Summary auto-generated
Rice ragged stunt virus (RRSV) is a plant reovirus that causes disease in rice and is transmitted by brown planthoppers. This study characterized the structural proteins and morphology of RRSV particles. Electron microscopy revealed RRSV particles consist of a polyhedral core approximately 50 nm in diameter with attached flat spikes about 20 nm wide and 10 nm high, giving a total diameter of approximately 70 nm. Polyacrylamide gel electrophoresis identified five major polypeptides with molecular weights of 145,000 (145K), 137K, 72K, 47K, and 37K. Treatment with magnesium chloride selectively removed spikes while preserving core particles, allowing protein localization. The 145K, 137K, and 72K proteins were identified as core components, while the 47K and 37K proteins appear to be spike components. Immunoblotting showed all RRSV proteins are recognized as antigens, indicating RRSV particles are structurally more labile than related plant reoviruses such as rice dwarf and rice gall dwarf viruses. The protein composition of RRSV differs significantly from other characterized plant reoviruses.
Key findings
- RRSV particles are 70 nm in diameter consisting of a 50 nm polyhedral core with 20×10 nm spikes
- Five major structural proteins identified: 145K, 137K, and 72K (core proteins) and 47K and 37K (spike proteins)
- All RRSV structural proteins are antigenic, suggesting particle instability compared to related plant reoviruses
- RRSV protein composition and molecular weight distribution are distinct from other characterized plant reoviruses
- MgCl₂ treatment effectively removes spikes while preserving core particles, enabling protein localization studies
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Abstract
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.