Purification of chrysancorin, a novel antifungal protein with mitogenic activity from garland chrysanthemum seeds

A novel antifungal protein, designated chrysancorin, was isolated from seed s of Chrysanthemum coronarium var. spatiosum with a procedure involving ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi -gel blue resin, ion exchange chromatography on SP-Sepharose and FPLC-gel f iltration on Superdex 75. The N-terminus of chrysancorin displays sequence similarity to the genomic sequence of chromosome 1 from Arabidopsis thalian a BAC T19E23. Chrysancorin exhibits a molecular mass of 13.4 kDa in gel fil tration and SDS-polyacrylamide gel electrophoresis. It stimulates the proli feration of mouse splenocytes and inhibits the activity of human immunodefi ciency virus-1 reverse transcriptase. The protein possesses antifungal acti vity against Botrytis cinerea, Mycosphaerella arachidicola and Physalospora piricola, but not against Rhizoctonia solani, Fusarium oxysporum and Copri nus comatus. However, we could not detect antibacterial activity against a variety of bacteria.