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Journal of Virology, February 2007, p. 1899-1911, Vol. 81, No. 4
0022-538X/07/$08.00+0     doi:10.1128/JVI.02009-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Mutations in the Central Domain of Potato Virus X TGBp2 Eliminate Granular Vesicles and Virus Cell-to-Cell Trafficking{triangledown}

Ho-Jong Ju, James E. Brown, Chang-Ming Ye, and Jeanmarie Verchot-Lubicz*

Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, Oklahoma 74078

Received 14 September 2006/ Accepted 26 November 2006

Most RNA viruses remodel the endomembrane network to promote virus replication, maturation, or egress. Rearrangement of cellular membranes is a crucial component of viral pathogenesis. The PVX TGBp2 protein induces vesicles of the granular type to bud from the endoplasmic reticulum network. Green fluorescent protein (GFP) was fused to the PVX TGBp2 coding sequence and inserted into the viral genome and into pRTL2 plasmids to study protein subcellular targeting in the presence and absence of virus infection. Mutations were introduced into the central domain of TGBp2, which contains a stretch of conserved amino acids. Deletion of a 10-amino-acid segment (m2 mutation) overlapping the segment of conserved residues eliminated the granular vesicle and inhibited virus movement. GFP-TGBp2m2 proteins accumulated in enlarged vesicles. Substitution of individual conserved residues in the same region similarly inhibited virus movement and caused the mutant GFP-TGBp2 fusion proteins to accumulate in enlarged vesicles. These results identify a novel element in the PVX TGBp2 protein which determines vesicle morphology. In addition, the data indicate that vesicles of the granular type induced by TGBp2 are necessary for PVX plasmodesmata transport.

* Corresponding author. Mailing address: Oklahoma State University, 127 Noble Research Center, Stillwater, OK 74078. Phone: (405) 744-7895. Fax: (405) 744-6039. E-mail: verchot.lubicz{at}okstate.edu.

{triangledown} Published ahead of print on 6 December 2006.

Journal of Virology, February 2007, p. 1899-1911, Vol. 81, No. 4
0022-538X/07/$08.00+0     doi:10.1128/JVI.02009-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wei, T., Wang, A. (2008). Biogenesis of Cytoplasmic Membranous Vesicles for Plant Potyvirus Replication Occurs at Endoplasmic Reticulum Exit Sites in a COPI- and COPII-Dependent Manner. J. Virol. 82: 12252-12264 [Abstract] [Full Text]  
  • Verchot-Lubicz, J., Ye, C.-M., Bamunusinghe, D. (2007). Molecular biology of potexviruses: recent advances. J. Gen. Virol. 88: 1643-1655 [Abstract] [Full Text]  


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