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

Proteomics
Stacy L DeBlasioMichelle Cilia

Abstract

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 d...Continue Reading

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Citations

Dec 15, 2015·Advanced Drug Delivery Reviews·Svenja HindererKatja Schenke-Layland
Apr 1, 2015·Virology·Anna E WhitfieldDorith Rotenberg
Oct 21, 2016·Journal of Proteome Research·Stacy L DeBlasioMichelle Cilia
Nov 22, 2016·Viruses·Juliette DoumayrouW Allen Miller
Dec 21, 2016·Molecular Plant Pathology·Claire Bendix, Jennifer D Lewis
May 27, 2020·Annual Review of Virology·Madhu KappagantuJames N Culver
Feb 25, 2018·Current Opinion in Plant Biology·Svetlana Y Folimonova, Jens Tilsner
Jun 9, 2021·Current Opinion in Plant Biology·James M ElmoreJustin W Walley
Aug 14, 2020·Journal of Proteome Research·Michelle Heck, Benjamin A Neely

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