SrasV1, PascalFrancis, Corpus, bibRecord, 000078

Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease

Identifieur interne : 000078 ( PascalFrancis/Corpus ); précédent : 000077; suivant : 000079

Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease

Auteurs : Stephanie Bertram ; 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 Pöhlmann

Source :

Journal of virology [ 0022-538X ] ; 2011.

RBID : Pascal:12-0041035

Descripteurs français

Pascal (Inist)
- Coronavirus, Homme, Protéine, Voie respiratoire, Syndrome respiratoire aigu sévère.

English descriptors

KwdEn :
- Coronavirus, Human, Protein, Respiratory tract, Severe acute respiratory syndrome.

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.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A11	`14`	`1`		`@1 PÖHLMANN (Stefan)`
A14	`01`			`@1 Institute of Virology, Hannover Medical School @2 Hannover @3 DEU @Z 1 aut. @Z 2 aut. @Z 5 aut. @Z 13 aut. @Z 14 aut.`
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A14	`03`			`@1 Institute of Virology, University of Bonn Medical Centre @2 Bonn @3 DEU @Z 3 aut. @Z 7 aut. @Z 10 aut.`
A14	`04`			`@1 Oxfabs, Nuffield Department of Clinical Laboratory Sciences, John Radcliffe Hospital, University of Oxford @2 Oxford @3 GBR @Z 4 aut.`
A14	`05`			`@1 Institute of Pathogen Biology, Chinese Academy of Medical Sciences, and Peking Union Medical College @2 Beijing @3 CHN @Z 8 aut.`
A14	`06`			`@1 Blood Systems Research Institute and Department of Laboratory Medicine, University of California @2 San Francisco, California @3 USA @Z 9 aut. @Z 13 aut.`
A14	`07`			`@1 Department of Cellular Pathology, John Radcliffe Hospital @2 Oxford @3 GBR @Z 11 aut.`
A14	`08`			`@1 Nuffield Department of Clinical Laboratory Sciences, John Radcliffe Hospital, University of Oxford @3 GBR @Z 11 aut.`
A14	`09`			`@1 Proteomics Group, Max Planck Institute of Experimental Medicine @2 Göttingen @3 DEU @Z 12 aut.`
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C01	`01`		`ENG`	@0 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.
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C03	`02`	`X`	`FRE`	`@0 Homme @5 02`
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C03	`03`	`X`	`ENG`	`@0 Protein @5 05`
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C07	`04`	`X`	`ENG`	`@0 Respiratory disease @5 13`
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C07	`05`	`X`	`FRE`	`@0 Virose`
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Format Inist (serveur)

NO :	PASCAL 12-0041035 INIST
ET :	Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease
AU :	BERTRAM (Stephanie); GLOWACKA (Ilona); MÜLLER (Marcel A.); LAVENDER (Hayley); GNIRSS (Kerstin); NEHLMEIER (Inga); NIEMEYER (Daniela); YUXIAN HE; SIMMONS (Graham); DROSTEN (Christian); SOILLEUX (Elizabeth J.); JAHN (Olaf); STEFFEN (Imke); PÖHLMANN (Stefan)
AF :	Institute of Virology, Hannover Medical School/Hannover/Allemagne (1 aut., 2 aut., 5 aut., 13 aut., 14 aut.); German Primate Center/Göttingen/Allemagne (1 aut., 6 aut., 14 aut.); Institute of Virology, University of Bonn Medical Centre/Bonn/Allemagne (3 aut., 7 aut., 10 aut.); Oxfabs, Nuffield Department of Clinical Laboratory Sciences, John Radcliffe Hospital, University of Oxford/Oxford/Royaume-Uni (4 aut.); Institute of Pathogen Biology, Chinese Academy of Medical Sciences, and Peking Union Medical College/Beijing/Chine (8 aut.); Blood Systems Research Institute and Department of Laboratory Medicine, University of California/San Francisco, California/Etats-Unis (9 aut., 13 aut.); Department of Cellular Pathology, John Radcliffe Hospital/Oxford/Royaume-Uni (11 aut.); Nuffield Department of Clinical Laboratory Sciences, John Radcliffe Hospital, University of Oxford/Royaume-Uni (11 aut.); Proteomics Group, Max Planck Institute of Experimental Medicine/Göttingen/Allemagne (12 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2011; Vol. 85; No. 24; Pp. 13363-13372; Bibl. 49 ref.
LA :	Anglais
EA :	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.
CC :	002A05C10
FD :	Coronavirus; Homme; Protéine; Voie respiratoire; Syndrome respiratoire aigu sévère
FG :	Coronaviridae; Nidovirales; Virus; Pathologie de l'appareil respiratoire; Virose; Infection; Pathologie des poumons
ED :	Coronavirus; Human; Protein; Respiratory tract; Severe acute respiratory syndrome
EG :	Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease
SD :	Coronavirus; Hombre; Proteína; Vía respiratoria; Síndrome respiratorio agudo severo
LO :	INIST-13592.354000505971530510
ID :	12-0041035

