Double-stranded RNA of Rice Gall Dwarf Virus

Hibi, Tadaaki; Omura, Toshihiro; Saito, Yasuo

doi:10.1099/0022-1317-65-9-1585

Cited by 14 publications

(6 citation statements)

References 12 publications

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“…RGDV is thought to be a Phytoreovirus , a suggestion supported by the finding that the genome of RGDV consists of 12 segments of double-stranded RNA (Hibi et al, 1984).…”

Section: Introductionmentioning

confidence: 75%

Location of Structural Proteins in Particles of Rice Gall Dwarf Virus

Omura¹,

Minobe

Matsuoka

et al. 1985

Journal of General Virology

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SUMMARYProtein from particles of rice gall dwarf virus was resolved into seven components by polyacrylamide gel electrophoresis. The estimated molecular weights ( × 103) were 183, 165, 150, 143, 120, 56 and 45 (K). Cores prepared by treating intact particles with CsC1 contained the 183K, 165K, 120K and 56K proteins: the 150K, 143K and 45K proteins were recovered from the top layer of gradients after CsC1 equilibrium centrifugation. Antiserum against intact particles reacted mainly with 150K and 45K proteins and antiserum against core particles reacted mainly with 183K and 120K proteins. The results suggest that the 150K and 45K proteins are located on the surface of the outer capsid, that the 183K and 120K proteins are on the surface of the core, that the 165K and 56K proteins are inside the core, and that the 143K protein is either inside the outer capsid or inside the core.

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“…RGDV is thought to be a Phytoreovirus , a suggestion supported by the finding that the genome of RGDV consists of 12 segments of double-stranded RNA (Hibi et al, 1984).…”

Section: Introductionmentioning

confidence: 75%

Location of Structural Proteins in Particles of Rice Gall Dwarf Virus

Omura¹,

Minobe

Matsuoka

et al. 1985

Journal of General Virology

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“…Both viruses multiply in their insect vectors, in which they cause no apparent symptoms, as well as in their plant hosts, in which they induce severe growth abnormalities, including dwarfing. In morphology and architecture of virions, RGDV and RDV, as well as Wound tumor virus (WTV) (the type member of the genus Phytoreovirus), have angular spikeless icosahedral double-shelled particles approximately 65-70 nm in diameter and contain 12 segments of double-stranded RNA (dsRNA) [7,8] and at least six structural proteins including four core structural proteins and two outer capsid proteins [9,10]. The two rice viruses are also similar in the molecular sizes and the molar ratios of their structural proteins; interestingly, the double-shelled viruslike particles, which are indistinguishable by electron microscope from native RDV and RGDV virions, are reassembled successfully with heterogenous core and outer capsid proteins of RGDV and RDV [11,12].…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of the largest and smallest genome segments, S1 and S12, of Rice gall dwarf virus

et al. 2007

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The nucleotide sequences of segments S1 and S12 of a Chinese isolate of Rice gall dwarf virus (RGDV) were determined. This provides the first complete sequences of these segments. The complete sequence of S1, the largest genome segment of RGDV, was 4,505 nucleotides in length and was predicted to encode a large protein of 1,458 amino acids with a calculated molecular mass of nearly 166.2 kDa. The protein was related to that encoded by S1 of Rice dwarf virus (RDV; 50% identity and 67% similarity) and (to a lesser extent) to some large proteins of other reoviruses. It appears to be an RNA-dependent RNA polymerase (RdRp) and is probably present in particles as a minor core protein. S12, the smallest genome segment of RGDV, was 853 nucleotides in length, encoding a single major protein of 206 amino acids with a calculated molecular mass of nearly 23.6 kDa. This protein, though a little larger than those of RDV S11 and Wound tumor virus (WTV) S12 in size, showed some similarity to them, especially in the conserved N-terminal region and may have RNA-binding properties. Despite having a common host plant, RDV and RGDV were not more closely related to one another than either of them was to WTV. Phylogenetic analysis of the RdRp showed that members of the genus Phytoreovirus were more closely related to those of the genus Rotavirus than to any other genus within the family Reoviridae.

