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Journal of Virology, February 1999, p. 1682-1688, Vol. 73, No. 2
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

DNA Repair Enzyme Uracil DNA Glycosylase Is Specifically Incorporated into Human Immunodeficiency Virus Type 1 Viral Particles through a Vpr-Independent Mechanism

Karen E. Willetts, Françoise Rey, Isabelle Agostini, Jean-Marc Navarro, Yves Baudat, Robert Vigne, and Joséphine Sire*

INSERM U372, 13276 Marseille Cedex 9, France

Received 8 July 1998/Accepted 15 October 1998

The Vpr protein, encoded by the human immunodeficiency virus type 1 (HIV-1) genome, is one of the nonstructural proteins packaged in large amounts into viral particles. We have previously reported that Vpr associates with the DNA repair enzyme uracil DNA glycosylase (UDG). In this study, we extended these observations by investigating whether UDG is incorporated into virions and whether this incorporation requires the presence of Vpr. Our results, with highly purified viruses, show that UDG is efficiently incorporated either into wild-type virions or into Vpr-deficient HIV-1 virions, indicating that Vpr is not involved in UDG packaging. Using an in vitro protein-protein binding assay, we reveal a direct interaction between the precursor form of UDG and the viral integrase (IN). Finally, we demonstrate that IN-defective viruses fail to incorporate UDG, indicating that IN is required for packaging of UDG into virions.

* Corresponding author. Mailing address: INSERM U372, 163 ave. de Luminy, BP 178, 13276 Marseille Cedex 9, France. Phone: (33) 4 91 82 75 91. Fax: (33) 4 91 82 60 61. E-mail: jsire{at}inserm-u372.univ-mrs.fr.

Journal of Virology, February 1999, p. 1682-1688, Vol. 73, No. 2
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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