Abrogation of Vif function by peptide derived from the N-terminal region of the human immunodeficiency virus type 1 (HIV-1) protease

Marina Hutoran, Elena Britan, Lea Baraz, Immanuel Blumenzweig, Michael Steinitz, Moshe Kotler

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

The human immunodeficiency virus type 1 (HIV-1) auxiliary gene vif is essential for virus propagation in peripheral blood lymphocytes, macrophages, and in some T-cell lines. Previously, it was demonstrated that Vif inhibits the autoprocessing of truncated HIV-1 Gag-Pol polyproteins expressed in bacterial cells, and that purified recombinant Vif and Vif-derived peptides inhibit and bind HIV-1 protease (PR). Here we show that Vif interacts with the N-terminal region of HIV-1 PR, and demonstrate that peptide derived from the N-terminal region of PR abrogates Vif function in non-permissive cells. Specifically, we show that (i) Vif protein binds HIV-1 PR, but not covalently linked tethered PR-PR; (ii) the four amino acids residing at the N terminus of HIV-1 PR are essential for Vif/PR interaction; (iii) synthetic peptide derived from the N terminus of HIV-1 PR inhibits Vif/PR binding; and (iv) this peptide inhibits the propagation of HIV-1 in restrictive cells. Based on these data, we suggest that Vif interacts with the dimerization sites of the viral protease, and that peptide residing at the N terminus of PR abrogates Vif function(s).

Original languageEnglish
Pages (from-to)261-270
Number of pages10
JournalVirology
Volume330
Issue number1
DOIs
StatePublished - 5 Dec 2004

Keywords

  • APOBEC3G
  • HIV-1
  • HIV-1 protease
  • Synthetic peptides
  • Vif

Fingerprint

Dive into the research topics of 'Abrogation of Vif function by peptide derived from the N-terminal region of the human immunodeficiency virus type 1 (HIV-1) protease'. Together they form a unique fingerprint.

Cite this