Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.
Identifieur interne : 003152 ( Main/Exploration ); précédent : 003151; suivant : 003153Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.
Auteurs : Berend Jan Bosch [Pays-Bas] ; Willem Bartelink ; Peter J M. RottierSource :
- Journal of virology [ 1098-5514 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux, Cathepsine L, Cathepsines (métabolisme), Cathepsines (pharmacologie), Cellules Vero, Concentration en ions d'hydrogène, Cysteine endopeptidases (métabolisme), Cysteine endopeptidases (pharmacologie), Facteurs temps, Peptides (métabolisme), Plasmides, Protéines de fusion virale (), Protéines de fusion virale (métabolisme), Protéines à fluorescence verte (métabolisme), Température, Transfection, Trypsine (pharmacologie), Virus du SRAS (métabolisme).
- MESH :
- métabolisme : Cathepsines, Cysteine endopeptidases, Peptides, Protéines de fusion virale, Protéines à fluorescence verte, Virus du SRAS.
- pharmacologie : Cathepsines, Cysteine endopeptidases, Trypsine.
- Animaux, Cathepsine L, Cellules Vero, Concentration en ions d'hydrogène, Facteurs temps, Plasmides, Protéines de fusion virale, Température, Transfection.
English descriptors
- KwdEn :
- Animals, Cathepsin L, Cathepsins (metabolism), Cathepsins (pharmacology), Chlorocebus aethiops, Cysteine Endopeptidases (metabolism), Cysteine Endopeptidases (pharmacology), Green Fluorescent Proteins (metabolism), Hydrogen-Ion Concentration, Peptides (metabolism), Plasmids, SARS Virus (metabolism), Temperature, Time Factors, Transfection, Trypsin (pharmacology), Vero Cells, Viral Fusion Proteins (classification), Viral Fusion Proteins (metabolism).
- MESH :
- chemical , classification : Viral Fusion Proteins.
- chemical , metabolism : Cathepsins, Cysteine Endopeptidases, Green Fluorescent Proteins, Peptides, Viral Fusion Proteins.
- chemical , pharmacology : Cathepsins, Cysteine Endopeptidases, Trypsin.
- chemical : Cathepsin L.
- metabolism : SARS Virus.
- Animals, Chlorocebus aethiops, Hydrogen-Ion Concentration, Plasmids, Temperature, Time Factors, Transfection, Vero Cells.
Abstract
Unlike other class I viral fusion proteins, spike proteins on severe acute respiratory syndrome coronavirus virions are uncleaved. As we and others have demonstrated, infection by this virus depends on cathepsin proteases present in endosomal compartments of the target cell, suggesting that the spike protein acquires its fusion competence by cleavage during cell entry rather than during virion biogenesis. Here we demonstrate that cathepsin L indeed activates the membrane fusion function of the spike protein. Moreover, cleavage was mapped to the same region where, in coronaviruses carrying furin-activated spikes, the receptor binding subunit of the protein is separated from the membrane-anchored fusion subunit.
DOI: 10.1128/JVI.00415-08
PubMed: 18562523
Affiliations:
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Le document en format XML
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<term>Cysteine Endopeptidases (pharmacology)</term>
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<front><div type="abstract" xml:lang="en">Unlike other class I viral fusion proteins, spike proteins on severe acute respiratory syndrome coronavirus virions are uncleaved. As we and others have demonstrated, infection by this virus depends on cathepsin proteases present in endosomal compartments of the target cell, suggesting that the spike protein acquires its fusion competence by cleavage during cell entry rather than during virion biogenesis. Here we demonstrate that cathepsin L indeed activates the membrane fusion function of the spike protein. Moreover, cleavage was mapped to the same region where, in coronaviruses carrying furin-activated spikes, the receptor binding subunit of the protein is separated from the membrane-anchored fusion subunit.</div>
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