The complete nucleotide sequence of the rice grassy stunt virus genome and genomic comparisons with viruses of the genus Tenuivirus.

Toriyama, Shigemitsu; Kimishima, Takao; Takahashi, M.; Shimizu, Takumi; Minaka, Nobuhiro; Akutsu, Katsumi

doi:10.1099/0022-1317-79-8-2051

Cited by 44 publications

(25 citation statements)

References 28 publications

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“…The p5-p5 interaction was reproduced in an Sos recruitment-mediated yeast two-hybrid system as well in by far-Western blots. Native p5 protein extracted from RGSV-infected rice tissue was detected in a large complex with a molecular mass of approximately 260 kDa composed of 12 molecules of p5 or a p5 oligomer with an unidentified host factor(s).The genome of Rice grassy stunt tenuivirus (RGSV), a member in the genus Tenuivirus (12) and an important rice pathogen in East, Southeast, and South Asian countries (8), consists of six ambisense RNA segments containing a total of 12 open reading frames (ORFs) (13,16,17). RGSV replicates and is transmitted by a brown planthopper (Nilaparvata lugens Stal) (9).…”

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confidence: 99%

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Detection of rice grassy stunt tenuivirus nonstructural proteins p2, p5 and p6 from infected rice plants and from viruliferous brown planthoppers

Chomchan

Miranda

Shirako

2002

Archives of Virology

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We investigated the interaction of Rice grassy stunt tenuivirus (RGSV) nonstructural protein p5, a protein of 22 kDa encoded on vRNA 5, with all 12 RGSV proteins by using a GAL4 transcription activator-based yeast two-hybrid system. The p5 protein interacted only with itself and not with any other viral protein; the interacting domains were localized within the N-terminal 96 amino acids of p5. The p5-p5 interaction was reproduced in an Sos recruitment-mediated yeast two-hybrid system as well in by far-Western blots. Native p5 protein extracted from RGSV-infected rice tissue was detected in a large complex with a molecular mass of approximately 260 kDa composed of 12 molecules of p5 or a p5 oligomer with an unidentified host factor(s).The genome of Rice grassy stunt tenuivirus (RGSV), a member in the genus Tenuivirus (12) and an important rice pathogen in East, Southeast, and South Asian countries (8), consists of six ambisense RNA segments containing a total of 12 open reading frames (ORFs) (13,16,17). RGSV replicates and is transmitted by a brown planthopper (Nilaparvata lugens Stal) (9). So far, little has been known about the functions of the individual RGSV proteins, except for the 339-kDa RNA-dependent RNA polymerase (RdRp) encoded on the complementary strand of RNA 1 (cRNA 1) and the 36-kDa nucleocapsid protein (N) encoded on cRNA 5 ( Fig. 1), both of which are found along with genomic and possibly complementary RNAs as thin filamentous ribonucleoprotein (RNP) particles. Recently, we showed that the 22-kDa p5 protein encoded on the virus genomic strand of RNA 5 (vRNA 5) accumulates in large amounts in both RGSV-infected rice leaves and viruliferous brown planthoppers, while the 23-kDa p2 protein encoded on vRNA 2 and the 21-kDa p6 protein encoded on vRNA 6 were preferentially expressed in infected rice leaf tissues rather than in viruliferous insects (5). We hypothesized that p5 has an essential role in virus infection in both the plant and insect hosts (5).In this study, we investigated possible interactions between the p5 protein and the other RGSV proteins by using a GAL4 transcription activator-based yeast two-hybrid system (4, 6). We found that p5 interacts with itself through domains located in the N-terminal half of the protein, but does not interact with any other RGSV protein with this yeast two-hybrid system. The p5-p5 interaction was confirmed by an Sos recruitment-mediated yeast two-hybrid system (1, 2) as well as by far-Western blots, indicating that the strength of the p5-p5 interaction is significant and suggesting that the interaction is biologically significant as well. p5-p5 interaction in the N-terminal region detected by a GAL4 transcription activator-based yeast two-hybrid system.Interactions between the p5 protein and all 12 RGSV proteins were examined by using a yeast two-hybrid system based on the GAL4 transcription activator (4, 6) (MatchMaker 2; Clontech). In this system, the yeast GAL4 transcription activator has been separated into two functional domains: (i) the DNA binding act...

