Purification and characterization of cassiicolin, the toxin produced by Corynespora cassiicola, causal agent of the leaf fall disease of rubber tree.
Cassiicolin, a phytotoxin produced by the necrotrophic fungus Corynespora cassiicola, was purified to homogeneity from a rubber tree isolate. The optimized protocol involves reverse phase chromatography followed by size exclusion chromatography, with monitoring of the toxicity on detached rubber tree leaves. Cassiicolin appeared to be a peptide composed of 27 amino acids, glycosylated on the second residue, with a N-terminal pyroglutamic acid and 6 cysteines involved in disulfide bonds. Its molecular mass was estimated to be 2885 Da. No significant sequence homology with other proteins could be found. The availability of pure toxin in sufficient amount is a prerequisite for its structure determination, which is a key step in the understanding of the aggression mechanism.
de Lamotte
Frédéric
F
INRA-UMR PIA - 2 Place Viala - Bat 31, 34 060 Montpellier cedex 01, France.
Duviau
Marie-Pierre
MP
Sanier
Christine
C
Thai
Robert
R
Poncet
Joël
J
Bieysse
Daniel
D
Breton
Frédéric
F
Pujade-Renaud
Valérie
V
D000595:Amino Acid Sequence; D001203:Ascomycota / Q000378:metabolism*; D002853:Chromatography, Liquid / Q000379:methods; D004586:Electrophoresis / Q000379:methods; D028482:Hevea / Q000187:drug effects / Q000382:microbiology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009183:Mycotoxins / Q000737:chemistry / Q000302:isolation & purification* / Q000633:toxicity; D018515:Plant Leaves / Q000187:drug effects / Q000382:microbiology*; D015203:Reproducibility of Results; D020539:Sequence Analysis, Protein; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods
D009183:Mycotoxins