| Autor: |
DeBlasio SL; Emerging Pests and Pathogens Research Unit, USDA Agricultural Research Service, Ithaca, New York 14853, United States.; Boyce Thompson Institute for Plant Research, Ithaca, New York 14853, United States., Wilson JR; Boyce Thompson Institute for Plant Research, Ithaca, New York 14853, United States.; Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, New York 14853, United States., Tamborindeguy C; Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, New York 14853, United States., Johnson RS; Department of Genome Sciences, University of Washington, Seattle, Washington 98109, United States., Pinheiro PV; Boyce Thompson Institute for Plant Research, Ithaca, New York 14853, United States.; Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, New York 14853, United States., MacCoss MJ; Department of Genome Sciences, University of Washington, Seattle, Washington 98109, United States., Gray SM; Emerging Pests and Pathogens Research Unit, USDA Agricultural Research Service, Ithaca, New York 14853, United States.; Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, New York 14853, United States., Heck M; Emerging Pests and Pathogens Research Unit, USDA Agricultural Research Service, Ithaca, New York 14853, United States.; Boyce Thompson Institute for Plant Research, Ithaca, New York 14853, United States.; Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, New York 14853, United States. |
| Abstrakt: |
The vast majority of plant viruses are transmitted by insect vectors, with many crucial aspects of the transmission process being mediated by key protein-protein interactions. Still, very few vector proteins interacting with viruses have been identified and functionally characterized. Potato leafroll virus (PLRV) is transmitted most efficiently by Myzus persicae , the green peach aphid, in a circulative, non-propagative manner. Using affinity purification coupled to high-resolution mass spectrometry (AP-MS), we identified 11 proteins from M. persicae displaying a high probability of interaction with PLRV and an additional 23 vector proteins with medium confidence interaction scores. Three of these aphid proteins were confirmed to directly interact with the structural proteins of PLRV and other luteovirid species via yeast two-hybrid. Immunolocalization of one of these direct PLRV-interacting proteins, an orthologue of the human innate immunity protein complement component 1 Q subcomponent-binding protein (C1QBP), shows that MpC1QBP partially co-localizes with PLRV in cytoplasmic puncta and along the periphery of aphid gut epithelial cells. Artificial diet delivery to aphids of a chemical inhibitor of C1QBP leads to increased PLRV acquisition by aphids and subsequently increased titer in inoculated plants, supporting a role for C1QBP in the acquisition and transmission efficiency of PLRV by M. persicae . This study presents the first use of AP-MS for the in vivo isolation of a functionally relevant insect vector-virus protein complex. MS data are available from ProteomeXchange.org using the project identifier PXD022167. |
