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 protein that, in vitro, display both cytolytic and calmodulin-binding and -inhibitory properties that could contribute to cellular dysfunctions and cytopathogenesis during a persistent viral infection. In the current study, the structural specificity of the cytolytic and calmodulin-binding activities of the human immunodeficiency virus type 1 lentivirus lytic peptide (LLP-1) are examined with synthetic peptide homologs and analogs. The results of these studies demonstrate that even minor changes in LLP-1 amino acid content can markedly affect these properties, suggesting that sequence variation in these highly conserved LLP sequences may correlate with alterations in viral cytopathic properties.
Tencza
S B
SB
Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pennsylvania 15261, USA.
Miller
M A
MA
Islam
K
K
Mietzner
T A
TA
Montelaro
R C
RC
D000595:Amino Acid Sequence; D002147:Calmodulin / Q000235:genetics / Q000378:metabolism*; D003588:Cytopathogenic Effect, Viral; D015700:HIV Envelope Protein gp41 / Q000378:metabolism*; D015497:HIV-1 / Q000378:metabolism* / Q000502:physiology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000378:metabolism*
D002147:Calmodulin; D015700:HIV Envelope Protein gp41; D010446:Peptide Fragments; D014759:Viral Envelope Proteins