Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.
Identifieur interne : 000832 ( PubMed/Corpus ); précédent : 000831; suivant : 000833Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.
Auteurs : Shutoku Matsuyama ; Kazuya Shirato ; Miyuki Kawase ; Yutaka Terada ; Kengo Kawachi ; Shuetsu Fukushi ; Wataru KamitaniSource :
- Journal of virology [ 1098-5514 ] ; 2018.
English descriptors
- KwdEn :
- Amino Acid Chloromethyl Ketones (pharmacology), Animals, Cathepsin B (antagonists & inhibitors), Cathepsin B (genetics), Cathepsin B (metabolism), Cathepsin L (antagonists & inhibitors), Cathepsin L (genetics), Cathepsin L (metabolism), Chlorocebus aethiops, Furin (antagonists & inhibitors), Furin (genetics), Furin (metabolism), Humans, Middle East Respiratory Syndrome Coronavirus (genetics), Middle East Respiratory Syndrome Coronavirus (metabolism), Papain (antagonists & inhibitors), Papain (genetics), Papain (metabolism), Proteolysis, Serine Endopeptidases (genetics), Serine Endopeptidases (metabolism), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Vero Cells, Virus Internalization.
- MESH :
- chemical , antagonists & inhibitors : Cathepsin B, Cathepsin L, Furin, Papain.
- chemical , genetics : Cathepsin B, Cathepsin L, Furin, Papain, Serine Endopeptidases, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Cathepsin B, Cathepsin L, Furin, Papain, Serine Endopeptidases, Spike Glycoprotein, Coronavirus.
- chemical , pharmacology : Amino Acid Chloromethyl Ketones.
- genetics : Middle East Respiratory Syndrome Coronavirus.
- metabolism : Middle East Respiratory Syndrome Coronavirus.
- Animals, Chlorocebus aethiops, Humans, Proteolysis, Vero Cells, Virus Internalization.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) utilizes host cellular proteases to enter cells. A previous report shows that furin, which is distributed mainly in the Golgi apparatus and cycled to the cell surface and endosomes, proteolytically activates the MERS-CoV spike (S) protein following receptor binding to mediate fusion between the viral and cellular membranes. In this study, we reexamined furin usage by MERS-CoV using a real-time PCR-based virus cell entry assay after inhibition of cellular proteases. We found that the furin inhibitor dec-RVKR-CMK blocked entry of MERS-CoV harboring an S protein lacking furin cleavage sites; it even blocked entry into furin-deficient LoVo cells. In addition, dec-RVKR-CMK inhibited not only the enzymatic activity of furin but also those of cathepsin L, cathepsin B, trypsin, papain, and TMPRSS2. Furthermore, a virus cell entry assay and a cell-cell fusion assay provided no evidence that the S protein was activated by exogenous furin. Therefore, we conclude that furin does not play a role in entry of MERS-CoV into cells and that the inhibitory effect of dec-RVKR-CMK is specific for TMPRSS2 and cathepsin L rather than furin.IMPORTANCE Previous studies using the furin inhibitor dec-RVKR-CMK suggest that MERS-CoV utilizes a cellular protease, furin, to activate viral glycoproteins during cell entry. However, we found that dec-RVKR-CMK inhibits not only furin but also other proteases. Furthermore, we found no evidence that MERS-CoV uses furin. These findings suggest that previous studies in the virology field based on dec-RVKR-CMK should be reexamined carefully. Here we describe appropriate experiments that can be used to assess the effect of protease inhibitors on virus cell entry.
