[Protease-dependent cell entry mechanism of coronaviruses].
Identifieur interne : 002003 ( Main/Exploration ); précédent : 002002; suivant : 002004[Protease-dependent cell entry mechanism of coronaviruses].
Auteurs : Shutoku Matsuyama [Japon]Source :
- Uirusu [ 0042-6857 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux, Cathepsines (physiologie), Coronavirus (pathogénicité), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Pancreatic elastase (physiologie), Peptide hydrolases (physiologie), Protéines de l'enveloppe virale (métabolisme), Pénétration virale, Serine endopeptidases (physiologie), Syndrome respiratoire aigu sévère (virologie), Tropisme viral, Trypsine (physiologie), Virus de l'hépatite murine.
- MESH :
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- pathogénicité : Coronavirus.
- physiologie : Cathepsines, Pancreatic elastase, Peptide hydrolases, Serine endopeptidases, Trypsine.
- virologie : Syndrome respiratoire aigu sévère.
- Animaux, Glycoprotéine de spicule des coronavirus, Humains, Pénétration virale, Tropisme viral, Virus de l'hépatite murine.
English descriptors
- KwdEn :
- Animals, Cathepsins (physiology), Coronavirus (pathogenicity), Humans, Membrane Glycoproteins (metabolism), Murine hepatitis virus, Pancreatic Elastase (physiology), Peptide Hydrolases (physiology), Serine Endopeptidases (physiology), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Trypsin (physiology), Viral Envelope Proteins (metabolism), Viral Tropism, Virus Internalization.
- MESH :
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , physiology : Cathepsins, Pancreatic Elastase, Peptide Hydrolases, Serine Endopeptidases, Trypsin.
- pathogenicity : Coronavirus.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Humans, Murine hepatitis virus, Spike Glycoprotein, Coronavirus, Viral Tropism, Virus Internalization.
Abstract
Previous studies have demonstrated that the SARS-CoV S protein requires proteolytic cleavage by elastase, cathepsin or TMPRSS2 for S-mediated cell-cell or virus-cell membrane fusion. Activation of viral glycoprotein (GP) by protease also has been reported for influenza virus. The most distinctive difference between influenza virus and SARS-CoV is the stage during virus replication in which viral glycoproteins are cleaved by proteases. In influenza virus, the protease makes a simple cut in the GP during maturation. In contrast, SARS-CoV S protein is cleaved by the protease following receptor-induced conformational changes. The protease cleavage site in S protein is thought to be exposed only after receptor binding. In support of this model, we reported that the S protein of mouse hepatitis virus type 2 (MHV-2), which is highly similar to the S protein of SARS-CoV, requires two-step conformational changes mediated by sequential receptor binding and proteolysis to be activated for membrane fusion. Such a mechanism allows for tight temporal control over fusion by protecting the activating cleavage site from premature proteolysis yet allowing efficient cleavage upon binding to the receptor on target cells.
DOI: 10.2222/jsv.61.109
PubMed: 21972562
Affiliations:
Links toward previous steps (curation, corpus...)
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Le document en format XML
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Virology III, National Institute of Infectious Diseases. matuyama@nih.go.jp</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21972562</idno><idno type="pmid">21972562</idno><idno type="doi">10.2222/jsv.61.109</idno><idno type="wicri:Area/PubMed/Corpus">001464</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001464</idno><idno type="wicri:Area/PubMed/Curation">001464</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001464</idno><idno type="wicri:Area/PubMed/Checkpoint">001397</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001397</idno><idno type="wicri:Area/Ncbi/Merge">002395</idno><idno type="wicri:Area/Ncbi/Curation">002395</idno><idno type="wicri:Area/Ncbi/Checkpoint">002395</idno><idno type="wicri:doubleKey">0042-6857:2011:Matsuyama S:protease:dependent:cell</idno><idno type="wicri:Area/Main/Merge">002027</idno><idno type="wicri:Area/Main/Curation">002003</idno><idno type="wicri:Area/Main/Exploration">002003</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">[Protease-dependent cell entry mechanism of coronaviruses].</title><author><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name><affiliation wicri:level="1"><nlm:affiliation>Dept. Virology III, National Institute of Infectious Diseases. matuyama@nih.go.jp</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation></author></analytic><series><title level="j">Uirusu</title><idno type="ISSN">0042-6857</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cathepsins (physiology)</term><term>Coronavirus (pathogenicity)</term><term>Humans</term><term>Membrane Glycoproteins (metabolism)</term><term>Murine hepatitis virus</term><term>Pancreatic Elastase (physiology)</term><term>Peptide Hydrolases (physiology)</term><term>Serine Endopeptidases (physiology)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Trypsin (physiology)</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Tropism</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cathepsines (physiologie)</term><term>Coronavirus (pathogénicité)</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Pancreatic elastase (physiologie)</term><term>Peptide hydrolases (physiologie)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Pénétration virale</term><term>Serine endopeptidases (physiologie)</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Tropisme viral</term><term>Trypsine (physiologie)</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Cathepsins</term><term>Pancreatic Elastase</term><term>Peptide Hydrolases</term><term>Serine Endopeptidases</term><term>Trypsin</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cathepsines</term><term>Pancreatic elastase</term><term>Peptide hydrolases</term><term>Serine endopeptidases</term><term>Trypsine</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Murine hepatitis virus</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Tropism</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Pénétration virale</term><term>Tropisme viral</term><term>Virus de l'hépatite murine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Previous studies have demonstrated that the SARS-CoV S protein requires proteolytic cleavage by elastase, cathepsin or TMPRSS2 for S-mediated cell-cell or virus-cell membrane fusion. Activation of viral glycoprotein (GP) by protease also has been reported for influenza virus. The most distinctive difference between influenza virus and SARS-CoV is the stage during virus replication in which viral glycoproteins are cleaved by proteases. In influenza virus, the protease makes a simple cut in the GP during maturation. In contrast, SARS-CoV S protein is cleaved by the protease following receptor-induced conformational changes. The protease cleavage site in S protein is thought to be exposed only after receptor binding. In support of this model, we reported that the S protein of mouse hepatitis virus type 2 (MHV-2), which is highly similar to the S protein of SARS-CoV, requires two-step conformational changes mediated by sequential receptor binding and proteolysis to be activated for membrane fusion. Such a mechanism allows for tight temporal control over fusion by protecting the activating cleavage site from premature proteolysis yet allowing efficient cleavage upon binding to the receptor on target cells.</div></front></TEI><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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