Purified preparations of isolate C of andean potato mottle virus (APMV) contained isometric particles 28 nm in diam. with sedimentation coefficients ( ) of about 53, and 93 and 112S. The two nucleoprotein components, middle (M) and bottom (B), were serologically indistinguishable, and each contained similar relative amounts of two polypeptide species, of mol. wt. 22100 and 41800. M particles had a density in CsCl of 1.41 g/ml, contained a single RNA species of mol. wt. 1.4 × 10 and stained differently from B particles with uranyl formate; B particles had a density of 1.46 g/ml and contained a single RNA species of mol. wt. 2.0 × 10. Preparations of M and B particles were much less infective when inoculated separately than in mixtures. In these properties APMV resembles other comoviruses. The present cryptogram of APMV is R/1:1.4/(27) + 2.0/(34):S/S:S/*, comovirus group.

The two isolates studied, C and H, infected systemically, and therefore differ from the type strain of APMV. Isolate C was antigenically indistinguishable from the type strain and produced similar symptoms in several solanaceous species. Isolate H differed antigenically from C and the type strain, and also differed somewhat in symptomatology and host range.


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