Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy.
Identifieur interne : 003299 ( PubMed/Checkpoint ); précédent : 003298; suivant : 003300Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy.
Auteurs : Yossef Kliger [Israël] ; Erez Y. LevanonSource :
- BMC microbiology [ 1471-2180 ] ; 2003.
Descripteurs français
- KwdFr :
- Agents antiVIH (pharmacologie), Antiviraux (pharmacologie), Conception de médicament, Conformation des protéines, Données de séquences moléculaires, Fragments peptidiques (pharmacologie), Protéine d'enveloppe gp41 du VIH (pharmacologie), Protéines de fusion virale (), Protéines de fusion virale (génétique), Protéines de fusion virale (métabolisme), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (), Virus du SRAS ().
- MESH :
- génétique : Protéines de fusion virale.
- métabolisme : Protéines de fusion virale.
- pharmacologie : Agents antiVIH, Antiviraux, Fragments peptidiques, Protéine d'enveloppe gp41 du VIH.
- Conception de médicament, Conformation des protéines, Données de séquences moléculaires, Protéines de fusion virale, VIH-1 (Virus de l'Immunodéficience Humaine de type 1), Virus du SRAS.
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
Affiliations:
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pubmed:14499001Le document en format XML
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<term>Antiviral Agents</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>HIV-1</term>
<term>SARS Virus</term>
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<term>Données de séquences moléculaires</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>
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<Month>Sep</Month>
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<Title>BMC microbiology</Title>
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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>
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