The physical interactome between Peregrinus maidis proteins and the maize mosaic virus glycoprotein provides insights into the cellular biology of a rhabdovirus in the insect vector.

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 107 P. maidis proteins that physically interacted with MMV G, of which approximately 53% matched proteins with known functions including endocytosis, vesicle-mediated transport, protein synthesis and turnover, nuclear 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 localization with G in insect cells. This study describes the first protein interactome for a rhabdovirus spike protein and insect vector. • Rhabdovirus glycoproteins (G) serve multifunctional roles in virus entry, assembly, and exit. • An MbY2H screen identified 107 Peregrinus maidis proteins that interact with maize mosaic virus G. • Proteins involved in endocytosis, vesicle-mediated transport, nuclear export, and host defense interacted with MMV G. • CypA and ApoLpIII co-immunoprecipitated with MMV G and showed patterns of localization with G in insect cells. • This study describes the first protein interactome for a rhabdovirus spike protein and insect vector. [ABSTRACT FROM AUTHOR]