A non-occluded virus of Galleria mellonella was purified using a chloroform+butanol treatment followed by sucrose gradient centrifugation. Purified virus and top component were produced in proportions of 1:3; their diameters were approximately 200 Å, and their sedimentation coefficients 119S and 58S respectively. The virus had an approximate DNA:protein ratio of 37:63.
Virus and top component were serologically identical in gel diffusion tests and both were different antigenically from insect proteins with sedimentation coefficients of 2 to 3S, 17S, 30S and 70 to 75S, present in both healthy and infected larvae. The amino acid composition of the protein from the virus and top component was very similar, and differed from that of the 17S component. No soluble antigens were detected in the extracts of infected larvae.
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