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confidence: 99%

“…The genome of Rice grassy stunt tenuivirus (RGSV), a member in the genus Tenuivirus (12) and an important rice pathogen in East, Southeast, and South Asian countries (8), consists of six ambisense RNA segments containing a total of 12 open reading frames (ORFs) (13,16,17). RGSV replicates and is transmitted by a brown planthopper (Nilaparvata lugens Stal) (9).…”

mentioning

confidence: 99%

Detection of rice grassy stunt tenuivirus nonstructural proteins p2, p5 and p6 from infected rice plants and from viruliferous brown planthoppers

Chomchan

Miranda

Shirako

2002

Archives of Virology

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“…Phylogenetic analysis of the nucleocapsid protein and the 94-kDa virion membrane-glycoprotein-like protein of RGSV, RSV, MStV and RHBV showed that RGSV is a monophyletic group that is set apart from the other members of the genus Tenuivirus [24]. Early studies demonstrated that the properties of the RGSV were probably different from those of other members of the genus Tenuivirus.…”

Section: Discussionmentioning

confidence: 98%

“…The functions of three RGSV-encoded proteins are known. The protein pC1 (339.1-kDa), encoded on RNA 1 in the viral complementary sense (vcRNA1), may function as an RNA-dependent RNA polymerase (RdRp) and is similar to the RdRp of RSV, with 37 ± 9 % amino acid sequence identity over 2140 amino acid residues [23,24]. The protein pC5 (35.9 kDa), encoded by vcRNA5, is the nucleocapsid protein (N) and accumulates in both RGSVinfected rice and viruliferous brown planthoppers [3].…”

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Rice grassy stunt virus nonstructural protein p5 serves as a viral suppressor of RNA silencing and interacts with nonstructural protein p3

Zhang

Liu

et al. 2015

Arch Virol

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Rice grassy stunt virus (RGSV), a member of the genus Tenuivirus, causes serious rice disease in Southeast Asian countries. In this study, a green fluorescent protein (GFP)-based transient expression assay was conducted to show that p5, encoded on RNA5 in the viral sense, is a viral suppressor of RNA silencing (VSR). Protein-protein interactions (PPIs) between p5 and all RGSV proteins except pC1 and pC2 were investigated using Gal4-based yeast two-hybrid (Y2H) experiments. The results demonstrated that p5 interacts with itself and with p3 encoded on RNA3 in the viral sense. p5-p5 and p5-p3 interactions were detected by bimolecular fluorescence complementation (BiFC) assay, and the p5-p3 interaction was confirmed by subcellular co-localization and co-immunoprecipitation (Co-IP) assays. Using the Y2H system, we demonstrated that the p5-p3 interaction requires both the N-terminal (amino acid residues 1 to 99) and C-terminal (amino acid residues 94 to 191) domains of p5. In addition, either p5 or p3 could enhance the pathogenicity of potato virus X (PVX) in Nicotiana benthamiana plants. A much more significant enhancement of PVX pathogenicity and accumulation was observed when p5 and p3 were expressed together. Our data also showed that RGSV p3 does not function as a VSR, and it had no effect on the VSR activity of p5 or the subcellular localization pattern of p5 in plant cells from Nicotiana benthamiana.

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Oryza sativa (Rice)

Sasaki

2001

Encyclopedia of Genetics

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The complete nucleotide sequence of the rice grassy stunt virus genome and genomic comparisons with viruses of the genus Tenuivirus.

Cited by 44 publications

References 28 publications

Detection of rice grassy stunt tenuivirus nonstructural proteins p2, p5 and p6 from infected rice plants and from viruliferous brown planthoppers

Detection of rice grassy stunt tenuivirus nonstructural proteins p2, p5 and p6 from infected rice plants and from viruliferous brown planthoppers

Rice grassy stunt virus nonstructural protein p5 serves as a viral suppressor of RNA silencing and interacts with nonstructural protein p3

Oryza sativa (Rice)

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