Proteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research.
Identifieur interne : 001880 ( Main/Exploration ); précédent : 001879; suivant : 001881Proteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research.
Auteurs : Graham Simmons [États-Unis] ; Pawel Zmora ; Stefanie Gierer ; Adeline Heurich ; Stefan PöhlmannSource :
- Antiviral research [ 1872-9096 ] ; 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.
- Humains, Maladies transmissibles émergentes, Modèles biologiques, Protéolyse, Pénétration virale, Réplication virale.
English descriptors
- KwdEn :
- Cathepsins (metabolism), Communicable Diseases, Emerging, Coronavirus Infections (virology), Endosomes (metabolism), Humans, Lung (enzymology), Lung (pathology), Lung (virology), Membrane Proteins (metabolism), Models, Biological, Peptidyl-Dipeptidase A (metabolism), Proteolysis, SARS Virus (physiology), Serine Endopeptidases (metabolism), Serine Proteases (metabolism), Severe Acute Respiratory Syndrome (pathology), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus (metabolism), 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: 10years of research on highly pathogenic human coronaviruses.''
DOI: 10.1016/j.antiviral.2013.09.028
PubMed: 24121034
Affiliations:
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Le document en format XML
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<term>Endosomes (metabolism)</term>
<term>Humans</term>
<term>Lung (enzymology)</term>
<term>Lung (pathology)</term>
<term>Lung (virology)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Models, Biological</term>
<term>Peptidyl-Dipeptidase A (metabolism)</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>Spike Glycoprotein, Coronavirus (metabolism)</term>
<term>Virus Internalization</term>
<term>Virus Replication</term>
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<term>Syndrome respiratoire aigu sévère (virologie)</term>
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<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: 10years of research on highly pathogenic human coronaviruses.'' </div>
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