E infection of human airway epithelial cells; therefore, clinical isolates are less able to use cathepsin.</div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Shirato, Kazuya" sort="Shirato, Kazuya" uniqKey="Shirato K" first="Kazuya" last="Shirato">Kazuya Shirato</name></region><name sortKey="Kanou, Kazuhiko" sort="Kanou, Kazuhiko" uniqKey="Kanou K" first="Kazuhiko" last="Kanou">Kazuhiko Kanou</name><name sortKey="Kawase, Miyuki" sort="Kawase, Miyuki" uniqKey="Kawase M" first="Miyuki" last="Kawase">Miyuki Kawase</name><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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