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The human polycomb group EED protein interacts with the integrase of human immunodeficiency virus type 1.

Human EED, a member of the superfamily of WD-40 repeat proteins and of the Polycomb group proteins, has been identified as a cellular partner of the human immunodeficiency virus type 1 (HIV-1) matrix (MA) protein (R. Peytavi et al., J. Biol. Chem. 274:1635-1645, 1999). In the present study, EED was found to interact with HIV-1 integrase (IN) both in vitro and in vivo in yeast. In vitro, data from mutagenesis studies, pull-down assays, and phage biopanning suggested that EED-binding site(s) are located in the C-terminal domain of IN, between residues 212 and 264. In EED, two putative discrete IN-binding sites were mapped to its N-terminal moiety, at a distance from the MA-binding site, but EED-IN interaction also required the integrity of the EED last two WD repeats. EED showed an apparent positive effect on IN-mediated DNA integration reaction in vitro, in a dose-dependent manner. In situ analysis by immunoelectron microscopy (IEM) of cellular distribution of IN and EED in HIV-1-infected cells (HeLa CD4(+) cells or MT4 lymphoid cells) showed that IN and EED colocalized in the nucleus and near nuclear pores, with maximum colocalization events occurring at 6 h postinfection (p.i.). Triple colocalizations of IN, EED, and MA were also observed in the nucleoplasm of infected cells at 6 h p.i., suggesting the ocurrence of multiprotein complexes involving these three proteins at early steps of the HIV-1 virus life cycle. Such IEM patterns were not observed with a noninfectious, envelope deletion mutant of HIV-1.

Pubmed ID: 14610174


  • Violot S
  • Hong SS
  • Rakotobe D
  • Petit C
  • Gay B
  • Moreau K
  • Billaud G
  • Priet S
  • Sire J
  • Schwartz O
  • Mouscadet JF
  • Boulanger P


Journal of virology

Publication Data

December 11, 2003

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Cell Line
  • HIV Integrase
  • HIV-1
  • Humans
  • Microscopy, Immunoelectron
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Polycomb Repressive Complex 2
  • Protein Binding
  • Recombinant Proteins
  • Repressor Proteins
  • Sequence Homology, Amino Acid
  • Two-Hybrid System Techniques