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Journal of Virology, January 2005, p. 597-601, Vol. 79, No. 1
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.1.597-601.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Poxviral RING Protein p28 Is a Ubiquitin Ligase That Targets Ubiquitin to Viral Replication Factories

Bianca T. Hovey Nerenberg,1,{dagger} John Taylor,2,{dagger} Eric Bartee,1 Kristine Gouveia,1 Michele Barry,2 and Klaus Früh1*

Vaccine and Gene Therapy Institute, Oregon Health and Science University, Beaverton, Oregon,1 Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada2

Received 29 June 2004/ Accepted 3 August 2004

The poxviral RING protein p28 is a virulence factor whose molecular function is unknown. Many cellular RING-containing proteins act as ubiquitin ligases (RING-E3s) connecting selected substrate proteins to the ubiquitination machinery. Here we demonstrate that vaccinia virus p28 and its homologue in myxoma virus, M143R, can mediate the formation of polyubiquitin conjugates, while RING mutants of both p28 and M143R cannot. Furthermore, p28 is ubiquitinated in vivo and ubiquitin colocalizes with p28 to virus factories independently of an intact RING domain. These results implicate the ubiquitin system in poxviral virulence.

* Corresponding author. Mailing address: Vaccine and Gene Therapy Institute, Oregon Health and Science University, 505 NW 185th Ave., Beaverton, OR 97006. Phone: (503) 418-2735. Fax: (503) 418-2701. E-mail: fruehk{at}ohsu.edu.

{dagger} B. T. Hovey Nerenberg and J. Taylor contributed equally to this work.

Journal of Virology, January 2005, p. 597-601, Vol. 79, No. 1
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.1.597-601.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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