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Journal of Virology, February 2008, p. 1284-1293, Vol. 82, No. 3
0022-538X/08/$08.00+0     doi:10.1128/JVI.01164-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Intracellular Targeting of a Hordeiviral Membrane-Spanning Movement Protein: Sequence Requirements and Involvement of an Unconventional Mechanism{triangledown}

Mikhail V. Schepetilnikov,1,2,{dagger} Andrey G. Solovyev,1,4 Elena N. Gorshkova,1 Joachim Schiemann,3 Alexey I. Prokhnevsky,2 Valerian V. Dolja,2* and Sergey Y. Morozov1*

A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia,1 Department of Botany and Plant Pathology and Center for Genome Research and Biocomputing, Oregon State University, Corvallis, Oregon 97331,2 Institute of Plant Virology, Microbiology, and Biosafety, Federal Biological Research Centre for Agriculture and Forestry, Messeweg 11/12, D-38104 Braunschweig, Germany,3 Institute of Agricultural Biotechnology, Russian Academy of Agricultural Sciences, Timiryazevskaya 42, 127550 Moscow, Russia4

Received 29 May 2007/ Accepted 12 November 2007

The membrane-spanning protein TGBp3 is one of the three movement proteins (MPs) of Poa semilatent virus. TGBp3 is thought to direct other viral MPs and genomic RNA to peripheral bodies located in close proximity to plasmodesmata. We used the ectopic expression of green fluorescent protein-fused TGBp3 in epidermal cells of Nicotiana benthamiana leaves to study the TGBp3 intracellular trafficking pathway. Treatment with inhibitors was used to reveal that the targeting of TGBp3 to plasmodesmata does not require a functional cytoskeleton or secretory system. In addition, the suppression of endoplasmic reticulum-derived vesicle formation by a dominant negative mutant of small GTPase Sar1 had no detectable effect on TGBp3 trafficking to peripheral bodies. Collectively, these results suggested the involvement of an unconventional pathway in the intracellular transport of TGBp3. The determinants of targeting to plasmodesmata were localized to the C-terminal region of TGBp3, including the conserved hydrophilic and terminal membrane-spanning domains.

* Corresponding author. Mailing address for Valerian V. Dolja: Department of Botany and Plant Pathology, Oregon State University, Cordley Hall 2082, Corvallis, OR 97331. Phone: (541) 737-5472. Fax: (541) 737-3573. E-mail: doljav{at}science.oregonstate.edu. Mailing address for Sergey Y. Morozov: A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia. Phone: 7 (495) 939-3198. Fax: 7 (495) 939-3181. E-mail: morozov{at}genebee.msu.su

{triangledown} Published ahead of print on 21 November 2007.

{dagger} Present address: Institut de Biologie Moléculaire des Plantes, Laboratoire propre du CNRS (UPR 2357) conventionné avec l'Université Louis Pasteur (Strasbourg 1), Strasbourg, France.

Journal of Virology, February 2008, p. 1284-1293, Vol. 82, No. 3
0022-538X/08/$08.00+0     doi:10.1128/JVI.01164-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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