ArticleJournal of virology2003
The human polycomb group EED protein interacts with the integrase of human immunodeficiency virus type 1.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 78 citations in OpenAlex.
- Epigenetic Regulation by Polycomb Complexes from Drosophila to Human and Its Relation to Communicable Disease Pathogenesis.International journal of molecular sciences · 2022Review
- A Noncanonical Function of Polycomb Repressive Complexes Promotes Human Cytomegalovirus Lytic DNA Replication and Serves as a Novel Cellular Target for Antiviral Intervention.Journal of virology · 2019Article
- Interaction of HIV-1 integrase with polypyrimidine tract binding protein and associated splicing factor (PSF) and its impact on HIV-1 replication.Retrovirology · 2019Article
- The role of enhancer of zeste homolog 2: From viral epigenetics to the carcinogenesis of hepatocellular carcinoma.Journal of cellular physiology · 2018Review
- Interactions between Retroviruses and the Host Cell Genome.Molecular therapy. Methods & clinical development · 2018Review
- Epigenetic regulation of HIV-1 latency: focus on polycomb group (PcG) proteins.Clinical epigenetics · 2018Review
- Stem-loop binding protein is a multifaceted cellular regulator of HIV-1 replication.The Journal of clinical investigation · 2016Article
- Inhibiting the HIV integration process: past, present, and the future.Journal of medicinal chemistry · 2014Article
- Proteomic analysis of early HIV-1 nucleoprotein complexes.Journal of proteome research · 2013Article
- Promoter polymorphism of the EED gene is associated with the susceptibility to ulcerative colitis.Digestive diseases and sciences · 2012Article
- Correlation of recombinant integrase activity and functional preintegration complex formation during acute infection by replication-defective integrase mutant human immunodeficiency virus.Journal of virology · 2012Article
- Sequential deletion of the integrase (Gag-Pol) carboxyl terminus reveals distinct phenotypic classes of defective HIV-1.Journal of virology · 2011Article
- Inhibition of early stages of HIV-1 assembly by INI1/hSNF5 transdominant negative mutant S6.Journal of virology · 2011Article
- Identification of host proteins associated with HIV-1 preintegration complexes isolated from infected CD4+ cells.Retrovirology · 2010Article
- Transcription factor YY1 interacts with retroviral integrases and facilitates integration of moloney murine leukemia virus cDNA into the host chromosomes.Journal of virology · 2010Article
- Prospective strategies for targeting HIV-1 integrase function.Future medicinal chemistry · 2010Article
- Article
- Changes in the accessibility of the HIV-1 Integrase C-terminus in the presence of cellular proteins.Retrovirology · 2010Article
- Article
- Methods for integration site distribution analyses in animal cell genomes.Methods (San Diego, Calif.) · 2009Article
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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