Cmcp. Gouvea et al., ACCUMULATION OF A HOST MICROSOMAL FRACTION PROTEIN IN VIRUS-INFECTED CUCUMBER AND TOMATO, Plant physiology and biochemistry, 33(4), 1995, pp. 453-461
Total, soluble and microsomal fraction proteins were isolated from lea
ves of healthy and virus-infected cucumber and tomato plants, and sepa
rated by SDS-polyacrylamide gel electrophoresis. The analysis revealed
the accumulation of a microsomal fraction protein in severely infecte
d plants: cucumber with zucchini yellow mosaic virus (ZYMV) and tomato
with cucumber mosaic virus (CMV). The proteins accumulated (MP 39) in
the hosts when they showed severe disease symptoms exhibited the same
electrophoretic mobility and had a molecular mass of approximately 39
kDa. The MP 39 was not revealed by concanavalin-A, and was present in
the aqueous phase from Triton X-114 fractionation, indicating that th
e MP 39 is a peripheral membrane protein. Bidimensional electrophoreti
c analysis revealed the same characteristics for the protein accumulat
ed in infected cucumber and tomato. Antibodies directly raised against
virus particles failed to react with the MP 39, suggesting the accumu
lated protein is unrelated to any of the structural proteins of ZYMV a
nd CMV, being probably a host encoded protein that accumulates in seve
rely virus-infected plants. While activities of soluble and cell wall
bound peroxidases were increased in infected plants, no peroxidase act
ivity was found associated with MP 39. The data obtained in this work
are a good base for subsequent studies on the role of the MP 39 in inf
ected plants.