SrasV1, PubMed, Checkpoint, bibRecord, 001793

SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.

Identifieur interne : 001793 ( PubMed/Checkpoint ); précédent : 001792; suivant : 001794

SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.

Auteurs : Ikenna G. Madu [États-Unis] ; Sandrine Belouzard ; Gary R. Whittaker

Source :

Virology [ 1096-0341 ] ; 2009.

RBID : pubmed:19717178

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Cell Fusion, Cell Line, Chlorocebus aethiops, Conserved Sequence, Cricetinae, Cysteine (genetics), Humans, Membrane Fusion, Membrane Glycoproteins (genetics), Molecular Sequence Data, Mutagenesis, Site-Directed, SARS Virus (genetics), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics).
MESH :
- chemical , genetics : Cysteine, Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : SARS Virus.
- physiology : SARS Virus.
- Amino Acid Sequence, Animals, Cell Fusion, Cell Line, Chlorocebus aethiops, Conserved Sequence, Cricetinae, Humans, Membrane Fusion, Molecular Sequence Data, Mutagenesis, Site-Directed, Spike Glycoprotein, Coronavirus.

Abstract

The S2 domain of the coronavirus spike (S) protein is known to be responsible for mediating membrane fusion. In addition to a well-recognized cleavage site at the S1-S2 boundary, a second proteolytic cleavage site has been identified in the severe acute respiratory syndrome coronavirus (SARS-CoV) S2 domain (R797). C-terminal to this S2 cleavage site is a conserved region flanked by cysteine residues C822 and C833. Here, we investigated the importance of this well conserved region for SARS-CoV S-mediated fusion activation. We show that the residues between C822-C833 are well conserved across all coronaviruses. Mutagenic analysis of SARS-CoV S, combined with cell-cell fusion and pseudotyped virion infectivity assays, showed a critical role for the core-conserved residues C822, D830, L831, and C833. Based on available predictive models, we propose that the conserved domain flanked by cysteines 822 and 833 forms a loop structure that interacts with components of the SARS-CoV S trimer to control the activation of membrane fusion.

DOI: 10.1016/j.virol.2009.07.038
PubMed: 19717178

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The S2 domain of the coronavirus spike (S) protein is known to be responsible for mediating membrane fusion. In addition to a well-recognized cleavage site at the S1-S2 boundary, a second proteolytic cleavage site has been identified in the severe acute respiratory syndrome coronavirus (SARS-CoV) S2 domain (R797). C-terminal to this S2 cleavage site is a conserved region flanked by cysteine residues C822 and C833. Here, we investigated the importance of this well conserved region for SARS-CoV S-mediated fusion activation. We show that the residues between C822-C833 are well conserved across all coronaviruses. Mutagenic analysis of SARS-CoV S, combined with cell-cell fusion and pseudotyped virion infectivity assays, showed a critical role for the core-conserved residues C822, D830, L831, and C833. Based on available predictive models, we propose that the conserved domain flanked by cysteines 822 and 833 forms a loop structure that interacts with components of the SARS-CoV S trimer to control the activation of membrane fusion.</div>
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<ReferenceList><Reference><Citation>J Virol. 2000 Oct;74(20):9738-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11000247</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2009 Aug;83(15):7411-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19439480</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2001 Oct;75(20):9741-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11559807</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2002 May 31;277(22):19727-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11912215</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Immunol. 2002 Aug;3(8):727-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12089508</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>Antioxid Redox Signal. 2003 Feb;5(1):133-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12626125</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>N Engl J Med. 2003 May 15;348(20):1967-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12690091</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>N Engl J Med. 2003 May 15;348(20):1948-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12748314</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2003 May 15;423(6937):240</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12748632</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2003 Oct 10;310(1):78-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14511651</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>J Virol. 2004 Jan;78(2):683-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14694099</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Mar;78(6):2682-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14990688</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>J Virol. 2004 Jul;78(13):6938-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15194770</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Sep;78(18):9904-17</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15331724</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Oct;78(19):10328-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15367599</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1996 Aug;70(8):5634-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8764078</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1997 Feb;71(2):1688-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8995701</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1998 Jun 18;393(6686):648-59</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9641677</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 1998;440:43-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9782263</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 1998;440:89-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9782269</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2004 Dec 24;325(4):1210-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15555555</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>
<Reference><Citation>Mol Membr Biol. 2004 Nov-Dec;21(6):361-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15764366</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2005 Oct 25;341(2):215-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16099010</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Feb;80(3):1280-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16415005</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>Virology. 2006 Jul 5;350(2):358-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16519916</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Sep;80(17):8639-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16912312</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2007 Apr 10;360(2):264-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17134730</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>Virology. 2007 Oct 25;367(2):367-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17631932</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. 2008 Mar;82(6):3131-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18184714</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 Virol. 2009 Jan;83(2):712-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18971274</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2009 Mar;83(6):2584-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19109378</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2009 Apr 7;106(14):5871-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19321428</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Avian Dis. 2001 Apr-Jun;45(2):366-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11417816</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
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   |texte=   SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.
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SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.

SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.

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