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Journal of Virology, August 2008, p. 8000-8012, Vol. 82, No. 16
0022-538X/08/$08.00+0     doi:10.1128/JVI.02752-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Murine Gammaherpesvirus 68 Open Reading Frame 75c Tegument Protein Induces the Degradation of PML and Is Essential for Production of Infectious Virus{triangledown}

Paul D. Ling,* Jie Tan, Jaturong Sewatanon, and RongSheng Peng

Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 77030

Received 27 December 2007/ Accepted 19 May 2008

Promyelocytic Leukemia nuclear body (PML NB) proteins mediate an intrinsic cellular host defense response against virus infections. Herpesviruses express proteins that modulate PML or PML-associated proteins by a variety of strategies, including degradation of PML or relocalization of PML NB proteins. The consequences of PML-herpesvirus interactions during infection in vivo have yet to be investigated in detail, largely because of the species-specific tropism of many human herpesviruses. Murine gammaherpesvirus 68 ({gamma}HV68) is emerging as a suitable model to study basic biological questions of virus-host interactions because it naturally infects mice. Therefore, we sought to determine whether {gamma}HV68 targets PML NBs as part of its natural life cycle. We found that {gamma}HV68 induces PML degradation through a proteasome-dependent mechanism and that loss of PML results in more robust virus replication in mouse fibroblasts. Surprisingly, {gamma}HV68-mediated PML degradation was mediated by the virion tegument protein ORF75c, which shares homology with the cellular formylglycinamide ribotide amidotransferase enzyme. In addition, we show that ORF75c is essential for production of infectious virus. ORF75 homologs are conserved in all rhadinoviruses but so far have no assigned functions. Our studies shed light on a potential role for this unusual protein in rhadinovirus biology and suggest that {gamma}HV68 will be a useful model for investigation of PML-herpesvirus interactions in vivo.

* Corresponding author. Mailing address: Department of Molecular Virology and Microbiology, Baylor College of Medicine, Mail Stop BCM-385, One Baylor Plaza, Houston, Texas 77030. Phone: 713 798-8474. Fax: 713 798 3586. E-mail: pling{at}bcm.edu

{triangledown} Published ahead of print on 28 May 2008.

Journal of Virology, August 2008, p. 8000-8012, Vol. 82, No. 16
0022-538X/08/$08.00+0     doi:10.1128/JVI.02752-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Guo, H., Wang, L., Peng, L., Zhou, Z. H., Deng, H. (2009). Open Reading Frame 33 of a Gammaherpesvirus Encodes a Tegument Protein Essential for Virion Morphogenesis and Egress. J. Virol. 83: 10582-10595 [Abstract] [Full Text]  


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