PLEIOTROPIC EFFECTS OF SMALL PEPTIDES CORRESPONDING IN SEQUENCE TO THE CYTOPLASMIC DOMAIN OF THE INFLUENZA-VIRUS HEMAGGLUTININ 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 envelo ped virus transmembrane glycoproteins have been extended to include ad ditional 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 haema gglutinin HA(2) C-terminal sequence was not specific for influenza vir us and the integrity of newly released, extracellular vesicular stomat itis virus particles was affected by the peptide. A shortened, six ami no acid form of this peptide inactivated cell-free preparations of inf luenza, vesicular stomatitis and Sindbis viruses and also bound effect ively to virus-encoded structural proteins. For this virus-protein int eraction, the peptide sequence was highly specific with respect to its hydrophobicity and net ionic charge.