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J. Virol., Jun 1997, 4842-4846, Vol 71, No. 6
Copyright © 1997, American Society for Microbiology

Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest

L Selig, S Benichou, ME Rogel, LI Wu, MA Vodicka, J Sire, R Benarous and M Emerman
Laboratoire de Genetique Moleculaire des Interactions Proteiques, INSERM U332, ICGM, Universite Paris V, France.

The Vpr protein encoded by human immunodeficiency virus type 1 (HIV-1) is important for growth of virus in macrophages and prevents infected cells from passing into mitosis (G2 arrest). The cellular target for these functions is not known, but Vpr of HIV-1 and the related Vpr from simian immunodeficiency virus of sooty mangabeys (SIV(SM)) bind the DNA repair enzyme UNG, while the Vpx protein of SIV(SM) does not. Nonetheless, a mutational analysis of Vpr showed that binding to UNG is neither necessary nor sufficient for the effect of Vpr on the cell cycle.

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