Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease.
Identifieur interne : 001462 ( PubMed/Curation ); précédent : 001461; suivant : 001463Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease.
Auteurs : Stephanie Bertram [Allemagne] ; Ilona Glowacka ; Marcel A. Müller ; Hayley Lavender ; Kerstin Gnirss ; Inga Nehlmeier ; Daniela Niemeyer ; Yuxian He ; Graham Simmons ; Christian Drosten ; Elizabeth J. Soilleux ; Olaf Jahn ; Imke Steffen ; Stefan PöhlmannSource :
- Journal of virology [ 1098-5514 ] ; 2011.
Descripteurs français
- KwdFr :
- Expression des gènes, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Interactions hôte-pathogène, Lignée cellulaire, Peptidyl-Dipeptidase A (biosynthèse), Protéines de l'enveloppe virale (métabolisme), Protéolyse, Récepteurs viraux (biosynthèse), Serine endopeptidases (métabolisme), Virus du SRAS (pathogénicité).
- MESH :
- biosynthèse : Peptidyl-Dipeptidase A, Récepteurs viraux.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Serine endopeptidases.
- pathogénicité : Virus du SRAS.
- Expression des gènes, Glycoprotéine de spicule des coronavirus, Humains, Interactions hôte-pathogène, Lignée cellulaire, Protéolyse.
English descriptors
- KwdEn :
- Cell Line, Gene Expression, Host-Pathogen Interactions, Humans, Membrane Glycoproteins (metabolism), Peptidyl-Dipeptidase A (biosynthesis), Proteolysis, Receptors, Virus (biosynthesis), SARS Virus (pathogenicity), Serine Endopeptidases (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism).
- MESH :
- chemical , biosynthesis : Peptidyl-Dipeptidase A, Receptors, Virus.
- chemical , metabolism : Membrane Glycoproteins, Serine Endopeptidases, Viral Envelope Proteins.
- pathogenicity : SARS Virus.
- Cell Line, Gene Expression, Host-Pathogen Interactions, Humans, Proteolysis, Spike Glycoprotein, Coronavirus.
Abstract
The highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) poses a constant threat to human health. The viral spike protein (SARS-S) mediates host cell entry and is a potential target for antiviral intervention. Activation of SARS-S by host cell proteases is essential for SARS-CoV infectivity but remains incompletely understood. Here, we analyzed the role of the type II transmembrane serine proteases (TTSPs) human airway trypsin-like protease (HAT) and transmembrane protease, serine 2 (TMPRSS2), in SARS-S activation. We found that HAT activates SARS-S in the context of surrogate systems and authentic SARS-CoV infection and is coexpressed with the viral receptor angiotensin-converting enzyme 2 (ACE2) in bronchial epithelial cells and pneumocytes. HAT cleaved SARS-S at R667, as determined by mutagenesis and mass spectrometry, and activated SARS-S for cell-cell fusion in cis and trans, while the related pulmonary protease TMPRSS2 cleaved SARS-S at multiple sites and activated SARS-S only in trans. However, TMPRSS2 but not HAT expression rendered SARS-S-driven virus-cell fusion independent of cathepsin activity, indicating that HAT and TMPRSS2 activate SARS-S differentially. Collectively, our results show that HAT cleaves and activates SARS-S and might support viral spread in patients.
DOI: 10.1128/JVI.05300-11
PubMed: 21994442
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Müller</name></author><author><name sortKey="Lavender, Hayley" sort="Lavender, Hayley" uniqKey="Lavender H" first="Hayley" last="Lavender">Hayley Lavender</name></author><author><name sortKey="Gnirss, Kerstin" sort="Gnirss, Kerstin" uniqKey="Gnirss K" first="Kerstin" last="Gnirss">Kerstin Gnirss</name></author><author><name sortKey="Nehlmeier, Inga" sort="Nehlmeier, Inga" uniqKey="Nehlmeier I" first="Inga" last="Nehlmeier">Inga Nehlmeier</name></author><author><name sortKey="Niemeyer, Daniela" sort="Niemeyer, Daniela" uniqKey="Niemeyer D" first="Daniela" last="Niemeyer">Daniela Niemeyer</name></author><author><name sortKey="He, Yuxian" sort="He, Yuxian" uniqKey="He Y" first="Yuxian" last="He">Yuxian He</name></author><author><name sortKey="Simmons, Graham" sort="Simmons, Graham" uniqKey="Simmons G" first="Graham" last="Simmons">Graham Simmons</name></author><author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name></author><author><name sortKey="Soilleux, Elizabeth J" sort="Soilleux, Elizabeth J" uniqKey="Soilleux E" first="Elizabeth J" last="Soilleux">Elizabeth J. Soilleux</name></author><author><name sortKey="Jahn, Olaf" sort="Jahn, Olaf" uniqKey="Jahn O" first="Olaf" last="Jahn">Olaf Jahn</name></author><author><name sortKey="Steffen, Imke" sort="Steffen, Imke" uniqKey="Steffen I" first="Imke" last="Steffen">Imke Steffen</name></author><author><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line</term><term>Gene Expression</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Membrane Glycoproteins (metabolism)</term><term>Peptidyl-Dipeptidase A (biosynthesis)</term><term>Proteolysis</term><term>Receptors, Virus (biosynthesis)</term><term>SARS Virus (pathogenicity)</term><term>Serine Endopeptidases (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Expression des gènes</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Interactions hôte-pathogène</term><term>Lignée cellulaire</term><term>Peptidyl-Dipeptidase A (biosynthèse)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéolyse</term><term>Récepteurs viraux (biosynthèse)</term><term>Serine endopeptidases (métabolisme)</term><term>Virus du SRAS (pathogénicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Serine Endopeptidases</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Serine endopeptidases</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Gene