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 : 001B19 ( PubMed/Curation ); précédent : 001B18; suivant : 001B20Cathepsin 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
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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></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18562523</PMID><DateCompleted><Year>2008</Year><Month>09</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>82</Volume><Issue>17</Issue><PubDate><Year>2008</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. 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IdType="pubmed">16731916</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Jul;80(14):6794-800</Citation><ArticleIdList><ArticleId IdType="pubmed">16809285</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2006 Jul 5;350(2):358-69</Citation><ArticleIdList><ArticleId IdType="pubmed">16519916</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17903-8</Citation><ArticleIdList><ArticleId IdType="pubmed">17093041</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2007;2(10):e1082</Citation><ArticleIdList><ArticleId IdType="pubmed">17957264</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2000 Mar 7;1477(1-2):98-111</Citation><ArticleIdList><ArticleId IdType="pubmed">10708852</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2000 May 25;271(1):122-31</Citation><ArticleIdList><ArticleId IdType="pubmed">10814577</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Immunol. 2003 Jun;3(6):472-82</Citation><ArticleIdList><ArticleId IdType="pubmed">12776207</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2003 Aug;77(16):8801-11</Citation><ArticleIdList><ArticleId IdType="pubmed">12885899</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4240-5</Citation><ArticleIdList><ArticleId IdType="pubmed">15010527</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2004 Jun;78(11):6048-54</Citation><ArticleIdList><ArticleId IdType="pubmed">15141003</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60</Citation><ArticleIdList><ArticleId IdType="pubmed">15150417</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 2004 Sep 3;321(4):994-1000</Citation><ArticleIdList><ArticleId IdType="pubmed">15358126</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Virol. 1988 Nov;69 ( Pt 11):2785-95</Citation><ArticleIdList><ArticleId IdType="pubmed">3183628</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Virol. 1990 Dec;71 ( Pt 12):3075-80</Citation><ArticleIdList><ArticleId IdType="pubmed">2177097</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Feb 10;281(6):3198-203</Citation><ArticleIdList><ArticleId IdType="pubmed">16339146</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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