Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 23, Pages 21013-21022Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.189274
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Funding
- National Institutes of Health [AI052014]
- Agence Nationale pour la Recherche sur le SIDA et les Hepatites Virales (ANRS)
- Sidaction
- French Research Ministry
- Mitsubishi Pharma Foundation
- Conseil Regional d'Ile de France
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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.
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