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Functional variation in cognate proteins of nucleotrophic negative-strand RNA viruses of plants
Michael Goodin: University of Kentucky
<div>Rhabdoviruses infect a wide range of hosts, and members of this group include viruses that infect humans, terrestrial animals/vertebrates, fish, arthropods, and plants. The genomes of the plant-adapted viruses are organized generally into seven open reading frames with the gene order 3’-N-X-P-Y-M-G-L-5’, which encodes the nucleocapsid, phospho, movement, matrix, glyco, and RNA-dependent RNA polymerase proteins, respectively, except for X, which is of unknown function. In addition to its structural role in virion formation, the M protein of <i>Potato yellow dwarf virus </i>(PYDV) is capable of inducing the intranuclear accumulation of the inner nuclear membranes (INM) in transfected cells. The M protein also interacts with the nuclear import and export receptors Importin-alpha and Exportin 1, suggesting a role for M in transport of condensed nucleocapsids from the nucleus. Interestingly, the ability to remodel the INM is conferred by the P, but not M, protein of coffee ringspot dichorhavirus, demonstrating that functional domains within rhabdoviral proteins are portable. This variation likely contributes to the finding that protein interaction and localization maps (PILMs) for each virus are unique. How these variations in protein sequence contribute to the manner by which these viruses remodel the architecture of plant nuclei will be discussed. <i></i></div>

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