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The hydrophobic segment of Potato virus X TGBp3 is a major determinant of the protein intracellular trafficking

¹ A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia
² Institute of Plant Virology, Microbiology and Biosafety, Federal Biological Research Centre for Agriculture and Forestry, Messeweg 11/12, D-38104 Braunschweig, Germany
³ Natural Sciences Center of A. M. Prokhorov, General Physics Institute, Russian Academy of Sciences, Bld L-2, 38 Vavilov Str., Moscow 119991, Russia
⁴ Department of Plant Biology and Forest Genetics, Swedish University of Agricultural Sciences (SLU), PO Box 7080, S-750 07 Uppsala, Sweden

Correspondence
S. Yu. Morozov
morozov{at}genebee.msu.su

Potato virus X (PVX) encodes three movement proteins, TGBp1, TGBp2 and TGBp3. The 8 kDa TGBp3 is a membrane-embedded protein that has an N-terminal hydrophobic sequence segment and a hydrophilic C terminus. TGBp3 mutants with deletions in the C-terminal hydrophilic region retain the ability to be targeted to cell peripheral structures and to support limited PVX cell-to-cell movement, suggesting that the basic TGBp3 functions are associated with its N-terminal transmembrane region. Fusion of green fluorescent protein to the TGBp3 N terminus abrogates protein activities in intracellular trafficking and virus movement. The intracellular transport of TGBp3 from sites of its synthesis in the rough endoplasmic reticulum (ER) to ER-derived peripheral bodies involves a non-conventional COPII-independent pathway. However, integrity of the C-terminal hydrophilic sequence is required for entrance to this non-canonical route.

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