Double-stranded RNA (dsRNA) from virus particles isolated from a P4 killer strain (isolate 77) of , which secretes a protein toxin of apparent approx. 10000 (10K) was resolved by PAGE into eight segments with sizes (kbp) 6·7 (H1), 4·5 (H2), 3·2 (H3a), 3·1 (H3b), 2·6 (H4), 0·98 (M2-4), 0·92 (M3-4) and 0·36 (L1). A subculture, designated 77-3A, was found to have lost the H2 and M3-4 segments, but still produced virus particles and protein toxin. Northern hybridization showed that dsRNA segments M2-4 and L1 are related but no homology was detected between H1, H3a, H3b and H4, or between any of these H segments and M2-4 or L1. When individual denatured dsRNA segments were translated in a reticulocyte lysate system H1, H3a, H3b and H4 each gave rise to polypeptides in the range 100K to 128K. Polypeptides of apparent 108K and 128K, encoded by H3b, and 100K, encoded by H4, were immunoprecipitated by antiserum to purified virus particles from subculture 77-3A. translation of denatured M2-4 gave rise to polypeptides of apparent 26K and 13K which were immunoprecipitated by antiserum to the secreted protein toxin. No translation product was detected from denatured L1.


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