LEDGF/p75 interferes with the formation of synaptic nucleoprotein complexes that catalyze full-site HIV-1 DNA integration in vitro: implications for the mechanism of viral cDNA integration

Virology. 2007 Mar 30;360(1):1-5. doi: 10.1016/j.virol.2006.12.022. Epub 2007 Jan 26.

Abstract

An integrase dimer can process and integrate a single HIV-1 DNA end in vitro, whereas a tetramer is required to integrate two ends. LEDGF/p75 can potently stimulate integrase activity, but its effects on half- versus full-site integration have not been investigated. Stimulation of half-site but inhibition of full-site integration is revealed here. LEDGF/p75 seems to interfere with integrase oligomerization, but does not inhibit the catalytic activity of pre-assembled complexes. We therefore speculate that LEDGF/p75 function is restricted to a point in the viral lifecycle that occurs after the formation of the preintegration synaptic complex, for example, as a chromatin-associated tethering factor.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • DNA, Complementary / physiology*
  • DNA, Viral / physiology*
  • HIV Integrase / metabolism
  • HIV-1 / physiology*
  • Humans
  • Intercellular Signaling Peptides and Proteins / physiology*
  • Nucleoproteins / metabolism*
  • Synaptic Membranes / metabolism
  • Synaptic Membranes / virology*
  • Viral Proteins / physiology*
  • Virus Integration

Substances

  • DNA, Complementary
  • DNA, Viral
  • Intercellular Signaling Peptides and Proteins
  • Nucleoproteins
  • Viral Proteins
  • lens epithelium-derived growth factor
  • HIV Integrase