Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy.
Identifieur interne : 003182 ( PubMed/Corpus ); précédent : 003181; suivant : 003183Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy.
Auteurs : Yossef Kliger ; Erez Y. LevanonSource :
- BMC microbiology [ 1471-2180 ] ; 2003.
English descriptors
- KwdEn :
- Anti-HIV Agents (pharmacology), Antiviral Agents (pharmacology), Drug Design, Enfuvirtide, HIV Envelope Protein gp41 (pharmacology), HIV-1 (chemistry), HIV-1 (drug effects), Molecular Sequence Data, Peptide Fragments (pharmacology), Protein Conformation, SARS Virus (chemistry), SARS Virus (drug effects), Viral Fusion Proteins (chemistry), Viral Fusion Proteins (genetics), Viral Fusion Proteins (metabolism).
- MESH :
- chemical , chemistry : Viral Fusion Proteins.
- chemical , genetics : Viral Fusion Proteins.
- chemical , metabolism : Viral Fusion Proteins.
- chemical , pharmacology : Anti-HIV Agents, Antiviral Agents, HIV Envelope Protein gp41, Peptide Fragments.
- chemistry : HIV-1, SARS Virus.
- drug effects : HIV-1, SARS Virus.
- Drug Design, Enfuvirtide, Molecular Sequence Data, Protein Conformation.
Abstract
Severe acute respiratory syndrome (SARS) is a febrile respiratory illness. The disease has been etiologically linked to a novel coronavirus that has been named the SARS-associated coronavirus (SARS-CoV), whose genome was recently sequenced. Since it is a member of the Coronaviridae, its spike protein (S2) is believed to play a central role in viral entry by facilitating fusion between the viral and host cell membranes. The protein responsible for viral-induced membrane fusion of HIV-1 (gp41) differs in length, and has no sequence homology with S2.
DOI: 10.1186/1471-2180-3-20
PubMed: 14499001
Links to Exploration step
pubmed:14499001Le document en format XML
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<author><name sortKey="Kliger, Yossef" sort="Kliger, Yossef" uniqKey="Kliger Y" first="Yossef" last="Kliger">Yossef Kliger</name>
<affiliation><nlm:affiliation>Compugen LTD, Tel Aviv, 69512, Israel. kliger@compugen.co.il</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Levanon, Erez Y" sort="Levanon, Erez Y" uniqKey="Levanon E" first="Erez Y" last="Levanon">Erez Y. Levanon</name>
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<author><name sortKey="Kliger, Yossef" sort="Kliger, Yossef" uniqKey="Kliger Y" first="Yossef" last="Kliger">Yossef Kliger</name>
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<author><name sortKey="Levanon, Erez Y" sort="Levanon, Erez Y" uniqKey="Levanon E" first="Erez Y" last="Levanon">Erez Y. Levanon</name>
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<series><title level="j">BMC microbiology</title>
<idno type="eISSN">1471-2180</idno>
<imprint><date when="2003" type="published">2003</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anti-HIV Agents (pharmacology)</term>
<term>Antiviral Agents (pharmacology)</term>
<term>Drug Design</term>
<term>Enfuvirtide</term>
<term>HIV Envelope Protein gp41 (pharmacology)</term>
<term>HIV-1 (chemistry)</term>
<term>HIV-1 (drug effects)</term>
<term>Molecular Sequence Data</term>
<term>Peptide Fragments (pharmacology)</term>
<term>Protein Conformation</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (drug effects)</term>
<term>Viral Fusion Proteins (chemistry)</term>
<term>Viral Fusion Proteins (genetics)</term>
<term>Viral Fusion Proteins (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Viral Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Viral Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anti-HIV Agents</term>
<term>Antiviral Agents</term>
<term>HIV Envelope Protein gp41</term>
<term>Peptide Fragments</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>HIV-1</term>
<term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>HIV-1</term>
<term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Drug Design</term>
<term>Enfuvirtide</term>
<term>Molecular Sequence Data</term>
<term>Protein Conformation</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is a febrile respiratory illness. The disease has been etiologically linked to a novel coronavirus that has been named the SARS-associated coronavirus (SARS-CoV), whose genome was recently sequenced. Since it is a member of the Coronaviridae, its spike protein (S2) is believed to play a central role in viral entry by facilitating fusion between the viral and host cell membranes. The protein responsible for viral-induced membrane fusion of HIV-1 (gp41) differs in length, and has no sequence homology with S2.</div>
</front>
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<DateCompleted><Year>2004</Year>
<Month>02</Month>
<Day>24</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>30</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1471-2180</ISSN>
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<PubDate><Year>2003</Year>
<Month>Sep</Month>
<Day>21</Day>
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<Title>BMC microbiology</Title>
<ISOAbbreviation>BMC Microbiol.</ISOAbbreviation>
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<ArticleTitle>Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy.</ArticleTitle>
<Pagination><MedlinePgn>20</MedlinePgn>
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<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Severe acute respiratory syndrome (SARS) is a febrile respiratory illness. The disease has been etiologically linked to a novel coronavirus that has been named the SARS-associated coronavirus (SARS-CoV), whose genome was recently sequenced. Since it is a member of the Coronaviridae, its spike protein (S2) is believed to play a central role in viral entry by facilitating fusion between the viral and host cell membranes. The protein responsible for viral-induced membrane fusion of HIV-1 (gp41) differs in length, and has no sequence homology with S2.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">Sequence analysis reveals that the two viral proteins share the sequence motifs that construct their active conformation. These include (1) an N-terminal leucine/isoleucine zipper-like sequence, and (2) a C-terminal heptad repeat located upstream of (3) an aromatic residue-rich region juxtaposed to the (4) transmembrane segment.</AbstractText>
<AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">This study points to a similar mode of action for the two viral proteins, suggesting that anti-viral strategy that targets the viral-induced membrane fusion step can be adopted from HIV-1 to SARS-CoV. Recently the FDA approved Enfuvirtide, a synthetic peptide corresponding to the C-terminal heptad repeat of HIV-1 gp41, as an anti-AIDS agent. Enfuvirtide and C34, another anti HIV-1 peptide, exert their inhibitory activity by binding to a leucine/isoleucine zipper-like sequence in gp41, thus inhibiting a conformational change of gp41 required for its activation. We suggest that peptides corresponding to the C-terminal heptad repeat of the S2 protein may serve as inhibitors for SARS-CoV entry.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kliger</LastName>
<ForeName>Yossef</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Compugen LTD, Tel Aviv, 69512, Israel. kliger@compugen.co.il</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Levanon</LastName>
<ForeName>Erez Y</ForeName>
<Initials>EY</Initials>
</Author>
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<Language>eng</Language>
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<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
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