Equivalent inhibition of half-site and full-site retroviral strand transfer reactions by structurally diverse compounds

J Virol. 1997 Jan;71(1):807-11. doi: 10.1128/JVI.71.1.807-811.1997.

Abstract

In vitro assay systems which use recombinant retroviral integrase (IN) and short DNA oligonucleotides fail to recapitulate the full-site integration reaction as it is known to occur in vivo. The relevance of using such circumscribed in vitro assays to define inhibitors of retroviral integration has not been formerly demonstrated. Therefore, we analyzed a series of structurally diverse inhibitors with respect to inhibition of both half-site and full-site strand transfer reactions with either recombinant or virion-produced IN. Half-site and full-site reactions catalyzed by avian myeloblastosis virus and human immunodeficiency virus type 1 (HIV-1) IN from virions are shown to be equivalently sensitive to inhibition by compounds which inhibit half-site reactions catalyzed by the recombinant HIV-1 IN. These studies therefore support the utility of using in vitro assays employing either recombinant or virion-derived IN to identify inhibitors of integration.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Avian Myeloblastosis Virus / enzymology*
  • HIV Integrase / metabolism*
  • HIV Integrase Inhibitors / chemistry
  • HIV Integrase Inhibitors / pharmacology*
  • HIV-1 / enzymology*
  • Humans
  • Integrase Inhibitors / chemistry
  • Integrase Inhibitors / pharmacology*
  • Integrases / metabolism*
  • Magnesium
  • Manganese
  • Molecular Structure
  • Oligodeoxyribonucleotides
  • Recombinant Proteins / antagonists & inhibitors
  • Virus Integration*

Substances

  • HIV Integrase Inhibitors
  • Integrase Inhibitors
  • Oligodeoxyribonucleotides
  • Recombinant Proteins
  • Manganese
  • HIV Integrase
  • Integrases
  • Magnesium