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The movement protein encoded by gene 3 of rice transitory yellowing virus is associated with virus particles.
Hiraguri, Akihiro; Hibino, Hiroyuki; Hayashi, Takaharu; Netsu, Osamu; Shimizu, Takumi; Uehara-Ichiki, Tamaki; Omura, Toshihiro; Sasaki, Nobumitsu; Nyunoya, Hiroshi; Sasaya, Takahide.
Afiliación
  • Hiraguri A; National Agricultural Research Center, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-8666, Japan.
  • Hibino H; National Agricultural Research Center, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-8666, Japan.
  • Hayashi T; National Agricultural Research Center, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-8666, Japan.
  • Netsu O; National Agricultural Research Center, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-8666, Japan.
  • Shimizu T; National Agricultural Research Center, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-8666, Japan.
  • Uehara-Ichiki T; National Agricultural Research Center, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-8666, Japan.
  • Omura T; National Agricultural Research Center, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-8666, Japan.
  • Sasaki N; Gene Research Center, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu, Tokyo 183-8509 Japan.
  • Nyunoya H; Gene Research Center, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu, Tokyo 183-8509 Japan.
  • Sasaya T; National Agricultural Research Center, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-8666, Japan.
J Gen Virol ; 93(Pt 10): 2290-2298, 2012 Oct.
Article en En | MEDLINE | ID: mdl-22815270
ABSTRACT
Gene 3 in the genomes of several plant-infecting rhabdoviruses, including rice transitory yellowing virus (RTYV), has been postulated to encode a cell-to-cell movement protein (MP). Trans-complementation experiments using a movement-defective tomato mosaic virus and the P3 protein of RTYV, encoded by gene 3, facilitated intercellular transport of the mutant virus. In transient-expression experiments with the GFP-fused P3 protein in epidermal leaf cells of Nicotiana benthamiana, the P3 protein was associated with the nucleus and plasmodesmata. Immunogold-labelling studies of thin sections of RTYV-infected rice plants using an antiserum against Escherichia coli-expressed His(6)-tagged P3 protein indicated that the P3 protein was located in cell walls and on virus particles. In Western blots using antisera against E. coli-expressed P3 protein and purified RTYV, the P3 protein was detected in purified RTYV, whilst antiserum against purified RTYV reacted with the E. coli-expressed P3 protein. After immunogold labelling of crude sap from RTYV-infected rice leaves, the P3 protein, as well as the N protein, was detected on the ribonucleocapsid core that emerged from partially disrupted virus particles. These results provide evidence that the P3 protein of RTYV, which functions as a viral MP, is a viral structural protein and seems to be associated with the ribonucleocapsid core of virus particles.
Asunto(s)

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Enfermedades de las Plantas / Rhabdoviridae / Oryza / Virión / Proteínas de Movimiento Viral en Plantas Tipo de estudio: Risk_factors_studies Idioma: En Revista: J Gen Virol Año: 2012 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Enfermedades de las Plantas / Rhabdoviridae / Oryza / Virión / Proteínas de Movimiento Viral en Plantas Tipo de estudio: Risk_factors_studies Idioma: En Revista: J Gen Virol Año: 2012 Tipo del documento: Article