Free accessBrief reportFirst published online 1997-8
Pleiotropic Effects of Small Peptides Corresponding in Sequence to the Cytoplasmic Domain of the Influenza Virus Haemagglutinin on Influenza,Vesicular Stomatitis and Sindbis Viruses
Studies on the antiviral effects of short peptides of six to 10 amino acids that correspond in sequence to the cytoplasmic domains of enveloped virus transmembrane glycoproteins have been extended to include additional kinds of assay in order to determine a site for inhibition of virus replication. Based on these experiments, the antiviral activity previously described for a decapeptide with the influenza virus haemagglutinin HA2 C-terminal sequence was not specific for influenza virus and the integrity of newly released, extracellular vesicular stomatitis virus particles was affected by the peptide. A shortened, six amino acid form of this peptide inactivated cell-free preparations of influenza, vesicular stomatitis and Sindbis viruses and also bound effectively to virus-encoded structural proteins. For this virus-protein interaction, the peptide sequence was highly specific with respect to its hydrophobicity and net ionic charge.
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