RT Journal Article SR Electronic(1) A1 Schepetilnikov, M. V. A1 Manske, U. A1 Solovyev, A. G. A1 Zamyatnin, A. A. A1 Schiemann, J. A1 Morozov, S. Yu.YR 2005 T1 The hydrophobic segment of Potato virus X TGBp3 is a major determinant of the protein intracellular trafficking JF Journal of General Virology, VO 86 IS 8 SP 2379 OP 2391 DO https://doi.org/10.1099/vir.0.80865-0 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.80865-0