Links to Exploration step

Pascal:12-0041035

Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease</title>
<author><name sortKey="Bertram, Stephanie" sort="Bertram, Stephanie" uniqKey="Bertram S" first="Stephanie" last="Bertram">Stephanie Bertram</name>
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<author><name sortKey="Glowacka, Ilona" sort="Glowacka, Ilona" uniqKey="Glowacka I" first="Ilona" last="Glowacka">Ilona Glowacka</name>
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<author><name sortKey="Muller, Marcel A" sort="Muller, Marcel A" uniqKey="Muller M" first="Marcel A." last="Müller">Marcel A. Müller</name>
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<author><name sortKey="Lavender, Hayley" sort="Lavender, Hayley" uniqKey="Lavender H" first="Hayley" last="Lavender">Hayley Lavender</name>
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<author><name sortKey="Gnirss, Kerstin" sort="Gnirss, Kerstin" uniqKey="Gnirss K" first="Kerstin" last="Gnirss">Kerstin Gnirss</name>
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<ET>Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease</ET>
<AU>BERTRAM (Stephanie); GLOWACKA (Ilona); MÜLLER (Marcel A.); LAVENDER (Hayley); GNIRSS (Kerstin); NEHLMEIER (Inga); NIEMEYER (Daniela); YUXIAN HE; SIMMONS (Graham); DROSTEN (Christian); SOILLEUX (Elizabeth J.); JAHN (Olaf); STEFFEN (Imke); PÖHLMANN (Stefan)</AU>
<AF>Institute of Virology, Hannover Medical School/Hannover/Allemagne (1 aut., 2 aut., 5 aut., 13 aut., 14 aut.); German Primate Center/Göttingen/Allemagne (1 aut., 6 aut., 14 aut.); Institute of Virology, University of Bonn Medical Centre/Bonn/Allemagne (3 aut., 7 aut., 10 aut.); Oxfabs, Nuffield Department of Clinical Laboratory Sciences, John Radcliffe Hospital, University of Oxford/Oxford/Royaume-Uni (4 aut.); Institute of Pathogen Biology, Chinese Academy of Medical Sciences, and Peking Union Medical College/Beijing/Chine (8 aut.); Blood Systems Research Institute and Department of Laboratory Medicine, University of California/San Francisco, California/Etats-Unis (9 aut., 13 aut.); Department of Cellular Pathology, John Radcliffe Hospital/Oxford/Royaume-Uni (11 aut.); Nuffield Department of Clinical Laboratory Sciences, John Radcliffe Hospital, University of Oxford/Royaume-Uni (11 aut.); Proteomics Group, Max Planck Institute of Experimental Medicine/Göttingen/Allemagne (12 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2011; Vol. 85; No. 24; Pp. 13363-13372; Bibl. 49 ref.</SO>
<LA>Anglais</LA>
<EA>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.</EA>
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Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease

Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease

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