Affinity Purification–Mass Spectrometry Identifies a Novel Interaction between a Polerovirus and a Conserved Innate Immunity Aphid Protein that Regulates Transmission Efficiency

The vast majority of plant viruses are transmitted by insect vectors, with many crucial aspects the transmission process being mediated key protein–protein interactions. Still, very few vector proteins interacting have been identified and functionally characterized. Potato leafroll virus (PLRV) is most efficiently Myzus persicae, green peach aphid, in a circulative, non-propagative manner. Using affinity purification coupled to high-resolution mass spectrometry (AP–MS), we 11 from M. persicaedisplaying high probability interaction PLRV an additional 23 medium confidence scores. Three these aphid were confirmed directly interact structural other luteovirid species via yeast two-hybrid. Immunolocalization one direct PLRV-interacting proteins, orthologue human innate immunity protein complement component 1 Q subcomponent-binding (C1QBP), shows that MpC1QBP partially co-localizes cytoplasmic puncta along periphery gut epithelial cells. Artificial diet delivery aphids chemical inhibitor C1QBP leads increased acquisition subsequently titer inoculated plants, supporting role for efficiency persicae. This study presents first use AP–MS vivo isolation relevant vector–virus complex. MS data available ProteomeXchange.org using project identifier PXD022167.