Location of Structural Proteins in Particles of Rice Gall Dwarf Virus

Abstract

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.

Component Proteins and Structure of Rice Ragged Stunt Virus

“…Furthermore, the antiserum reacted with all the component proteins of RRSV (data not shown). This contrasts with results from similar experiments with RDV and RGDV proteins (Minobe et al, 1984;Omura et al, 1985) in which it was mainly surface proteins that were recognized as antigens. However, antiserum to SDS-dissociated RDV particles did contain antibodies to all the component proteins of RDV particles .…”

“…The molecular weight distribution of the major proteins of RRSV is unlike that of plant reoviruses (Nakata et al, 1978;Reddy & Macleod, 1976;Nuss & Peterson, 1980;Omura et al, 1985 ;Van der Lubbe et al, 1979;Boccardo & Milne, 1975) (Fig. 2) and is perhaps a reflection of the lack of serological relationship between RRSV and the other plant reoviruses.…”

“…1 c) and no particles were pelleted in 2 M-MgClz. Electrophoresis of polypeptides, staining of the gels, scanning and molecular weight determination were performed according to the methods of Omura et al (1985) except that protein was dissolved in 1% SDS and 1% 2-mercaptoethanol by heating a suspension for 1 rain at 100 °C. Molecular weights of proteins were determined using SDS-PAGE Marker I [tool.…”

Conserved primary structures in core capsid proteins and reassembly of core particles and outer capsids between rice gall dwarf and rice dwarf phytoreoviruses

“…After 1 rain, the grid was rinsed with sodium phosphate buffer pH 7.0, then with water, and finally it was negatively stained with 2% uranyl acetate. The antisera against intact particles of RGDV and RDV used were those reported by Omura et al (1982) and Matsuoka et al (1985), respectively.…”

“…Immunoblotting was carried out according to the method described by Matsuoka et al (1985) using antiserum to RGDV (Omura et al, 1982). The antiserum to dissociated RDV used was that originally reported by Matsuoka et al (1985).…”