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Journal of Virology, January 2006, p. 875-882, Vol. 80, No. 2
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.2.875-882.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Uracil DNA Glycosylase Is Dispensable for Human Immunodeficiency Virus Type 1 Replication and Does Not Contribute to the Antiviral Effects of the Cytidine Deaminase Apobec3G

Shari M. Kaiser1,2 and Michael Emerman2*

Molecular and Cellular Biology Program, University of Washington, Seattle, Washington,1 Division of Human Biology, Fred Hutchinson Cancer Research Center, Seattle, Washington 981092

Received 5 October 2005/ Accepted 28 October 2005

It is well established that many host factors are involved in the replication of human immunodeficiency virus (HIV) type 1. One host protein, uracil DNA glycosylase 2 (UNG2), binds to multiple viral proteins and is packaged into HIV type 1 virions. UNG initiates the removal of uracils from DNA, and this has been proposed to be important both for reverse transcription and as a mediator to the antiviral effect of virion-incorporated Apobec3G, a cytidine deaminase that generates numerous uracils in the viral DNA during virus replication. We used a natural human UNG–/– cell line as well as cells that express a potent catalytic active-site inhibitor of UNG to assess the effects of removing UNG activity on HIV infectivity. In both cases, we find UNG2 activity and protein to be completely dispensable for virus replication. Moreover, we find that virion-associated UNG2 does not affect the loss of infectivity caused by Apobec3G.

* Corresponding author. Mailing address: Division of Human Biology, Mail Stop C2-023, Fred Hutchinson Cancer Research Center, 1100 Fairview Ave. N, P.O. Box 10924, Seattle, WA 98109-1024. Phone: (206) 667-5058. Fax: (206) 667-6523. E-mail: memerman{at}fhcrc.org.

Journal of Virology, January 2006, p. 875-882, Vol. 80, No. 2
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.2.875-882.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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