Fimbrial-dependent mating in Microbotryum violaceum involves a mannose-lectin interaction

Fimbriae of the anther smut fungus, Microbotryum violaceum are polymers of six 74-kDa glycoprotein isoforms. Digestion of fimbrial monomers with alpha-mannosidase yielded two polypeptides with masses of 70 and 48 kDa. The 70-kDa polypeptide is probably a product of incomplete digestion and the 48-kDa polypeptide is the aglycone. Thus, most of the carbohydrate component of fimbrial protein is mannose. Previous observations have suggested that fimbriae are necessary for mating in M. violaceum. Further evidence for this role was obtained in the present study by showing that mating is inhibited by an anti-fimbrial protein antiserum, by mannose and related sugars glucose and arabinose, and by the lectin concanavalin A. Since inhibition was not complete, however, two mechanisms for adhesion between compatible cells were proposed, one fimbrial dependent and one independent. Lastly, fimbrial protein from a(1) but not a(2) mating types bound to a mannose-agarose column, suggesting a lectin-like capability. The fimbrial dependent mechanism of cell-to-cell adhesion may involve binding of the mannose residues of the fimbriae of a(2) cells by the fimbriae of a(1) cells.