Peptide inhibitors of HIV-1 egress

ACS Chem Biol. 2008 Dec 19;3(12):745-7. doi: 10.1021/cb800296j.

Abstract

HIV-1 release requires a direct interaction between the p6 domain of the Gag protein and Tsg101, a component of the cellular endosomal sorting complex required for transport I (ESCRT-I). Disruption of the binding between Gag and Tsg101 is highly detrimental to particle release, making this viral-host cell interaction a potential target for the development of novel anti-HIV-1 agents. An article in this issue reports on the application of a bacterial reverse two-hybrid strategy to identify a cyclic peptide that disrupts Gag-Tsg101 binding and suppresses HIV-1 particle release.

Publication types

  • Editorial

MeSH terms

  • DNA-Binding Proteins / antagonists & inhibitors*
  • DNA-Binding Proteins / metabolism
  • Endosomal Sorting Complexes Required for Transport
  • Endosomes / metabolism
  • HIV-1 / drug effects*
  • HIV-1 / physiology*
  • Humans
  • Models, Biological
  • Peptides, Cyclic / pharmacology*
  • Protein Binding / drug effects
  • Transcription Factors / antagonists & inhibitors*
  • Transcription Factors / metabolism
  • Vesicular Transport Proteins / drug effects
  • Vesicular Transport Proteins / metabolism
  • gag Gene Products, Human Immunodeficiency Virus / antagonists & inhibitors*
  • gag Gene Products, Human Immunodeficiency Virus / metabolism

Substances

  • DNA-Binding Proteins
  • Endosomal Sorting Complexes Required for Transport
  • Peptides, Cyclic
  • Transcription Factors
  • Tsg101 protein
  • Vesicular Transport Proteins
  • gag Gene Products, Human Immunodeficiency Virus
  • p6 gag protein, Human immunodeficiency virus 1