EFFECT OF AMINO-ACID SUBSTITUTIONS ON CALMODULIN-BINDING AND CYTOLYTIC PROPERTIES OF THE LLP-1 PEPTIDE SEGMENT OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 TRANSMEMBRANE PROTEIN

Previous studies have identified two highly basic amphipathic helical regions in the human immunodeficiency virus type 1 transmembrane prote in that, in vitro, display both cytolytic and calmodulin-binding and - inhibitory properties that could contribute to cellular dysfunctions a nd cytopathogenesis during a persistent viral infection. In the curren t study, the structural specificity of the cytolytic and calmodulin-bi nding activities of the human immunodeficiency virus type 1 lentivirus lytic peptide (LLP-1) are examined with synthetic peptide homologs an d analogs. The results of these studies demonstrate that even minor ch anges in LLP-1 amino acid content can markedly affect these properties , suggesting that sequence variation in these highly conserved LLP seq uences may correlate with alterations in viral cytopathic properties.