Turnip Mosaic Virus Uses the SNARE Protein VTI11 in an Unconventional Route for Replication Vesicle Trafficking

Autor: Hugo Germain, Daniel Garcia Cabanillas, Huanquan Zheng, Yasuyuki Yamaji, Nooshin Movahed, Jean-François Laliberté, Jun Jiang
Přispěvatelé: Institut Armand Frappier (INRS-IAF), Institut National de la Recherche Scientifique [Québec] (INRS)-Réseau International des Instituts Pasteur (RIIP), McGill University = Université McGill [Montréal, Canada], Université du Québec à Trois-Rivières (UQTR), The University of Tokyo (UTokyo), This work was supported by grants from the Natural Science and Engineering Research Council of Canada and from Le Fonds Québécois de Recherche sur la Nature et les Technologies to H.Z. and J.-F.L., We thank F. Prieto Bruckner and V. Schurdi-Levraud for their advice and technical support for RT-qPCR experiments. We thank J. Tremblay for his technical expertise assistance with confocal microscopy and S.G. Lazarowitz (Cornell University) for the Arabidopsis syta-1 seeds. We thank P. Moffett (Université de Sherbrooke) for valuable advice and for critically reading the manuscript.
Jazyk: angličtina
Rok vydání: 2018
Předmět:
Zdroj: The Plant cell
The Plant cell, American Society of Plant Biologists (ASPB), 2018, 30 (10), pp.2594-2615. ⟨10.1105/tpc.18.00281⟩
ISSN: 1040-4651
1532-298X
DOI: 10.1105/tpc.18.00281⟩
Popis: International audience; Infection of plant cells by RNA viruses leads to the generation of organelle-like subcellular structures that contain the viral replication complex. During Turnip mosaic virus (TuMV) infection of Nicotiana benthamiana, the viral membrane protein 6K2 plays a key role in the release of motile replication vesicles from the host endoplasmic reticulum (ER). Here, we demonstrate that 6K2 contains a GxxxG motif within its predicted transmembrane domain that is vital for TuMV infection. Replacement of the Gly with Val within this motif inhibited virus production, and this was due to a relocation of the viral protein to the Golgi apparatus and the plasma membrane. This indicated that passage of 6K2 through the Golgi apparatus is a dead-end avenue for virus infection. Impairing the fusion of transport vesicles between the ER and the Golgi apparatus by overexpression of the SNARE Sec22 protein resulted in enhanced intercellular virus movement. Likewise, expression of nonfunctional, Golgi-located synaptotagmin during infection enhanced TuMV intercellular movement. 6K2 copurified with VTI11, a prevacuolar compartment SNARE protein. An Arabidopsis thaliana vti11 mutant was completely resistant to TuMV infection. We conclude that TuMV replication vesicles bypass the Golgi apparatus and take an unconventional pathway that may involve prevacuolar compartments/multivesicular bodies for virus infection.
Databáze: OpenAIRE