Purification and characterization of Fus sI3596*, a 65 kd allergen of Fusarium solani.

A component of Fusarium solani (F. solani), identified as the major allergen, Fus sI3596* was purified to homogeneity from culture filtrate (CF) by means of anion-exchange column chromatography, gel filtration and FPLC. The homogeneity of Fus sI3596* was assessed by IEF, PAGE, SDS-PAGE (non-reducing), immunoblot and HPLC. Fus sI3596* was isolated as a glycoprotein of MW 65 kd and pI 3.6. The IgE ELISA-inhibition assay after periodate treatment of the fraction showed a lower IgE binding capacity suggesting involvement of carbohydrate moiety in IgE binding reactions of the allergen. Peptide fragments of Fus sI3596* obtained after CNBr and trypsin treatment were analysed by immunoblotting for their allergenicity. This study indicated that there could be at least 3 allergenic determinants in the major allergen, Fus sI3596* of F. solani CF.