Alfalfa mosaic virus strains T6 and 425 differ in their capsid protein.
Capsid proteins (CPs) of two strains of alfalfa mosaic virus (AIMV)-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 AIMV strain T6 was isolated from lucerne in Czech Republic (Gallo, 1977). Previously, its morhology, symptomatology and RNA electrophoretic mobility were characterized and compared with those of the strain 425 (Hagedorn and Handson, 1963; Kúdela and Gallo, 1995). In this study we show that the CP composition of these two AIMV strains differs, too. AIMV, 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 non-coding regions or in CP composition (Kraal, 1975; Kraal et al., 1976; Collot et al., Dore et al., 1989; Neeleman et al., 1991).
Institute of Virology, Slovak Academy of Sciences, Bratislava, Slovak Republic.
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Gallo
D017794:Alfalfa mosaic virus / Q000302:isolation & purification / Q000378:metabolism*; D002213:Capsid / Q000737:chemistry*; D015180:Electrophoresis, Gel, Two-Dimensional; D010449:Peptide Mapping