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Differentiation of Potyviruses through Peptide Mapping of Cytoplasmic Inclusion Proteins
Author(s) -
Albrechtsen M.,
Paludan N.,
Heide M.
Publication year - 1991
Publication title -
journal of phytopathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.53
H-Index - 60
eISSN - 1439-0434
pISSN - 0931-1785
DOI - 10.1111/j.1439-0434.1991.tb01192.x
Subject(s) - peptide , potyvirus , biology , cleavage (geology) , cytoplasm , gel electrophoresis , tryptophan , polyacrylamide gel electrophoresis , virus , biochemistry , virology , microbiology and biotechnology , amino acid , enzyme , plant virus , paleontology , fracture (geology)
Cytoplasmic inclusion proteins (CIP) from 15 isolates representing 12 different potyviruses were purified and compared by peptide mapping in sodium dodecylsulphate polyacrylamide gels. Enzymatic cleavage by endoproteinase Glu‐C from Staphylococcus aureus V8 was performed in the gel during electrophoresis. Distinct patterns were obtained for all different potyviruses, while different isolates of the same virus produced identical patterns. When performed under standardized conditions this method produced very reproducible peptide maps. Chemical cleavage at tryptophan residues by N‐chlorosuccinimide produced very similar peptide patterns for CIP from all potyviruses studied with the exception of leek yellow stripe virus. The results suggest that peptide mapping of CIP using endoproteinase Glu‐C can be used in the identification and differentiation of potyviruses.