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Host protein interaction network associated with the non-incorporated form of the potato leafroll virus RTP identified using mass spectrometry
Stacy DeBlasio: USDA-ARS; Ana Rita Rebelo: Boyce Thompson Institute; Richard Johnson: Department of Genome Sciences, University of Washington; Stewart Gray: USDA-ARS; Stewart Gray: Department of Plant Pathology and Plant-Microbe Biology, Cornell University; Michael MacCoss: Department of Genomics Sciences, University of Washington; Michelle Cilia: Department of Plant Pathology and Plant-Microbe Biology, Cornell University; Michelle Cilia: USDA-ARS; Michelle Cilia: Boyce Thompson Institute
<div><i>Potato leafroll virus</i> (PLRV) is an aphid-transmitted plant virus in the family <i>Luteoviridae</i> that infects solanaceous crops<i>.</i> Its +ssRNA genome is protected by an icosahedral-shaped virion composed of 180 subunits of coat protein (CP), the major capsid component. Sporadic, translational readthrough of a stop codon at the end of the CP gene produces a readthrough protein (RTP), which exists as two forms, a minor structural protein that is incorporated into virions to regulate systemic movement and transmission, and a non-incorporated form, which restricts virus movement to the phloem. We used affinity-purification mass spectrometry coupled to reverse genetics using viral mutants to identify protein-protein interactions among virus and host proteins that are specific to virions from those that interact with the non-incorporated form of the RTP. By quantifying differences in the protein interaction networks of wild type PLRV and a mutant where the CP stop codon has been deleted, we have evidence showing that the non-incorporated RTP forms complexes with a distinct class of host proteins, viral RNA and several nonstructural viral proteins including P3a, a newly discovered PLRV protein involved in systemic movement. Our analysis has also revealed a class of plant proteins involved in vesicle trafficking whose interaction with PLRV is dependent on virion assembly. Characterization of the function of these host proteins in the context of a PLRV infection is ongoing.</div>

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