The Interaction Dynamics of Two Potato Leafroll Virus Movement Proteins Affects Their Localization to the Outer Membranes of Mitochondria and Plastids

Viruses

AnaRita Rebelo¹  MichaelJ. MacCoss²  RichardS. Johnson²  Yi Xu³  StacyL. DeBlasio⁴  StewartM. Gray⁴  Michelle Heck⁴ 

[1] Boyce Thompson Institute for Plant Research, Ithaca, NY 14853, USA;Department of Genome Sciences, University of Washington, Seattle WA 98109, USA;Section of Plant Pathology and Plant-Microbe Biology, School of Integrated Plant Science, Cornell University, Ithaca, NY 14853, USA;United States Department of Agriculture, Biological Integrated Pest Management Research Unit, Robert W. Holley Center for Agriculture and Health, 538 Tower Road, Ithaca, NY 14853, USA;

关键词: Potato leafroll virus;    plant pathogen;    phloem-limited;    movement protein;    viral trafficking;    Luteoviridae;    polerovirus;    insect-borne;    endomembrane system;   

DOI  :  10.3390/v10110585

来源: DOAJ

【 摘 要 】

The Luteoviridae is an agriculturally important family of viruses whose replication and transport are restricted to plant phloem. Their genomes encode for four proteins that regulate viral movement. These include two structural proteins that make up the capsid and two non-structural proteins known as P3a and P17. Little is known about how these proteins interact with each other and the host to coordinate virus movement within and between cells. We used quantitative, affinity purification-mass spectrometry to show that the P3a protein of Potato leafroll virus complexes with virus and that this interaction is partially dependent on P17. Bimolecular complementation assays (BiFC) were used to validate that P3a and P17 self-interact as well as directly interact with each other. Co-localization with fluorescent-based organelle markers demonstrates that P3a directs P17 to the mitochondrial outer membrane while P17 regulates the localization of the P3a-P17 heterodimer to plastids. Residues in the C-terminus of P3a were shown to regulate P3a association with host mitochondria by using mutational analysis and also varying BiFC tag orientation. Collectively, our work reveals that the PLRV movement proteins play a game of intracellular hopscotch along host organelles to transport the virus to the cell periphery.

【 授权许可】

Unknown