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J Biol Chem. 2011 Jun 10;286(23):21013-22. doi: 10.1074/jbc.M110.189274. Epub 2011 Mar 21.

Impairment of human immunodeficiency virus type-1 integrase SUMOylation correlates with an early replication defect.

Author information

  • 1CNRS UMR7212, INSERM U944, Institut Universitaire d'Hématologie-Université Paris7 Diderot, 75475 Paris, France. alessia.zamborlini@univ-paris-diderot.fr

Abstract

HIV-1 integrase (IN) orchestrates the integration of the reverse transcribed viral cDNA into the host cell genome and participates also in other steps of HIV-1 replication. Cellular and viral factors assist IN in performing its multiple functions, and post-translational modifications contribute to modulate its activities. Here, we show that HIV-1 IN is modified by SUMO proteins and that phylogenetically conserved SUMOylation consensus motifs represent major SUMO acceptor sites. Viruses harboring SUMOylation site IN mutants displayed a replication defect that was mapped during the early stages of infection, before integration but after reverse transcription. Because SUMOylation-defective IN mutants retained WT catalytic activity, we hypothesize that SUMOylation might regulate the affinity of IN for co-factors, contributing to efficient HIV-1 replication.

PMID:
21454548
[PubMed - indexed for MEDLINE]
PMCID:
PMC3121452
Free PMC Article

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