Association of the Tobacco mosaic virus 126kDa replication protein with a GDI protein affects host susceptibility.

An interaction between the Tobacco mosaic virus (TMV) 126kDa replication protein and a host-encoded Rab GDP dissociation inhibitor (GDI2) was identified and investigated for its role in infection. GDI proteins are essential components of vesicle trafficking pathways. TMV infection alters the localization of GDI2 from the cytoplasm to ER-associated complexes. Partial silencing of GDI2 results in significant increases in the number of TMV infection foci observed in inoculated tissues. However, GDI2 silencing does not affect TMV accumulation at the infection site, cell-to-cell movement, or susceptibility of the host to mechanical inoculation. Furthermore, increases in the number of successful infection foci were specific to TMV and correlated with the appearance of vesicle-like rearrangements in the vacuolar membrane. Tissue infiltrations with brefeldin A, an inhibitor of vesicle trafficking, also enhanced host susceptibility to TMV. Combined these findings suggest that the 126kDa-GDI2 interaction alters vesicle trafficking to enhance the establishment of an infection.