The proteins of purified polyhedra of the cytoplasmic polyhedrosis virus (CPV) of were examined by electrophoresis in polyacrylamide gels containing SDS. The major polypeptide in polyhedra, and in inclusion body protein (poly-hedral protein) had a mol. wt. of 37000, and stained positively for carbohydrate. Purified virus particles contained three polypeptides, with mol. wt. of 116000, 109000 and 30000. RNA extracted from the virus particles had a melting profile characteristic of double-stranded RNA. Nine bands were resolved when this RNA was electrophoresed through 3% polyacrylamide gels. A comparison of the molar proportions of these segments suggests that there are 10 pieces of RNA, which form a genome with a mol. wt. of 14.4 × 10. There was good agreement between the sizes of the structural polypeptides, and the estimated coding capacity of four of the RNA segments. CPV virus particles share features in common with reovirus and, in particular, with the ‘core’ particles obtained by the enzymic digestion of intact reovirus particles.


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