The V2 Protein from the Geminivirus Tomato Yellow Leaf Curl Virus Largely Associates to the Endoplasmic Reticulum and Promotes the Accumulation of the Viral C4 Protein in a Silencing Suppression-Independent Manner

• Published in: Viruses 2022-12, Vol.14 (12), p.2804
• Main Authors: Wang, Liping, Fan, Pengfei, Jimenez-Gongora, Tamara, Zhang, Dan, Ding, Xue, Medina-Puche, Laura, Lozano-Durán, Rosa
• Format: Article
• Language: English
• Subjects: Antibiotics; Begomovirus - genetics; Begomovirus - metabolism; C4 protein; Cloning; Communication; Endoplasmic reticulum; endoplasmic reticulum (ER); Endoplasmic Reticulum - metabolism; ERQC; Geminiviridae - genetics; Geminiviridae - metabolism; geminivirus; Gene expression; Gene silencing; Genomes; Infections; Kinases; Leaf-curl; Localization; Nicotiana; Physiological aspects; Plant Diseases; Plant virus diseases; Plant viruses; Plasmids; Post-transcription; Proteins; Quality control; RNA-mediated interference; tomato yellow leaf curl virus (TYLCV); Viral infections; Viral proteins; Viral Proteins - metabolism; virus; Virus diseases of plants; Virus research; Viruses; Yellow leaf
• ISSN: 1999-4915; 1999-4915
• DOI: 10.3390/v14122804

Viruses are strict intracellular parasites that rely on the proteins encoded in their genomes for the effective manipulation of the infected cell that ultimately enables a successful infection. Viral proteins have to be produced during the cell invasion and takeover in sufficient amounts and in a timely manner. Silencing suppressor proteins evolved by plant viruses can boost the production of viral proteins; although, additional mechanisms for the regulation of viral protein production likely exist. The strongest silencing suppressor encoded by the geminivirus tomato yellow leaf curl virus (TYLCV) is V2: V2 suppresses both post-transcriptional and transcriptional gene silencing (PTGS and TGS), activities that are associated with its localization in punctate cytoplasmic structures and in the nucleus, respectively. However, V2 has been previously described to largely localize in the endoplasmic reticulum (ER), although the biological relevance of this distribution remains mysterious. Here, we confirm the association of V2 to the ER in and assess the silencing suppression activity-independent impact of V2 on protein accumulation. Our results indicate that V2 has no obvious influence on the localization of ER-synthesized receptor-like kinases (RLKs) or ER quality control (ERQC)/ER-associated degradation (ERAD), but dramatically enhances the accumulation of the viral C4 protein, which is co-translationally myristoylated, possibly in proximity to the ER. By using the previously described V2 mutant, in which the silencing suppression activity is abolished, we uncouple RNA silencing from the observed effect. Therefore, this work uncovers a novel function of V2, independent of its capacity to suppress silencing, in the promotion of the accumulation of another crucial viral protein.