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

  • Yossef Kliger
  • Erez Y Levanon
BioMed Central
Publication Date
Sep 21, 2003
  • Biology
  • Medicine

Abstract ral ss BioMed CentBMC Microbiology Open AcceResearch article Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy Yossef Kliger* and Erez Y Levanon Address: Compugen LTD, Tel Aviv, 69512, Israel Email: Yossef Kliger* - [email protected]; Erez Y Levanon - [email protected] * Corresponding author Abstract 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. 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. 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. Background Infection by man


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