Identification of interacting proteins of maize mosaic virus glycoprotein in its vector, Peregrinus maidis.
Rhabdovirus glycoproteins (G) serve multifunctional roles in virus entry, assembly, and exit from animal cells. We hypothesize that maize mosaic virus (MMV) G is required for invasion, infection, and spread in Peregrinus maidis, the planthopper vector. Using a membrane-based yeast two-hybrid assay, we identified 125 P. maidis proteins that physically interacted with MMV G, of which 68% matched proteins with known functions in endocytosis, vesicle-mediated transport, protein synthesis and turnover, nuclear import/export, metabolism and host defense. Physical interaction networks among conserved proteins indicated a possible cellular coordination of processes associated with MMV G translation, protein folding and trafficking. Non-annotated proteins contained predicted functional sites, including a diverse array of ligand binding sites. Cyclophilin A and apolipophorin III co-immunoprecipitated with MMV G, and each showed different patterns of co-localization with G in insect cells. This study describes the first protein interactome for a rhabdovirus spike protein and insect vector.