Two concentric protein shell structure with spikes of silkworm Bombyx mori cytoplasmic polyhedrosis virus revealed by...

The overall and internal structures of the silkworm Bombyx mori cytoplasmic polyhedrosis virus was investigated by small-angle neutron scattering using the contrast variation method. Data were collected in aqueous buffer solutions containing 0, 50, 75, and 100% D2O in the q range of 0.002 to 0.0774 A-1 at 5 degrees C. The radius of gyration at infinite contrast was estimated to be 336 A. The contrast matching point of the virus was determined to correspond to about 50% D2O level, evidence that the virus is composed of protein and nucleic acid. The virus was basically spherical and had a diameter of about 700 A. The main feature of its structure is the clustering of protein into two concentric shells separated by about 100 A. Most of the RNA moieties are located in the central core and between these two protein shells. However, the distance distribution function P(r) showed a minor distribution beyond a distance of r = 700 A, with a maximum particle distance of the virus of 1350 A. This is indicative of an external structure region with very low scattering density, in addition to the basic spherical structure. This external region is thought to correspond to twelve pyramidal protruding spikes shown by electron microscopic studies.