Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research
Identifieur interne : 002175 ( Main/Exploration ); précédent : 002174; suivant : 002176Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research
Auteurs : Graham Simmons [États-Unis] ; Pawel Zmora [Allemagne] ; Stefanie Gierer [Allemagne] ; Adeline Heurich [Allemagne] ; Stefan Pöhlmann [Allemagne]Source :
- Antiviral research [ 0166-3542 ] ; 2013.
Descripteurs français
- KwdFr :
- Cathepsines (métabolisme), Endosomes (métabolisme), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Infections à coronavirus (virologie), Maladies transmissibles émergentes, Modèles biologiques, Peptidyl-Dipeptidase A (métabolisme), Poumon (anatomopathologie), Poumon (enzymologie), Poumon (virologie), Protéases à sérine (métabolisme), Protéines membranaires (métabolisme), Protéolyse, Pénétration virale, Réplication virale, Serine endopeptidases (métabolisme), Syndrome respiratoire aigu sévère (anatomopathologie), Syndrome respiratoire aigu sévère (virologie), Virus du SRAS (physiologie).
- MESH :
- anatomopathologie : Poumon, Syndrome respiratoire aigu sévère.
- enzymologie : Poumon.
- métabolisme : Cathepsines, Endosomes, Glycoprotéine de spicule des coronavirus, Peptidyl-Dipeptidase A, Protéases à sérine, Protéines membranaires, Serine endopeptidases.
- physiologie : Virus du SRAS.
- virologie : Infections à coronavirus, Poumon, Syndrome respiratoire aigu sévère.
- Pascal (Inist)
- Activation, Humains, Maladies transmissibles émergentes, Modèles biologiques, Protéolyse, Pénétration virale, Réplication virale, Virus syndrome respiratoire aigu sévère, Protéine, Enzyme, Antiviral, Relation structure activité, Syndrome respiratoire aigu sévère, Cathepsin L, Protéine S, Protéolyse, Transmembrane protease serine 2, Syndrome respiratoire du Moyen-Orient.
- Wicri :
- topic : Enzyme.
English descriptors
- KwdEn :
- Activation, Antiviral, Cathepsin L, Cathepsins (metabolism), Communicable Diseases, Emerging, Coronavirus Infections (virology), Endosomes (metabolism), Enzyme, Humans, Lung (enzymology), Lung (pathology), Lung (virology), Membrane Proteins (metabolism), Middle East respiratory syndrome, Models, Biological, Peptidyl-Dipeptidase A (metabolism), Protein, Protein S, Proteolysis, SARS Virus (physiology), Serine Endopeptidases (metabolism), Serine Proteases (metabolism), Severe Acute Respiratory Syndrome (pathology), Severe Acute Respiratory Syndrome (virology), Severe acute respiratory syndrome, Severe acute respiratory syndrome virus, Spike Glycoprotein, Coronavirus (metabolism), Structure activity relation, Virus Internalization, Virus Replication.
- MESH :
- chemical , metabolism : Cathepsins, Membrane Proteins, Peptidyl-Dipeptidase A, Serine Endopeptidases, Serine Proteases, Spike Glycoprotein, Coronavirus.
- enzymology : Lung.
- metabolism : Endosomes.
- pathology : Lung, Severe Acute Respiratory Syndrome.
- physiology : SARS Virus.
- virology : Coronavirus Infections, Lung, Severe Acute Respiratory Syndrome.
- Communicable Diseases, Emerging, Humans, Models, Biological, Proteolysis, Virus Internalization, Virus Replication.
Abstract
The severe acute respiratory syndrome (SARS) pandemic revealed that zoonotic transmission of animal coronaviruses (CoV) to humans poses a significant threat to public health and warrants surveillance and the development of countermeasures. The activity of host cell proteases, which cleave and activate the SARS-CoV spike (S) protein, is essential for viral infectivity and constitutes a target for intervention. However, the identities of the proteases involved have been unclear. Pioneer studies identified cathepsins and type II transmembrane serine proteases as cellular activators of SARS-CoV and demonstrated that several emerging viruses might exploit these enzymes to promote their spread. Here, we will review the proteolytic systems hijacked by SARS-CoV for S protein activation, we will discuss their contribution to viral spread in the host and we will outline antiviral strategies targeting these enzymes. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses."
