The ability of the fluorescent-coupled lectins wheat germ agglutin (WGA) and Concanavalin A (Con A) to react with selected Basidiomycetes, Ascomycetes, and Fungi Imperfecti was evaluated using pure cultures of 35 fungi grown on malt extract agar. WGA, which binds specifically to the n-acetylglucosamine residues found in fungal chitin, reacted with nearly all hyaline fungal structures but did not react with dematiaceous (dark) structures. Several reasons are suggested for this variation. Con A, which is specific for a-D-mannosyl and a-D-glucosyl residues, reacted with about one half of the fungi that reacted with WGA. This variation in reactivity may be useful for studying simultaneous degradation by morphologically similar fungi having different lectin specificities. The results indicate that WGA is a useful probe for studying fungal degradation by non-dematiaceous fungi particularly at the early stages of decay.

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