Abstract
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.
Published in
Journal of General Virology
2005, volume: 86, pages: 2379-2391
Publisher: SOC GENERAL MICROBIOLOGY
UKÄ Subject classification
Agricultural Science
Publication identifier
- DOI: https://doi.org/10.1099/vir.0.80865-0
Permanent link to this page (URI)
https://res.slu.se/id/publ/8433