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Proteomics. 2015 Jun;15(12):2098-112. doi: 10.1002/pmic.201400594. Epub 2015 Apr 29.

Potato leafroll virus structural proteins manipulate overlapping, yet distinct protein interaction networks during infection.

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Boyce Thompson Institute for Plant Research, Ithaca, NY, USA.
USDA-Agricultural Research Service, Ithaca, NY, USA.
Department of Genome Sciences, University of Washington, Seattle, WA, USA.
Department of Plant, Soil and Entomological Sciences, University of Idaho, Moscow, ID, USA.
Department of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY, USA.


Potato leafroll virus (PLRV) produces a readthrough protein (RTP) via translational readthrough of the coat protein amber stop codon. The RTP functions as a structural component of the virion and as a nonincorporated protein in concert with numerous insect and plant proteins to regulate virus movement/transmission and tissue tropism. Affinity purification coupled to quantitative MS was used to generate protein interaction networks for a PLRV mutant that is unable to produce the read through domain (RTD) and compared to the known wild-type PLRV protein interaction network. By quantifying differences in the protein interaction networks, we identified four distinct classes of PLRV-plant interactions: those plant and nonstructural viral proteins interacting with assembled coat protein (category I); plant proteins in complex with both coat protein and RTD (category II); plant proteins in complex with the RTD (category III); and plant proteins that had higher affinity for virions lacking the RTD (category IV). Proteins identified as interacting with the RTD are potential candidates for regulating viral processes that are mediated by the RTP such as phloem retention and systemic movement and can potentially be useful targets for the development of strategies to prevent infection and/or viral transmission of Luteoviridae species that infect important crop species.


Affinity purification MS; Luteoviridae, Polerovirus; Plant proteomics; Potato leafroll virus; Readthrough protein

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