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Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy.

Identifieur interne : 003299 ( PubMed/Checkpoint ); précédent : 003298; suivant : 003300

Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy.

Auteurs : Yossef Kliger [Israël] ; Erez Y. Levanon

Source :

RBID : pubmed:14499001

Descripteurs français

English descriptors

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


Affiliations:


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pubmed:14499001

Le document en format XML

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<term>Viral Fusion Proteins</term>
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<term>Viral Fusion Proteins</term>
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<term>Anti-HIV Agents</term>
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<term>HIV Envelope Protein gp41</term>
<term>Peptide Fragments</term>
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<term>HIV-1</term>
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<term>HIV-1</term>
<term>SARS Virus</term>
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<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>
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<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>
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