Url:
Affiliations:
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Le document en format XML
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aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Allemagne</country><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Göttingen</settlement></placeName></affiliation></author><author><name sortKey="Gierer, Stefanie" sort="Gierer, Stefanie" uniqKey="Gierer S" first="Stefanie" last="Gierer">Stefanie Gierer</name><affiliation wicri:level="3"><inist:fA14 i1="02"><s1>Infection Biology Unit, German Primate Center, Kellnerweg 4</s1><s2>37077 Göttingen</s2><s3>DEU</s3><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Allemagne</country><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Göttingen</settlement></placeName></affiliation></author><author><name sortKey="Heurich, Adeline" sort="Heurich, Adeline" uniqKey="Heurich A" first="Adeline" last="Heurich">Adeline Heurich</name><affiliation wicri:level="3"><inist:fA14 i1="02"><s1>Infection Biology Unit, German Primate Center, Kellnerweg 4</s1><s2>37077 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when="2013">2013</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Antiviral research</title><title level="j" type="abbreviated">Antivir. res.</title><idno type="ISSN">0166-3542</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Activation</term><term>Antiviral</term><term>Cathepsin L</term><term>Cathepsins (metabolism)</term><term>Communicable Diseases, Emerging</term><term>Coronavirus Infections (virology)</term><term>Endosomes (metabolism)</term><term>Enzyme</term><term>Humans</term><term>Lung (enzymology)</term><term>Lung (pathology)</term><term>Lung (virology)</term><term>Membrane Proteins (metabolism)</term><term>Middle East respiratory syndrome</term><term>Models, Biological</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Protein</term><term>Protein S</term><term>Proteolysis</term><term>SARS Virus (physiology)</term><term>Serine Endopeptidases (metabolism)</term><term>Serine Proteases (metabolism)</term><term>Severe Acute Respiratory Syndrome (pathology)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Severe acute respiratory syndrome</term><term>Severe acute respiratory syndrome virus</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Structure activity relation</term><term>Virus Internalization</term><term>Virus Replication</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cathepsines (métabolisme)</term><term>Endosomes (métabolisme)</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Humains</term><term>Infections à coronavirus (virologie)</term><term>Maladies transmissibles émergentes</term><term>Modèles biologiques</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Poumon (anatomopathologie)</term><term>Poumon (enzymologie)</term><term>Poumon (virologie)</term><term>Protéases à sérine (métabolisme)</term><term>Protéines membranaires (métabolisme)</term><term>Protéolyse</term><term>Pénétration virale</term><term>Réplication virale</term><term>Serine endopeptidases (métabolisme)</term><term>Syndrome respiratoire aigu sévère (anatomopathologie)</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cathepsins</term><term>Membrane Proteins</term><term>Peptidyl-Dipeptidase A</term><term>Serine Endopeptidases</term><term>Serine Proteases</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Poumon</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Poumon</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Lung</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endosomes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cathepsines</term><term>Endosomes</term><term>Glycoprotéine de spicule des coronavirus</term><term>Peptidyl-Dipeptidase A</term><term>Protéases à sérine</term><term>Protéines membranaires</term><term>Serine endopeptidases</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Lung</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à coronavirus</term><term>Poumon</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term><term>Lung</term><term>Severe Acute Respiratory 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xml:lang="fr"><term>Enzyme</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome (SARS) pandemic revealed that zoonotic transmission of animal coronaviruses (CoV) to humans poses a significant threat to public health and warrants surveillance and the development of countermeasures. The activity of host cell proteases, which cleave and activate the SARS-CoV spike (S) protein, is essential for viral infectivity and constitutes a target for intervention. However, the identities of the proteases involved have been unclear. Pioneer studies identified cathepsins and type II transmembrane serine proteases as cellular activators of SARS-CoV and demonstrated that several emerging viruses might exploit these enzymes to promote their spread. Here, we will review the proteolytic systems hijacked by SARS-CoV for S protein activation, we will discuss their contribution to viral spread in the host and we will outline antiviral strategies targeting these enzymes. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses."</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>États-Unis</li></country><region><li>Basse-Saxe</li><li>Californie</li></region><settlement><li>Göttingen</li></settlement></list><tree><country name="États-Unis"><region name="Californie"><name sortKey="Simmons, Graham" sort="Simmons, Graham" uniqKey="Simmons G" first="Graham" last="Simmons">Graham Simmons</name></region></country><country name="Allemagne"><region name="Basse-Saxe"><name sortKey="Zmora, Pawel" sort="Zmora, Pawel" uniqKey="Zmora P" first="Pawel" last="Zmora">Pawel Zmora</name></region><name sortKey="Gierer, Stefanie" sort="Gierer, Stefanie" uniqKey="Gierer S" first="Stefanie" last="Gierer">Stefanie Gierer</name><name sortKey="Heurich, Adeline" sort="Heurich, Adeline" uniqKey="Heurich A" first="Adeline" last="Heurich">Adeline Heurich</name><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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