Alfalfa mosaic virus strains T6 and 425 differ in their capsid protein
Subr, Z.; Kúdela, O.; Gallo, J.
Acta Virologica 40(3): 147-149
1996
ISSN/ISBN: 0001-723X PMID: 8891095 Document Number: 465099
Capsid proteins (CPs) of two strains of alfalfa mosaic virus (AlMV) - T6 and 425 - were compared using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) peptide mapping and two-dimensional PAGE (2D-PAGE). The CPs had identical molecular mass but differed in their peptide pattern and charge. The AlMV strain T6 was isolated from lucerne in Czech Republic (Gallo, 1977). Previously, its morphology, symptomatology and RNA electrophoretic mobility were characterized and compared with those of the strain 425 (Hagedorn and Handson, 1963; Kudela and Gallo, 1995). In this study we show that the CP composition of these two AlMV strains differs, too. AlMV, the unique member of the genus Alfamovirus, family Bromoviridae, is of economic significance in many countries in the world, particularly for its seed transmissibility and relative broad host range. Plenty of strains with different biological properties have been isolated (Van Regenmortel and Pinck, 1981). Some of them have been shown to differ in their RNA noncoding regions or in CP composition (Kraal, 1975; Kraal et al., 1976; Collot et al., 1976; Dore et al., 1989; Neeleman et al., 1991).