The 3D structure analysis of SARS-CoV S1 protein reveals a link to influenza virus neuraminidase and implications for drug and antibody discovery.
Identifieur interne : 002994 ( PubMed/Checkpoint ); précédent : 002993; suivant : 002995The 3D structure analysis of SARS-CoV S1 protein reveals a link to influenza virus neuraminidase and implications for drug and antibody discovery.
Auteurs : Xue Wu Zhang [République populaire de Chine] ; Yee Leng Yap [République populaire de Chine]Source :
- Theochem [ 0166-1280 ] ; 2004.
Abstract
The spike protein of SARS-associated coronavirus (SARS-CoV) is an important target for anti-SARS drug discovery. Its S1 domain is responsible for receptor binding and SARS-CoV entry into cells. In this study, we constructed a rational 3D model for S1 domain of SARS-CoV spike protein by fold recognition and molecular modeling techniques. We found that there is a structure similarity between S1 protein and influenza virus neuraminidase. Our analyses suggest that the existing anti-influenza virus inhibitors and anti-neuraminidase antibody could be used as a starting point for designing anti-SARS drugs, vaccines and antibodies. Interestingly, our prediction for antibody is consistent with a recently experimental discovery of anti-SARS antibody.
DOI: 10.1016/j.theochem.2004.04.065
PubMed: 32287547
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<front><div type="abstract" xml:lang="en">The spike protein of SARS-associated coronavirus (SARS-CoV) is an important target for anti-SARS drug discovery. Its S1 domain is responsible for receptor binding and SARS-CoV entry into cells. In this study, we constructed a rational 3D model for S1 domain of SARS-CoV spike protein by fold recognition and molecular modeling techniques. We found that there is a structure similarity between S1 protein and influenza virus neuraminidase. Our analyses suggest that the existing anti-influenza virus inhibitors and anti-neuraminidase antibody could be used as a starting point for designing anti-SARS drugs, vaccines and antibodies. Interestingly, our prediction for antibody is consistent with a recently experimental discovery of anti-SARS antibody.</div>
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<ReferenceList><Reference><Citation>Bioorg Med Chem. 2004 May 1;12(9):2219-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15080921</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nucleic Acids Res. 2003 Jul 1;31(13):3345-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12824323</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Struct Biol. 2001 Jun;8(6):499-504</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11373616</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Bioinformatics. 2003 May 22;19(8):1015-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12761065</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nature. 2003 Nov 27;426(6965):450-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14647384</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nucleic Acids Res. 2003 Jul 1;31(13):3370-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12824330</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 1995 Feb 3;245(5):623-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7844831</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 2002 Sep 27;322(4):871-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12270720</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 1992 Sep 5;227(1):122-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1381757</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Structure. 1999 Mar 15;7(3):297-307</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10368299</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Acta Pharmacol Sin. 2003 Jun;24(6):497-504</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12791174</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2003 Aug 15;308(1):148-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12890493</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2536-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14983044</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Antimicrob Chemother. 2004 Feb;53(2):133-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14688047</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 1999 Sep 17;292(2):195-202</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10493868</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 1993 Dec 5;234(3):779-815</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8254673</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Protein Sci. 2003 May;12(5):1073-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12717029</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):316-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15299935</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Protein Eng. 1998 Sep;11(9):739-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9796821</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 1999 Nov 12;293(5):1107-19</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10547289</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 1998 Jun 19;279(4):901-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9642070</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Chin Sci Bull. 2003;48(13):1277-1287</Citation>
<ArticleIdList><ArticleId IdType="pubmed">32214704</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2001 Jul 31;98(16):9056-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11481472</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Bioorg Med Chem Lett. 2003 Nov 17;13(22):3989-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14592491</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nucleic Acids Res. 1994 Nov 11;22(22):4673-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7984417</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Struct Biol. 1997 Feb;4(2):147-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9033596</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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