SrasV1, Main, Exploration, bibRecord, 003752

Cleavage of spike protein of SARS coronavirus by protease factor Xa is associated with viral infectivity.

Identifieur interne : 003752 ( Main/Exploration ); précédent : 003751; suivant : 003753

Cleavage of spike protein of SARS coronavirus by protease factor Xa is associated with viral infectivity.

Auteurs : Lanying Du [République populaire de Chine] ; Richard Y. Kao ; Yusen Zhou ; Yuxian He ; Guangyu Zhao ; Charlotte Wong ; Shibo Jiang ; Kwok-Yung Yuen ; Dong-Yan Jin ; Bo-Jian Zheng

Source :

Biochemical and biophysical research communications [ 0006-291X ] ; 2007.

RBID : pubmed:17533109

Descripteurs français

KwdFr :
- Activation virale (physiologie), Facteur Xa (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Liaison aux protéines, Lignée cellulaire, Protéines de l'enveloppe virale (métabolisme), Rein (virologie), Réplication virale (physiologie).
MESH :
- métabolisme : Facteur Xa, Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- physiologie : Activation virale, Réplication virale.
- virologie : Rein.
- Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Lignée cellulaire.

English descriptors

KwdEn :
- Cell Line, Factor Xa (metabolism), Humans, Kidney (virology), Membrane Glycoproteins (metabolism), Protein Binding, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism), Virus Activation (physiology), Virus Replication (physiology).
MESH :
- chemical , metabolism : Factor Xa, Membrane Glycoproteins, Viral Envelope Proteins.
- physiology : Virus Activation, Virus Replication.
- virology : Kidney.
- Cell Line, Humans, Protein Binding, Spike Glycoprotein, Coronavirus.

Abstract

The spike (S) protein of SARS coronavirus (SARS-CoV) has been known to recognize and bind to host receptors, whose conformational changes then facilitate fusion between the viral envelope and host cell membrane, leading to viral entry into target cells. However, other functions of SARS-CoV S protein such as proteolytic cleavage and its implications to viral infection are incompletely understood. In this study, we demonstrated that the infection of SARS-CoV and a pseudovirus bearing the S protein of SARS-CoV was inhibited by a protease inhibitor Ben-HCl. Also, the protease Factor Xa, a target of Ben-HCl abundantly expressed in infected cells, was able to cleave the recombinant and pseudoviral S protein into S1 and S2 subunits, and the cleavage was inhibited by Ben-HCl. Furthermore, this cleavage correlated with the infectivity of the pseudovirus. Taken together, our study suggests a plausible mechanism by which SARS-CoV cleaves its S protein to facilitate viral infection.

DOI: 10.1016/j.bbrc.2007.05.092
PubMed: 17533109

Affiliations:

République populaire de Chine

Le document en format XML

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<affiliation wicri:level="1"><nlm:affiliation>Department of Microbiology, The University of Hong Kong, Hong Kong, China.</nlm:affiliation>
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<author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name>
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<term>Membrane Glycoproteins (metabolism)</term>
<term>Protein Binding</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Virus Activation (physiology)</term>
<term>Virus Replication (physiology)</term>
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<term>Glycoprotéines membranaires (métabolisme)</term>
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<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
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<term>Rein (virologie)</term>
<term>Réplication virale (physiologie)</term>
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<front><div type="abstract" xml:lang="en">The spike (S) protein of SARS coronavirus (SARS-CoV) has been known to recognize and bind to host receptors, whose conformational changes then facilitate fusion between the viral envelope and host cell membrane, leading to viral entry into target cells. However, other functions of SARS-CoV S protein such as proteolytic cleavage and its implications to viral infection are incompletely understood. In this study, we demonstrated that the infection of SARS-CoV and a pseudovirus bearing the S protein of SARS-CoV was inhibited by a protease inhibitor Ben-HCl. Also, the protease Factor Xa, a target of Ben-HCl abundantly expressed in infected cells, was able to cleave the recombinant and pseudoviral S protein into S1 and S2 subunits, and the cleavage was inhibited by Ben-HCl. Furthermore, this cleavage correlated with the infectivity of the pseudovirus. Taken together, our study suggests a plausible mechanism by which SARS-CoV cleaves its S protein to facilitate viral infection.</div>
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<name sortKey="Jin, Dong Yan" sort="Jin, Dong Yan" uniqKey="Jin D" first="Dong-Yan" last="Jin">Dong-Yan Jin</name>
<name sortKey="Kao, Richard Y" sort="Kao, Richard Y" uniqKey="Kao R" first="Richard Y" last="Kao">Richard Y. Kao</name>
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Cleavage of spike protein of SARS coronavirus by protease factor Xa is associated with viral infectivity.

Cleavage of spike protein of SARS coronavirus by protease factor Xa is associated with viral infectivity.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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