MersV1, Ncbi, Merge, bibRecord, 000C84

Influence of hydrophobic and electrostatic residues on SARS-coronavirus S2 protein stability: insights into mechanisms of general viral fusion and inhibitor design.

Identifieur interne : 000C84 ( Ncbi/Merge ); précédent : 000C83; suivant : 000C85

Influence of hydrophobic and electrostatic residues on SARS-coronavirus S2 protein stability: insights into mechanisms of general viral fusion and inhibitor design.

Auteurs : Halil Aydin [Canada] ; Dina Al-Khooly ; Jeffrey E. Lee

Source :

Protein science : a publication of the Protein Society [ 1469-896X ] ; 2014.

RBID : pubmed:24519901

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Crystallography, X-Ray, Humans, Hydrophobic and Hydrophilic Interactions, Membrane Fusion, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Stability, Protein Structure, Tertiary, SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (physiology), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (genetics), Static Electricity, Virus Internalization.
MESH :
- chemical , chemistry : Spike Glycoprotein, Coronavirus.
- chemistry : SARS Virus.
- genetics : SARS Virus, Spike Glycoprotein, Coronavirus.
- physiology : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Crystallography, X-Ray, Humans, Hydrophobic and Hydrophilic Interactions, Membrane Fusion, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Stability, Protein Structure, Tertiary, Static Electricity, Virus Internalization.

Abstract

Severe acute respiratory syndrome (SARS) is an acute respiratory disease caused by the SARS-coronavirus (SARS-CoV). SARS-CoV entry is facilitated by the spike protein (S), which consists of an N-terminal domain (S1) responsible for cellular attachment and a C-terminal domain (S2) that mediates viral and host cell membrane fusion. The SARS-CoV S2 is a potential drug target, as peptidomimetics against S2 act as potent fusion inhibitors. In this study, site-directed mutagenesis and thermal stability experiments on electrostatic, hydrophobic, and polar residues to dissect their roles in stabilizing the S2 postfusion conformation was performed. It was shown that unlike the pH-independent retroviral fusion proteins, SARS-CoV S2 is stable over a wide pH range, supporting its ability to fuse at both the plasma membrane and endosome. A comprehensive SARS-CoV S2 analysis showed that specific hydrophobic positions at the C-terminal end of the HR2, rather than electrostatics are critical for fusion protein stabilization. Disruption of the conserved C-terminal hydrophobic residues destabilized the fusion core and reduced the melting temperature by 30°C. The importance of the C-terminal hydrophobic residues led us to identify a 42-residue substructure on the central core that is structurally conserved in all existing CoV S2 fusion proteins (root mean squared deviation=0.4 Å). This is the first study to identify such a conserved substructure and likely represents a common foundation to facilitate viral fusion. We have discussed the role of key residues in the design of fusion inhibitors and the potential of the substructure as a general target for the development of novel therapeutics against CoV infections.