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“…RGDV is transmitted propagatively to rice plants by leafhoppers (Morinaka et al , 1982). RGDV has a double-shelled, icosahedral capsid of approximately 65–70 nm in diameter (Omura et al , 1982) and contains 12 segments of dsRNA (S1–S12 in order of their mobility during SDS-PAGE; Hibi et al , 1984). S1, S2, S3, S5, S6 and S8 encode the structural proteins P1, P2, P3, P5, P6 and P8, respectively (Boccardo et al , 1985; Hibi et al , 1984).…”

Section: Introductionmentioning

confidence: 99%

Viroplasm matrix protein Pns9 from rice gall dwarf virus forms an octameric cylindrical structure

Akita

Miyazaki

Hibino

et al. 2011

Journal of General Virology

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The non-structural Pns9 protein of rice gall dwarf virus (RGDV) accumulates in viroplasm inclusions, which are structures that appear to play an important role in viral morphogenesis and are commonly found in host cells infected by viruses in the family Reoviridae. Immunofluorescence and immunoelectron microscopy of RGDV-infected vector cells in monolayers, using antibodies against Pns9 of RGDV and expression of Pns9 in Spodoptera frugiperda cells, demonstrated that Pns9 is the minimal viral factor necessary for formation of viroplasm inclusion during infection by RGDV. When Pns9 in solution was observed under a conventional electron microscope, it appeared as ring-like aggregates of approximately 100 Å in diameter. Cryo-electron microscopic analysis of these aggregates revealed cylinders of octameric Pns9, whose dimensions were similar to those observed under the conventional electron microscope. Octamerization of Pns9 in solution was confirmed by the results of size-exclusion chromatography. Among proteins of viruses that belong to the family Reoviridae whose three-dimensional structures are available, a matrix protein of the viroplasm of rotavirus, NSP2, forms similar octamers, an observation that suggests similar roles for Pns9 and NSP2 in morphogenesis in animal-infecting and in plantinfecting reoviruses. INTRODUCTION Rice gall dwarf virus (RGDV) is a member of the genusPhytoreovirus in the family Reoviridae , and multiplies in both plants and invertebrate insect vectors. RGDV is transmitted propagatively to rice plants by leafhoppers (Morinaka et al., 1982). RGDV has a doubleshelled, icosahedral capsid of approximately 65-70 nm in diameter and contains 12 segments of dsRNA (S1-S12 in order of their mobility during SDS-PAGE; Hibi et al., 1984). S1, S2, S3, S5, S6 and S8 encode the structural proteins P1, P2, P3, P5, P6 and P8, respectively (Boccardo et al., 1985;Hibi et al., 1984). The core capsid is composed of P3, the major protein, which encloses P1, P5 and P6 (Ichimi et al., 2002;Omura et al., 1985). The outer capsid of the virus is composed of the P2 protein (Yan et al., 1996) and the major outer-capsid protein P8 (Noda et al., 1991). The other segments of dsRNA encode putative nonstructural (Pns) proteins, namely Pns4, Pns7, Pns9, Pns10, Pns11 and Pns12 (Koganezawa et al., 1990;Moriyasu et al., 2000Moriyasu et al., , 2007Noda et al., 1991). The functions of Pns4, Pns10 and Pns11 are unknown. Pns7 and Pns12 are components of the viroplasm (Wei et al., 2009). The segment S9 encoding Pns9 is 1202 nt and contains a single ORF encoding a protein of 323 aa with a molecular mass of 35.6 kDa (Koganezawa et al., 1990). The deduced amino acid sequence of this protein is only 16 % identical to that of the non-structural protein Pns12 of rice dwarf virus (RDV; Moriyasu et al., 2007), which is a major component of the RDV viroplasm, in which viral particles are assembled (Wei et al., 2006).In the present study, we have shown that Pns9 of RGDV is one of the component proteins of viroplasm-like inclusions on the ba...

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Double-stranded RNA of Rice Gall Dwarf Virus

Cited by 14 publications

References 12 publications

Location of Structural Proteins in Particles of Rice Gall Dwarf Virus

Location of Structural Proteins in Particles of Rice Gall Dwarf Virus

Molecular characterization of the largest and smallest genome segments, S1 and S12, of Rice gall dwarf virus

Viroplasm matrix protein Pns9 from rice gall dwarf virus forms an octameric cylindrical structure

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