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

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

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Abstract Background Severe acute respiratory syndrome (SARS) is a All-Purpose Cleaners 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 3D TPU Parts as inhibitors for SARS-CoV entry.