Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.
Identifieur interne : 000B95 ( PubMed/Corpus ); précédent : 000B94; suivant : 000B96Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.
Auteurs : Kazuya Shirato ; Kazuhiko Kanou ; Miyuki Kawase ; Shutoku MatsuyamaSource :
- Journal of virology [ 1098-5514 ] ; 2017.
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
Links to Exploration step
pubmed:27733646Le document en format XML
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Respiratory Viral Diseases and Cytokines, Department of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name><affiliation><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></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:27733646</idno><idno type="pmid">27733646</idno><idno type="doi">10.1128/JVI.01387-16</idno><idno type="wicri:Area/PubMed/Corpus">000B95</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" 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Kawase</name><affiliation><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></affiliation></author><author><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name><affiliation><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></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 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(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="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="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="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" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Protease Inhibitors</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></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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27733646</PMID><DateCompleted><Year>2017</Year><Month>05</Month><Day>15</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>16</Day></DateRevised><Article PubModel="Electronic-Print"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>91</Volume><Issue>1</Issue><PubDate><Year>2017</Year><Month>Jan</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">e01387-16</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.01387-16</ELocationID><Abstract><AbstractText>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.</AbstractText><AbstractText Label="IMPORTANCE" NlmCategory="OBJECTIVE">Many enveloped viruses enter cells through endocytosis. Viral spike proteins drive the fusion of viral and endosomal membranes to facilitate insertion of the viral genome into the cytoplasm. Human coronavirus 229E (HCoV-229E) utilizes endosomal cathepsin L to activate the spike protein after receptor binding. Here, we found that clinical isolates of HCoV-229E preferentially utilize the cell surface protease TMPRSS2 rather than endosomal cathepsin L. The endosome is a main site of Toll-like receptor recognition, which then triggers an innate immune response; therefore, HCoV-229E presumably evolved to bypass the endosome by entering the cell via TMPRSS2. Thus, the virus uses a simple mechanism to evade the host innate immune system. Therefore, therapeutic agents for coronavirus-mediated diseases, such as severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS), should target cell surface TMPRSS2 rather than endosomal cathepsin.</AbstractText><CopyrightInformation>Copyright © 2016 American Society for Microbiology.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shirato</LastName><ForeName>Kazuya</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Laboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kanou</LastName><ForeName>Kazuhiko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Infectious Disease Surveillance Center, National Institute of Infectious Diseases, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kawase</LastName><ForeName>Miyuki</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsuyama</LastName><ForeName>Shutoku</ForeName><Initials>S</Initials><AffiliationInfo><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.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>12</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="D012697">Serine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="C421305">TMPRSS2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.15</RegistryNumber><NameOfSubstance UI="C534281">CTSL protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.15</RegistryNumber><NameOfSubstance UI="D056668">Cathepsin L</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005075" MajorTopicYN="N">Biological Evolution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D056668" MajorTopicYN="N">Cathepsin L</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003139" MajorTopicYN="N">Common Cold</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D028941" MajorTopicYN="N">Coronavirus 229E, Human</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004705" MajorTopicYN="N">Endocytosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011992" MajorTopicYN="N">Endosomes</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004847" MajorTopicYN="N">Epithelial Cells</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057131" MajorTopicYN="Y">Immune Evasion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020545" MajorTopicYN="N">Respiratory Mucosa</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012697" MajorTopicYN="N">Serine Endopeptidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053586" MajorTopicYN="Y">Virus 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