Location: Crop Diseases, Pests and Genetics Research
Title: Proteomic analysis of plant interactors with the RNA silencing suppressor V2 from Croton yellow vein mosaic virusAuthor
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Zhai, Ying |
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Peng, Hao |
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GNANASEKARAN, PRABU - Washington State University |
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ROY, ANIRBAN - Indian Agricultural Research Institute |
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PAPPU, HANU - Washington State University |
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Submitted to: Virology
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 12/5/2025 Publication Date: 12/10/2025 Citation: Zhai, Y., Peng, H., Gnanasekaran, P., Roy, A., Pappu, H.R. 2025. Proteomic analysis of plant interactors with the RNA silencing suppressor V2 from Croton yellow vein mosaic virus. Virology. 615:110773. https://doi.org/10.1016/j.virol.2025.110773. DOI: https://doi.org/10.1016/j.virol.2025.110773 Interpretive Summary: Croton yellow vein mosaic virus (CYVMV) is one of the most devastating viral diseases in the Indian subcontinent. CYVMV infects many vegetables, ornamentals, and weeds, and was transmitted by whiteflies. CYVMV infection causes typical symptoms of yellow vein mosaic in Croton and leaf curling in other plant species. Our previous study reported that V2 gene of CYVMV is critical for disease resistance. In this study, we identified twenty-three putative proteins in N. benthamiana can interacted with V2 protein via affinity purification-mass spectrometry (AP-MS). Particularly, two N. benthamiana proteins, receptor for activated C kinase 1 (NbRACK1) and Ankyrin repeat domain containing protein (NbANK), were verified to interact with V2 via both yeast two-hybrid (Y2H) and bimolecular fluorescence complementation (BiFC). Technical Abstract: Croton yellow vein mosaic virus (CYVMV) is a begomovirus infecting a wide range of vegetables, ornamentals, and weeds. The monopartite CYVMV genome consists of a single-stranded circular DNA (DNA-A) plus a betasatellite called CroYVMB (DNA-ß). DNA-A and DNA-ß encode four RNA silencing suppressors of V2/C2/C4 and ßC1, respectively. Among them, V2 interacts itself and the CYVMV V1 protein, and is critical for CYVMV virulence. However, little is known about the molecular mechanism of how V2 suppresses plant RNA silencing machinery and defense system. Here, we identified twenty-three putative V2-interacting proteins in N. benthamiana via affinity purification-mass spectrometry (AP-MS) and performed gene ontology (GO) analysis on these V2-Interacting candidates. In particular, two N. benthamiana proteins, Receptor for activated C kinase 1 (NbRACK1) and Ankyrin repeat domain containing protein (NbANK), were verified to physically interact with V2 via both yeast two-hybrid (Y2H) and bimolecular fluorescence complementation (BiFC). |
