Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.
Identifieur interne : 001937 ( PubMed/Corpus ); précédent : 001936; suivant : 001938Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.
Auteurs : Sandrine Belouzard ; Victor C. Chu ; Gary R. WhittakerSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2009.
English descriptors
- KwdEn :
- Binding Sites, Cell Fusion, Furin, Hydrolysis, Membrane Glycoproteins (metabolism), Membrane Glycoproteins (physiology), Mutagenesis, Site-Directed, SARS Virus (pathogenicity), Spike Glycoprotein, Coronavirus, Trypsin (metabolism), Viral Envelope Proteins (metabolism), Viral Envelope Proteins (physiology), Virus Internalization.
- MESH :
- chemical , metabolism : Membrane Glycoproteins, Trypsin, Viral Envelope Proteins.
- chemical , physiology : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical : Furin, Spike Glycoprotein, Coronavirus.
- pathogenicity : SARS Virus.
- Binding Sites, Cell Fusion, Hydrolysis, Mutagenesis, Site-Directed, Virus Internalization.
Abstract
The coronavirus spike protein (S) plays a key role in the early steps of viral infection, with the S1 domain responsible for receptor binding and the S2 domain mediating membrane fusion. In some cases, the S protein is proteolytically cleaved at the S1-S2 boundary. In the case of the severe acute respiratory syndrome coronavirus (SARS-CoV), it has been shown that virus entry requires the endosomal protease cathepsin L; however, it was also found that infection of SARS-CoV could be strongly induced by trypsin treatment. Overall, in terms of how cleavage might activate membrane fusion, proteolytic processing of the SARS-CoV S protein remains unclear. Here, we identify a proteolytic cleavage site within the SARS-CoV S2 domain (S2', R797). Mutation of R797 specifically inhibited trypsin-dependent fusion in both cell-cell fusion and pseudovirion entry assays. We also introduced a furin cleavage site at both the S2' cleavage site within S2 793-KPTKR-797 (S2'), as well as at the junction of S1 and S2. Introduction of a furin cleavage site at the S2' position allowed trypsin-independent cell-cell fusion, which was strongly increased by the presence of a second furin cleavage site at the S1-S2 position. Taken together, these data suggest a novel priming mechanism for a viral fusion protein, with a critical proteolytic cleavage event on the SARS-CoV S protein at position 797 (S2'), acting in concert with the S1-S2 cleavage site to mediate membrane fusion and virus infectivity.
DOI: 10.1073/pnas.0809524106
PubMed: 19321428
Links to Exploration step
pubmed:19321428Le document en format XML
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<front><div type="abstract" xml:lang="en">The coronavirus spike protein (S) plays a key role in the early steps of viral infection, with the S1 domain responsible for receptor binding and the S2 domain mediating membrane fusion. In some cases, the S protein is proteolytically cleaved at the S1-S2 boundary. In the case of the severe acute respiratory syndrome coronavirus (SARS-CoV), it has been shown that virus entry requires the endosomal protease cathepsin L; however, it was also found that infection of SARS-CoV could be strongly induced by trypsin treatment. Overall, in terms of how cleavage might activate membrane fusion, proteolytic processing of the SARS-CoV S protein remains unclear. Here, we identify a proteolytic cleavage site within the SARS-CoV S2 domain (S2', R797). Mutation of R797 specifically inhibited trypsin-dependent fusion in both cell-cell fusion and pseudovirion entry assays. We also introduced a furin cleavage site at both the S2' cleavage site within S2 793-KPTKR-797 (S2'), as well as at the junction of S1 and S2. Introduction of a furin cleavage site at the S2' position allowed trypsin-independent cell-cell fusion, which was strongly increased by the presence of a second furin cleavage site at the S1-S2 position. Taken together, these data suggest a novel priming mechanism for a viral fusion protein, with a critical proteolytic cleavage event on the SARS-CoV S protein at position 797 (S2'), acting in concert with the S1-S2 cleavage site to mediate membrane fusion and virus infectivity.</div>
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<Abstract><AbstractText>The coronavirus spike protein (S) plays a key role in the early steps of viral infection, with the S1 domain responsible for receptor binding and the S2 domain mediating membrane fusion. In some cases, the S protein is proteolytically cleaved at the S1-S2 boundary. In the case of the severe acute respiratory syndrome coronavirus (SARS-CoV), it has been shown that virus entry requires the endosomal protease cathepsin L; however, it was also found that infection of SARS-CoV could be strongly induced by trypsin treatment. Overall, in terms of how cleavage might activate membrane fusion, proteolytic processing of the SARS-CoV S protein remains unclear. Here, we identify a proteolytic cleavage site within the SARS-CoV S2 domain (S2', R797). Mutation of R797 specifically inhibited trypsin-dependent fusion in both cell-cell fusion and pseudovirion entry assays. We also introduced a furin cleavage site at both the S2' cleavage site within S2 793-KPTKR-797 (S2'), as well as at the junction of S1 and S2. Introduction of a furin cleavage site at the S2' position allowed trypsin-independent cell-cell fusion, which was strongly increased by the presence of a second furin cleavage site at the S1-S2 position. Taken together, these data suggest a novel priming mechanism for a viral fusion protein, with a critical proteolytic cleavage event on the SARS-CoV S protein at position 797 (S2'), acting in concert with the S1-S2 cleavage site to mediate membrane fusion and virus infectivity.</AbstractText>
