title: A mitochondrial membrane protein is a target for rice ragged stunt virus in its insect vector.
abstract: Rice ragged stunt virus (RRSV; Reoviridae) is exclusively transmitted by the brown planthopper Nilaparvata lugens in a persistent-propagative manner. It is understood that RNA viral proliferation is associated with the intracellular membranes of the insect host cells. However, the molecular mechanisms of the interaction between the RRSV proliferation and the intracellular membranes remain essentially unknown. It will be of great interest to determine whether RRSV protein(s) directly interact with intracellular membrane components of its host cells. In this study, we identified a RRSV nonstructural protein Pns10 interacting with a host oligomycin-sensitivity conferral protein (OSCP) using yeast two-hybrid system. The interaction between RRSV Pns10 and N. lugens OSCP was verified by a glutathione S-transferase pull-down assay. Confocal miscopy revealed colocalization of these two proteins in the cytoplasm of the salivary gland cells during the viral infection. The virions were further detected in the mitochondria under confocal miscopy and transmission electron microscopy combined with western blotting assay. This is the first observation that RRSV protein has a direct link with mitochondria. Suppressing OSCP gene expression by RNA interference notably decreased the viral loads in RRSV-infected insects. These findings revealed novel aspects of a viral protein in targeting the host mitochondrial membrane and provide insights concerning the mitochondrial membrane protein-based virus proliferation mode in the insect vector.
authors.affiliation: State Key Laboratory of Rice Biology and Ministry of Agriculture Key Laboratory of Agricultural Entomology, Institute of Insect Sciences, Zhejiang University, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China.
authors.forename: Hai-Jian
authors.initials: HJ
authors.lastname: Huang
authors.affiliation: State Key Laboratory of Rice Biology and Ministry of Agriculture Key Laboratory of Agricultural Entomology, Institute of Insect Sciences, Zhejiang University, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China.
authors.forename: Cheng-Wen
authors.initials: CW
authors.lastname: Liu
authors.affiliation: State Key Laboratory of Rice Biology and Ministry of Agriculture Key Laboratory of Agricultural Entomology, Institute of Insect Sciences, Zhejiang University, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China.
authors.forename: Xiang
authors.initials: X
authors.lastname: Zhou
authors.affiliation: State Key Laboratory of Rice Biology and Ministry of Agriculture Key Laboratory of Agricultural Entomology, Institute of Insect Sciences, Zhejiang University, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China.
authors.forename: Chuan-Xi
authors.initials: CX
authors.lastname: Zhang
authors.affiliation: State Key Laboratory of Rice Biology and Ministry of Agriculture Key Laboratory of Agricultural Entomology, Institute of Insect Sciences, Zhejiang University, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China. Electronic address: yybao@zju.edu.cn.
authors.forename: Yan-Yuan
authors.initials: YY
authors.lastname: Bao
mesh_terms: D000251:Adenosine Triphosphatases / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D005786:Gene Expression Regulation; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D006430:Hemiptera / Q000145:classification / Q000378:metabolism / Q000648:ultrastructure / Q000821:virology*; D019476:Insect Proteins / Q000235:genetics* / Q000378:metabolism; D007303:Insect Vectors / Q000378:metabolism / Q000648:ultrastructure / Q000821:virology; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism / Q000648:ultrastructure / Q000821:virology*; D025261:Mitochondrial Proton-Translocating ATPases; D012275:Oryza / Q000469:parasitology / Q000821:virology*; D010802:Phylogeny; D010935:Plant Diseases / Q000469:parasitology / Q000821:virology; D011485:Protein Binding; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D012367:RNA, Viral / Q000235:genetics / Q000378:metabolism; D012087:Reoviridae / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D012469:Salivary Glands / Q000378:metabolism / Q000648:ultrastructure / Q000821:virology; D016415:Sequence Alignment; D020798:Two-Hybrid System Techniques; D019562:Viral Load; D017361:Viral Nonstructural Proteins / Q000235:genetics* / Q000378:metabolism; D014771:Virion / Q000235:genetics / Q000254:growth & development / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D019476:Insect Proteins; D008565:Membrane Proteins; D034741:RNA, Small Interfering; D012367:RNA, Viral; C113494:S10 protein, Rice ragged stunt virus; D017361:Viral Nonstructural Proteins; D005982:Glutathione Transferase; D000251:Adenosine Triphosphatases; D025261:Mitochondrial Proton-Translocating ATPases; C020439:oligomycin sensitivity-conferring protein
keywords: Nilaparvata lugens; Oligomycin-sensitivity conferral protein; Pns10; Rice ragged stunt virus; Virus-host protein interaction