DOI: 10.1002/pro.2442
PubMed: 24519901

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Le document en format XML

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<term>Séquence d'acides aminés</term>
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<term>Virus du SRAS (génétique)</term>
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<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Protein Stability</term>
<term>Protein Structure, Tertiary</term>
<term>Static Electricity</term>
<term>Virus Internalization</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is an acute respiratory disease caused by the SARS-coronavirus (SARS-CoV). SARS-CoV entry is facilitated by the spike protein (S), which consists of an N-terminal domain (S1) responsible for cellular attachment and a C-terminal domain (S2) that mediates viral and host cell membrane fusion. The SARS-CoV S2 is a potential drug target, as peptidomimetics against S2 act as potent fusion inhibitors. In this study, site-directed mutagenesis and thermal stability experiments on electrostatic, hydrophobic, and polar residues to dissect their roles in stabilizing the S2 postfusion conformation was performed. It was shown that unlike the pH-independent retroviral fusion proteins, SARS-CoV S2 is stable over a wide pH range, supporting its ability to fuse at both the plasma membrane and endosome. A comprehensive SARS-CoV S2 analysis showed that specific hydrophobic positions at the C-terminal end of the HR2, rather than electrostatics are critical for fusion protein stabilization. Disruption of the conserved C-terminal hydrophobic residues destabilized the fusion core and reduced the melting temperature by 30°C. The importance of the C-terminal hydrophobic residues led us to identify a 42-residue substructure on the central core that is structurally conserved in all existing CoV S2 fusion proteins (root mean squared deviation=0.4 Å). This is the first study to identify such a conserved substructure and likely represents a common foundation to facilitate viral fusion. We have discussed the role of key residues in the design of fusion inhibitors and the potential of the substructure as a general target for the development of novel therapeutics against CoV infections.</div>
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<Abstract><AbstractText>Severe acute respiratory syndrome (SARS) is an acute respiratory disease caused by the SARS-coronavirus (SARS-CoV). SARS-CoV entry is facilitated by the spike protein (S), which consists of an N-terminal domain (S1) responsible for cellular attachment and a C-terminal domain (S2) that mediates viral and host cell membrane fusion. The SARS-CoV S2 is a potential drug target, as peptidomimetics against S2 act as potent fusion inhibitors. In this study, site-directed mutagenesis and thermal stability experiments on electrostatic, hydrophobic, and polar residues to dissect their roles in stabilizing the S2 postfusion conformation was performed. It was shown that unlike the pH-independent retroviral fusion proteins, SARS-CoV S2 is stable over a wide pH range, supporting its ability to fuse at both the plasma membrane and endosome. A comprehensive SARS-CoV S2 analysis showed that specific hydrophobic positions at the C-terminal end of the HR2, rather than electrostatics are critical for fusion protein stabilization. Disruption of the conserved C-terminal hydrophobic residues destabilized the fusion core and reduced the melting temperature by 30°C. The importance of the C-terminal hydrophobic residues led us to identify a 42-residue substructure on the central core that is structurally conserved in all existing CoV S2 fusion proteins (root mean squared deviation=0.4 Å). This is the first study to identify such a conserved substructure and likely represents a common foundation to facilitate viral fusion. We have discussed the role of key residues in the design of fusion inhibitors and the potential of the substructure as a general target for the development of novel therapeutics against CoV infections.</AbstractText>
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<ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2004 Jul 2;319(3):746-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15184046</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8709-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15161975</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W668-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15215473</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Aug;78(16):8701-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15280478</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Microbiol. 2004 Oct;12(10):466-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15381196</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1990 Apr;71 ( Pt 4):767-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2157795</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1991 Jul 1;88(13):5533-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1648219</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1992 Jun 4;357(6377):420-2</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1350662</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1993 Sep 9;365(6442):113</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8371754</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9770-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7937889</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Biol. 1996 May;3(5):465-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8612078</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1997 Jun 23;233(1):1-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9201212</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Med. 1998 Nov;4(11):1302-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9809555</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 1998 Nov;2(5):605-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9844633</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4319-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10200260</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2004 Nov 9;43(44):14064-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15518555</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Nov 19;279(47):49414-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15345712</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):17958-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15604146</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2005 Apr 29;330(1):39-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15781229</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2005 May 10;335(2):276-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15840526</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2005 May 31;102(22):7988-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15897467</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>Curr Opin Struct Biol. 2005 Dec;15(6):664-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16263266</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Struct Biol. 2006 Aug;155(2):162-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16765058</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2006 Dec 26;45(51):15205-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17176042</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>J Virol. 2008 Jan;82(1):588-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17942557</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>PLoS Negl Trop Dis. 2011 Nov;5(11):e1395</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22102923</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2012 Jan;86(1):364-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22031933</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2011 Dec 13;108(50):19967-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22123988</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Virol. 2011 Jul;1(1):27-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22440564</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1994 Sep 1;371(6492):37-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8072525</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS One. 2012;7(3):e33734</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22479434</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Virol. 2011 Dec;1(6):624-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22180768</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Viruses. 2012 Apr;4(4):557-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22590686</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>N Engl J Med. 2012 Nov 8;367(19):1814-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23075143</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2013 Mar 14;495(7440):251-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23486063</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Res. 2013 Aug;23(8):986-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23835475</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2013 Aug 8;500(7461):227-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23831647</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2013 Sep;87(17):9939-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23824801</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2013 Dec;87(24):13134-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24067982</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2013 Nov 28;503(7477):535-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24172901</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FASEB J. 2013 Dec;27(12):5059-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24036886</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2014 Jan;88(1):143-53</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24131724</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Commun. 2014;5:3067</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24473083</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>J Cell Biochem. 2008 Aug 15;104(6):2335-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18442051</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Sep;82(17):8887-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18562523</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antiviral Res. 2009 Jan;81(1):82-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18983873</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Microbiol. 2009 Mar;7(3):226-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19198616</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Emerg Infect Dis. 2009 Mar;15(3):482-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19239771</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Bioinformatics. 2009 Mar 1;25(5):621-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19176554</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>Nat Rev Microbiol. 2009 Jun;7(6):439-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19430490</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2009 Nov;83(21):11133-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19706706</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2011 Jul;39(Web Server issue):W24-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21602266</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Protein Sci. 2011 Sep;20(9):1587-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21739501</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 Jul;74(14):6614-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10864675</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2000 Nov 10;103(4):679-89</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11106737</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):1953-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12690092</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12730500</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 Mol Recognit. 2004 Jan-Feb;17(1):1-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14872533</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>Lancet. 2004 Mar 20;363(9413):938-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15043961</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(11):6048-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15141003</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2004 Jun 18;319(1):283-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15158473</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>
</ReferenceList>
</PubmedData>
</pubmed>
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Influence of hydrophobic and electrostatic residues on SARS-coronavirus S2 protein stability: insights into mechanisms of general viral fusion and inhibitor design.

Influence of hydrophobic and electrostatic residues on SARS-coronavirus S2 protein stability: insights into mechanisms of general viral fusion and inhibitor design.

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