Identification of interacting proteins of maize mosaic virus glycoprotein in its vector, Peregrinus maidis.

Alviar, K. B.; Rotenberg, D.; Martin, K. M.; Whitfield, A. E.

doi:10.1101/2022.02.01.478665

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bioRxiv · 10.1101/2022.02.01.478665

Identification of interacting proteins of maize mosaic virus glycoprotein in its vector, Peregrinus maidis.

Alviar, K. B.·Rotenberg, D.·Martin, K. M.·Whitfield, A. E.

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Abstract

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.

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Alviar, K. B., Rotenberg, D., Martin, K. M., Whitfield, A. E.. 2022-02-01. Identification of interacting proteins of maize mosaic virus glycoprotein in its vector, Peregrinus maidis.. https://doi.org/10.1101/2022.02.01.478665

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