DOI: 10.1128/JVI.00683-18
PubMed: 30021905
Links to Exploration step
pubmed:30021905Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.</title><author><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name><affiliation><nlm:affiliation>Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan matuyama@nih.go.jp.</nlm:affiliation></affiliation></author><author><name sortKey="Shirato, Kazuya" sort="Shirato, Kazuya" uniqKey="Shirato K" first="Kazuya" last="Shirato">Kazuya Shirato</name><affiliation><nlm:affiliation>Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kawase, Miyuki" sort="Kawase, Miyuki" uniqKey="Kawase M" first="Miyuki" last="Kawase">Miyuki Kawase</name><affiliation><nlm:affiliation>Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Terada, Yutaka" sort="Terada, Yutaka" uniqKey="Terada Y" first="Yutaka" last="Terada">Yutaka Terada</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka University, Osaka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kawachi, Kengo" sort="Kawachi, Kengo" uniqKey="Kawachi K" first="Kengo" last="Kawachi">Kengo Kawachi</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka University, Osaka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Fukushi, Shuetsu" sort="Fukushi, Shuetsu" uniqKey="Fukushi S" first="Shuetsu" last="Fukushi">Shuetsu Fukushi</name><affiliation><nlm:affiliation>Department of Virology I, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kamitani, Wataru" sort="Kamitani, Wataru" uniqKey="Kamitani W" first="Wataru" last="Kamitani">Wataru Kamitani</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka University, Osaka, Japan.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:30021905</idno><idno type="pmid">30021905</idno><idno type="doi">10.1128/JVI.00683-18</idno><idno type="wicri:Area/PubMed/Corpus">000832</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000832</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.</title><author><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name><affiliation><nlm:affiliation>Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan matuyama@nih.go.jp.</nlm:affiliation></affiliation></author><author><name sortKey="Shirato, Kazuya" sort="Shirato, Kazuya" uniqKey="Shirato K" first="Kazuya" last="Shirato">Kazuya Shirato</name><affiliation><nlm:affiliation>Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kawase, Miyuki" sort="Kawase, Miyuki" uniqKey="Kawase M" first="Miyuki" last="Kawase">Miyuki Kawase</name><affiliation><nlm:affiliation>Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Terada, Yutaka" sort="Terada, Yutaka" uniqKey="Terada Y" first="Yutaka" last="Terada">Yutaka Terada</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka University, Osaka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kawachi, Kengo" sort="Kawachi, Kengo" uniqKey="Kawachi K" first="Kengo" last="Kawachi">Kengo Kawachi</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka University, Osaka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Fukushi, Shuetsu" sort="Fukushi, Shuetsu" uniqKey="Fukushi S" first="Shuetsu" last="Fukushi">Shuetsu Fukushi</name><affiliation><nlm:affiliation>Department of Virology I, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kamitani, Wataru" sort="Kamitani, Wataru" uniqKey="Kamitani W" first="Wataru" last="Kamitani">Wataru Kamitani</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka University, Osaka, Japan.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Chloromethyl Ketones (pharmacology)</term><term>Animals</term><term>Cathepsin B (antagonists & inhibitors)</term><term>Cathepsin B (genetics)</term><term>Cathepsin B (metabolism)</term><term>Cathepsin L (antagonists & inhibitors)</term><term>Cathepsin L (genetics)</term><term>Cathepsin L (metabolism)</term><term>Chlorocebus aethiops</term><term>Furin (antagonists & inhibitors)</term><term>Furin (genetics)</term><term>Furin (metabolism)</term><term>Humans</term><term>Middle East Respiratory Syndrome Coronavirus (genetics)</term><term>Middle East Respiratory Syndrome Coronavirus (metabolism)</term><term>Papain (antagonists & inhibitors)</term><term>Papain (genetics)</term><term>Papain (metabolism)</term><term>Proteolysis</term><term>Serine Endopeptidases (genetics)</term><term>Serine Endopeptidases (metabolism)</term><term>Spike Glycoprotein, Coronavirus (genetics)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Vero Cells</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Cathepsin B</term><term>Cathepsin L</term><term>Furin</term><term>Papain</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cathepsin B</term><term>Cathepsin L</term><term>Furin</term><term>Papain</term><term>Serine Endopeptidases</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cathepsin B</term><term>Cathepsin L</term><term>Furin</term><term>Papain</term><term>Serine Endopeptidases</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Amino Acid Chloromethyl Ketones</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Proteolysis</term><term>Vero Cells</term><term>Virus Internalization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) utilizes host cellular proteases to enter cells. A previous report shows that furin, which is distributed mainly in the Golgi apparatus and cycled to the cell surface and endosomes, proteolytically activates the MERS-CoV spike (S) protein following receptor binding to mediate fusion between the viral and cellular membranes. In this study, we reexamined furin usage by MERS-CoV using a real-time PCR-based virus cell entry assay after inhibition of cellular proteases. We found that the furin inhibitor dec-RVKR-CMK blocked entry of MERS-CoV harboring an S protein lacking furin cleavage sites; it even blocked entry into furin-deficient LoVo cells. In addition, dec-RVKR-CMK inhibited not only the enzymatic activity of furin but also those of cathepsin L, cathepsin B, trypsin, papain, and TMPRSS2. Furthermore, a virus cell entry assay and a cell-cell fusion assay provided no evidence that the S protein was activated by exogenous furin. Therefore, we conclude that furin does not play a role in entry of MERS-CoV into cells and that the inhibitory effect of dec-RVKR-CMK is specific for TMPRSS2 and cathepsin L rather than furin.