A 16-kDa protein was isolated from Helianthus annuus flowers by its ability
to inhibit the germination of fungal spores. This protein, SAP16, displays
an associated activity of trypsin inhibitor and was further purified to ap
parent homogeneity by affinity chromatography on trypsin-agarose. SAP16 cau
ses the complete inhibition of Sclerotinia sclerotiorum ascospores germinat
ion at a concentration of 5 mug.mL(-1) (0.31 muM) and a clear reduction of
mycelial growth at lower concentrations, indicating a strong antifungal pot
ency against this natural pathogen of sunflower. Our data suggest that the
antifungal ability of SAP16 would not be the result of the inhibition of a
fungal protease. This study contributes to the characterization of the emer
ging family of antifungal proteins with an associated activity of trypsin i
nhibition and emphasizes their role in plant resistance against fungal atta
ck. (C) 2000 Editions scientifiques et medicales Elsevier SAS.