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<ReferenceList><Reference><Citation>Mol Cells. 1999 Jun 30;9(3):235-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10420980</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Aug 24;276(34):31642-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11418598</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2005 Jun 10;308(5728):1643-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15831716</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11876-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16081529</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2005 Aug 30;102(35):12543-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16116101</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Nov;79(22):14451-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16254381</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Feb 10;281(6):3198-203</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16339146</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Apr;80(7):3180-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16537586</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Apr;80(8):4174-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16571833</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 2006 Jun;87(Pt 6):1659-67</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16690931</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>Adv Exp Med Biol. 2006;581:235-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17037535</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Vet Res. 2007 Mar-Apr;38(2):281-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17296157</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2007 Jul 20;359(1):174-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17533109</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Struct Biol. 2007 Aug;17(4):427-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17870467</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Exp Med. 2003 Mar 3;197(5):633-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12615904</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Mol Cell Biol. 2003 Apr;4(4):309-19</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12671653</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 Nov 21;278(47):46854-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12952986</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2003 Dec 26;312(4):1159-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14651994</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2003 Nov 27;426(6965):450-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14647384</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):5642-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15140961</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Jun;78(12):6134-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15163706</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Infect Dis. 2004 Jul 1;190(1):91-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15195247</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2007 Nov;81(21):12029-39</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17715238</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Oct;78(19):10328-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15367599</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virus Res. 1986 Feb;4(2):133-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3010595</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Avian Dis. 1992 Oct-Dec;36(4):903-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1336663</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Ann N Y Acad Sci. 1993 May 31;680:135-46</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8512214</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Microbiol. 1994 Feb;2(2):39-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8162439</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2007 Dec;81(24):13378-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17928356</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Jan;82(1):588-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17942557</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2007 Dec 22;581(30):5807-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18037384</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Int J Biochem Cell Biol. 2008;40(6-7):1111-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18343183</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Jun;82(12):5986-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18385247</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Jun;82(12):6078-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18400867</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Crit Rev Biochem Mol Biol. 2008 May-Jun;43(3):189-219</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18568847</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Mol Biol. 2008 Jul;15(7):690-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18596815</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2008 Jul 10;454(7201):177-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18615077</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Sep;82(17):8887-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18562523</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Dec;82(23):11985-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18786990</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 2000 Dec;81(Pt 12):2867-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11086117</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9859-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11493675</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2005 Jan 21;326(3):554-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15596135</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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