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

S. B. Tencza, Mark Miller, K. Islam, T. A. Mietzner, R. C. Montelaro

Research output: Contribution to journalComment/debate

41 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)5199-5202
Number of pages4
JournalJournal of Virology
Volume69
Issue number8
StatePublished - 1995
Externally publishedYes

Fingerprint

transmembrane proteins
amino acid substitution
calmodulin
Amino Acid Substitution
Calmodulin
Human immunodeficiency virus 1
HIV-1
peptides
Lentivirus
Peptides
conserved sequences
Conserved Sequence
synthetic peptides
Virus Diseases
Proteins
Amino Acids
amino acids
infection
sequence diversity
In Vitro Techniques

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

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. / Tencza, S. B.; Miller, Mark; Islam, K.; Mietzner, T. A.; Montelaro, R. C.

In: Journal of Virology, Vol. 69, No. 8, 1995, p. 5199-5202.

Research output: Contribution to journalComment/debate

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AU - Montelaro, R. C.

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