PLRV co-immunoprecipitation from Solanum tuberosum

ABSTRACT: Phloem localization of plant viruses is advantageous for acquisition by sap-sucking vectors but hampers host-virus protein interaction studies. In this study, Potato leafroll virus (PLRV)-host protein complexes were isolated from systemically infected potato, a natural host of the virus. Comparing two different co-immunoprecipitation support matrices coupled to mass spectrometry, we identified 44 potato proteins and one viral protein (P1) specifically associated with virus isolated from infected phloem. An additional 142 proteins interact in complex with virus at varying degrees of confidence. Greater than 80% of these proteins were previously found to form high confidence interactions with PLRV isolated from the model host Nicotiana benthamiana. Bioinformatics revealed that these proteins are enriched for functions related to plasmodesmata, organelle membrane transport, translation and mRNA processing. Our results show that model system proteomics experiments are extremely valuable for understanding protein interactions regulating infection in recalcitrant pathogens such as phloem-limited viruses.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Solanum Tuberosum (potato)

TISSUE(S): Leaf

SUBMITTER: Stacy DeBlasio  

LAB HEAD: Michelle Cilia

PROVIDER: PXD004814 | Pride | 2016-12-14

REPOSITORIES: Pride