@article{mbs:/content/journal/jgv/10.1099/0022-1317-67-8-1711, author = "Hagiwara, K. and Minobe, Y. and Nozu, Y. and Hibino, H. and Kimura, I. and Omura, T.", title = "Component Proteins and Structure of Rice Ragged Stunt Virus", journal= "Journal of General Virology", year = "1986", volume = "67", number = "8", pages = "1711-1715", doi = "https://doi.org/10.1099/0022-1317-67-8-1711", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-67-8-1711", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "RRSV", keywords = "proteins", keywords = "plant reovirus", abstract = "Summary Rice ragged stunt virus (RRSV) particles consist of a polyhedral core particle approx. 50 nm in diameter to which are attached flat spikes about 20 nm wide and 10 nm high, giving a total diameter of about 70 nm. Polyacrylamide gel electrophoresis of disrupted particles of RRSV gave five major polypeptides with mol. wt. of 145000 (145K), 137K, 72K, 47K and 37K. Core particles prepared by suspending particles in 0.5 m-MgCl2 contained the 145K, 137K, 72K proteins and relatively small amounts of the 37K protein, whereas the supernatant fluid recovered after centrifugation of the core particles contained the 47K and 37K proteins. The results suggest that the 145K, 137K and 72K proteins are core proteins and one or both of the 47K and 37K proteins are components of the spike. Immunoblotting experiments indicated that all the proteins are recognized as antigens, suggesting that RRSV particles are less stable than those of the phytoreoviruses, rice dwarf and rice gall dwarf viruses.", }