Competitive inhibition of human immunodeficiency virus type-1 protease by the Gag-Pol transframe protein

C Paulus, S Hellebrand, U Tessmer, H Wolf, H G Kräusslich, R Wagner

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)

Abstract

The human immunodeficiency virus type-1 (HIV-1) transframe protein p6* is located between the structural and enzymatic domains of the Gag-Pol polyprotein, flanked by the nucleocapsid (NC) and the protease (PR) domain at its amino and carboxyl termini, respectively. Here, we report that recombinant highly purified HIV-1 p6* specifically inhibits mature HIV-1 PR activity. Kinetic analyses and cross-linking experiments revealed a competitive mechanism for PR inhibition by p6*. We further demonstrate that the four carboxyl-terminal residues of p6* are essential but not sufficient for p6*-mediated inhibition of PR activity. Based on these results, we suggest a role of the transframe protein p6* in regulating HIV-1 PR activity during viral replication.

Original languageEnglish
Pages (from-to)21539-43
Number of pages5
JournalJournal of Biological Chemistry
Volume274
Issue number31
Publication statusPublished - 30 Jul 1999

Keywords

  • Amino Acid Sequence
  • Binding, Competitive
  • Cross-Linking Reagents
  • Fusion Proteins, gag-pol
  • Gene Products, gag
  • HIV Protease
  • HIV Protease Inhibitors
  • Humans
  • Kinetics
  • Models, Chemical
  • Mutagenesis, Site-Directed
  • Recombinant Proteins
  • gag Gene Products, Human Immunodeficiency Virus
  • Journal Article
  • Research Support, Non-U.S. Gov't

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