Expression</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Proteolysis</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Expression des gènes</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Interactions hôte-pathogène</term><term>Lignée cellulaire</term><term>Protéolyse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) poses a constant threat to human health. The viral spike protein (SARS-S) mediates host cell entry and is a potential target for antiviral intervention. Activation of SARS-S by host cell proteases is essential for SARS-CoV infectivity but remains incompletely understood. Here, we analyzed the role of the type II transmembrane serine proteases (TTSPs) human airway trypsin-like protease (HAT) and transmembrane protease, serine 2 (TMPRSS2), in SARS-S activation. We found that HAT activates SARS-S in the context of surrogate systems and authentic SARS-CoV infection and is coexpressed with the viral receptor angiotensin-converting enzyme 2 (ACE2) in bronchial epithelial cells and pneumocytes. HAT cleaved SARS-S at R667, as determined by mutagenesis and mass spectrometry, and activated SARS-S for cell-cell fusion in cis and trans, while the related pulmonary protease TMPRSS2 cleaved SARS-S at multiple sites and activated SARS-S only in trans. However, TMPRSS2 but not HAT expression rendered SARS-S-driven virus-cell fusion independent of cathepsin activity, indicating that HAT and TMPRSS2 activate SARS-S differentially. Collectively, our results show that HAT cleaves and activates SARS-S and might support viral spread in patients.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21994442</PMID><DateCompleted><Year>2012</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>85</Volume><Issue>24</Issue><PubDate><Year>2011</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease.</ArticleTitle><Pagination><MedlinePgn>13363-72</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.05300-11</ELocationID><Abstract><AbstractText>The highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) poses a constant threat to human health. The viral spike protein (SARS-S) mediates host cell entry and is a potential target for antiviral intervention. Activation of SARS-S by host cell proteases is essential for SARS-CoV infectivity but remains incompletely understood. Here, we analyzed the role of the type II transmembrane serine proteases (TTSPs) human airway trypsin-like protease (HAT) and transmembrane protease, serine 2 (TMPRSS2), in SARS-S activation. We found that HAT activates SARS-S in the context of surrogate systems and authentic SARS-CoV infection and is coexpressed with the viral receptor angiotensin-converting enzyme 2 (ACE2) in bronchial epithelial cells and pneumocytes. HAT cleaved SARS-S at R667, as determined by mutagenesis and mass spectrometry, and activated SARS-S for cell-cell fusion in cis and trans, while the related pulmonary protease TMPRSS2 cleaved SARS-S at multiple sites and activated SARS-S only in trans. However, TMPRSS2 but not HAT expression rendered SARS-S-driven virus-cell fusion independent of cathepsin activity, indicating that HAT and TMPRSS2 activate SARS-S differentially. Collectively, our results show that HAT cleaves and activates SARS-S and might support viral spread in patients.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bertram</LastName><ForeName>Stephanie</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Institute of Virology, Hannover Medical School, Hannover, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Glowacka</LastName><ForeName>Ilona</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Müller</LastName><ForeName>Marcel A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Lavender</LastName><ForeName>Hayley</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Gnirss</LastName><ForeName>Kerstin</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Nehlmeier</LastName><ForeName>Inga</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Niemeyer</LastName><ForeName>Daniela</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>He</LastName><ForeName>Yuxian</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Simmons</LastName><ForeName>Graham</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Drosten</LastName><ForeName>Christian</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Soilleux</LastName><ForeName>Elizabeth J</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Jahn</LastName><ForeName>Olaf</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Steffen</LastName><ForeName>Imke</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Pöhlmann</LastName><ForeName>Stefan</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI074986</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01AI074986</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>10</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="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber><NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.17.-</RegistryNumber><NameOfSubstance UI="C413524">angiotensin converting enzyme 2</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="C112256">human airway trypsin-like protease</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054884" MajorTopicYN="Y">Host-Pathogen Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007703" MajorTopicYN="N">Peptidyl-Dipeptidase A</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="N">Proteolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName><QualifierName UI="Q000096" 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