Characterization of bean mild mosaic virus: particle morphology, composition and RNA cell-free translation.

Abstract

Virions of bean mild mosaic virus (BMMV) are built of 180 subunits of a single protein species of MW 40 x 10(3) [coat protein CP], packed into a T = 3 surface lattice. The capsomers on the five-fold symmetry axes protrude 2-3 nm from the particle surface. The virions encapsidate genome-size [approximately 4,200 nucleotides (nt)] as well as some heterogeneous RNAs of subgenomic size approximately 1,000-2,000 nt. In cell-free systems from Krebs-2 ascites cell extracts and rabbit reticulocyte lysates, genome-size RNA directed the synthesis predominantly of two polypeptides of MW 27 x 10(3) and 79 x 10(3) while the third major BMMV-specific polypeptide (MW 40 x 10(3), putative CP) seemed to be encoded by a shorter messenger RNA. The 'cap' analogue, m7GDP, partially inhibited BMMV RNA in vitro translation, suggesting that at least part of the BMMV-specific RNAs are capped. Oligo (dT)-cellulose column chromatography data suggested that poly(A)-tracts are absent from the BMMV genome. The data obtained confirm the previous classification of BMMV within the carmovirus group.