<b>IMPORTANCE</b> Previous studies using the furin inhibitor dec-RVKR-CMK suggest that MERS-CoV utilizes a cellular protease, furin, to activate viral glycoproteins during cell entry. However, we found that dec-RVKR-CMK inhibits not only furin but also other proteases. Furthermore, we found no evidence that MERS-CoV uses furin. These findings suggest that previous studies in the virology field based on dec-RVKR-CMK should be reexamined carefully. Here we describe appropriate experiments that can be used to assess the effect of protease inhibitors on virus cell entry.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30021905</PMID><DateCompleted><Year>2018</Year><Month>09</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Electronic-Print"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>92</Volume><Issue>19</Issue><PubDate><Year>2018</Year><Month>10</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">e00683-18</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.00683-18</ELocationID><Abstract><AbstractText>Middle East respiratory syndrome coronavirus (MERS-CoV) utilizes host cellular proteases to enter cells. A previous report shows that furin, which is distributed mainly in the Golgi apparatus and cycled to the cell surface and endosomes, proteolytically activates the MERS-CoV spike (S) protein following receptor binding to mediate fusion between the viral and cellular membranes. In this study, we reexamined furin usage by MERS-CoV using a real-time PCR-based virus cell entry assay after inhibition of cellular proteases. We found that the furin inhibitor dec-RVKR-CMK blocked entry of MERS-CoV harboring an S protein lacking furin cleavage sites; it even blocked entry into furin-deficient LoVo cells. In addition, dec-RVKR-CMK inhibited not only the enzymatic activity of furin but also those of cathepsin L, cathepsin B, trypsin, papain, and TMPRSS2. Furthermore, a virus cell entry assay and a cell-cell fusion assay provided no evidence that the S protein was activated by exogenous furin. Therefore, we conclude that furin does not play a role in entry of MERS-CoV into cells and that the inhibitory effect of dec-RVKR-CMK is specific for TMPRSS2 and cathepsin L rather than furin.<b>IMPORTANCE</b> Previous studies using the furin inhibitor dec-RVKR-CMK suggest that MERS-CoV utilizes a cellular protease, furin, to activate viral glycoproteins during cell entry. However, we found that dec-RVKR-CMK inhibits not only furin but also other proteases. Furthermore, we found no evidence that MERS-CoV uses furin. These findings suggest that previous studies in the virology field based on dec-RVKR-CMK should be reexamined carefully. Here we describe appropriate experiments that can be used to assess the effect of protease inhibitors on virus cell entry.</AbstractText><CopyrightInformation>Copyright © 2018 American Society for Microbiology.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Matsuyama</LastName><ForeName>Shutoku</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan matuyama@nih.go.jp.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shirato</LastName><ForeName>Kazuya</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kawase</LastName><ForeName>Miyuki</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Terada</LastName><ForeName>Yutaka</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka University, Osaka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kawachi</LastName><ForeName>Kengo</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka University, Osaka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fukushi</LastName><ForeName>Shuetsu</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Virology I, National Institute of Infectious Diseases, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kamitani</LastName><ForeName>Wataru</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka University, Osaka, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>09</Month><Day>12</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="D000590">Amino Acid Chloromethyl Ketones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C460143">decanoylRVKRchloromethylketone</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 3.4.21.75</RegistryNumber><NameOfSubstance UI="C468731">FURIN protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.75</RegistryNumber><NameOfSubstance UI="D045683">Furin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.1</RegistryNumber><NameOfSubstance UI="C533912">CTSB protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.1</RegistryNumber><NameOfSubstance UI="D002401">Cathepsin B</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><Chemical><RegistryNumber>EC 3.4.22.2</RegistryNumber><NameOfSubstance UI="D010206">Papain</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000590" MajorTopicYN="N">Amino Acid Chloromethyl Ketones</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002401" MajorTopicYN="N">Cathepsin B</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D056668" MajorTopicYN="N">Cathepsin L</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045683" MajorTopicYN="N">Furin</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010206" MajorTopicYN="N">Papain</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="Y">Proteolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012697" MajorTopicYN="N">Serine Endopeptidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053586" MajorTopicYN="Y">Virus Internalization</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">TMPRSS2</Keyword><Keyword MajorTopicYN="Y">cathepsin L</Keyword><Keyword MajorTopicYN="Y">coronavirus</Keyword><Keyword MajorTopicYN="Y">dec-RVKR-CMK</Keyword><Keyword MajorTopicYN="Y">furin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>04</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>07</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>7</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>7</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30021905</ArticleId><ArticleId IdType="pii">JVI.00683-18</ArticleId><ArticleId IdType="doi">10.1128/JVI.00683-18</ArticleId><ArticleId IdType="pmc">PMC6146822</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4240-5</Citation><ArticleIdList><ArticleId IdType="pubmed">15010527</ArticleId></ArticleIdList></Reference><Reference><Citation>Biomol Concepts. 2011 Oct 1;2(5):421-438</Citation><ArticleIdList><ArticleId IdType="pubmed">22308173</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2013 Dec;87(23):12552-61</Citation><ArticleIdList><ArticleId IdType="pubmed">24027332</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2008 Sep;82(17):8887-90</Citation><ArticleIdList><ArticleId IdType="pubmed">18562523</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Med (Berl). 2005 Nov;83(11):844-55</Citation><ArticleIdList><ArticleId IdType="pubmed">16215768</ArticleId></ArticleIdList></Reference><Reference><Citation>Traffic. 2016 Jun;17(6):593-614</Citation><ArticleIdList><ArticleId IdType="pubmed">26935856</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2008 Sep;82(17):8942-6</Citation><ArticleIdList><ArticleId IdType="pubmed">18562527</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2016 Oct 25;113(43):12262-12267</Citation><ArticleIdList><ArticleId IdType="pubmed">27791014</ArticleId></ArticleIdList></Reference><Reference><Citation>J Infect Dis. 2015 Mar 15;211(6):889-97</Citation><ArticleIdList><ArticleId IdType="pubmed">25057042</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Virol. 2015 Sep;160(9):2293-300</Citation><ArticleIdList><ArticleId IdType="pubmed">26138557</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 1993 Sep 15;195(2):1019-26</Citation><ArticleIdList><ArticleId IdType="pubmed">7690548</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Mol Cell Biol. 2002 Oct;3(10):753-66</Citation><ArticleIdList><ArticleId IdType="pubmed">12360192</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2009 Nov;83(21):11133-41</Citation><ArticleIdList><ArticleId IdType="pubmed">19706706</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2013 Sep;87(17):9953-8</Citation><ArticleIdList><ArticleId IdType="pubmed">23824802</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2009 Jun 5;284(23):15729-38</Citation><ArticleIdList><ArticleId IdType="pubmed">19332539</ArticleId></ArticleIdList></Reference><Reference><Citation>Neoplasia. 2008 Apr;10(4):363-70</Citation><ArticleIdList><ArticleId IdType="pubmed">18392131</ArticleId></ArticleIdList></Reference><Reference><Citation>Antimicrob Agents Chemother. 2016 Oct 21;60(11):6532-6539</Citation><ArticleIdList><ArticleId IdType="pubmed">27550352</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1995 Nov 3;270(44):26565-9</Citation><ArticleIdList><ArticleId IdType="pubmed">7592877</ArticleId></ArticleIdList></Reference><Reference><Citation>Virus Res. 2015 Apr 16;202:120-34</Citation><ArticleIdList><ArticleId IdType="pubmed">25445340</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2008 Dec;82(23):11985-91</Citation><ArticleIdList><ArticleId IdType="pubmed">18786990</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS Pathog. 2014 Nov 06;10(11):e1004502</Citation><ArticleIdList><ArticleId IdType="pubmed">25375324</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Pharmacol. 2017 Sep 15;140:8-15</Citation><ArticleIdList><ArticleId IdType="pubmed">28456517</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2012 Jun 22;287(26):21992-2003</Citation><ArticleIdList><ArticleId IdType="pubmed">22539349</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2014 Oct 21;111(42):15214-9</Citation><ArticleIdList><ArticleId IdType="pubmed">25288733</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2017 Jun 21;12(6):e0179177</Citation><ArticleIdList><ArticleId IdType="pubmed">28636671</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2014 May;88(9):4953-61</Citation><ArticleIdList><ArticleId IdType="pubmed">24554656</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2009 Apr 7;106(14):5871-6</Citation><ArticleIdList><ArticleId IdType="pubmed">19321428</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2004 Jun;78(11):6048-54</Citation><ArticleIdList><ArticleId IdType="pubmed">15141003</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Virol. 2013 Aug;94(Pt 8):1749-60</Citation><ArticleIdList><ArticleId IdType="pubmed">23620378</ArticleId></ArticleIdList></Reference><Reference><Citation>Viruses. 2012 Apr;4(4):557-80</Citation><ArticleIdList><ArticleId IdType="pubmed">22590686</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2017 Nov;511:95-105</Citation><ArticleIdList><ArticleId IdType="pubmed">28843094</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2013 May;87(10):5502-11</Citation><ArticleIdList><ArticleId IdType="pubmed">23468491</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000832 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 000832 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:30021905
|texte= Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:30021905" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |