Comparison of the virus-associated polymerases of cytoplasmic polyhedrosis virus types 1 and 2.

A detailed comparison was made of the virus-associated polymerase activities of cytoplasmic polyhedrosis virus (CPV) types 1 and 2 which had previously been shown to differ in their response to the methyl donor S-adenosyl-L-methionine (AdoMet). While the type 1 CPV polymerase was approximately twice as active as the type 2 CPV enzyme in the presence of AdoMet, temperature, pH and divalent cation optima of the two enzymes were similar. Both viruses synthesized in vitro single-stranded RNA copies of only one strand of the double-stranded RNA genome. In addition, each RNA segment of both viruses was transcribed in approximately equal amounts by weight. The results suggest that most features of CPV polymerase activity are highly conserved, even among CPV types which show substantial antigenic and biochemical differences.