The role of the conidial sheath in the recognition process and in the attachment of conidia of the beech endophyte, Discula umbrinella, to the host surface was investigated. After treatment of conidia with different lectins the adhesion of conidia to the host surface was effectively inhibited. A strong fluorescence was observed after treatment of conidia with TRITC-labelled concanavalin A. Fluorescence with TRITC-labelled wheat germ agglutinin was observed only on spores subjected to enzymatic digestion with proteases. Observations with the transmission electron microscope (TEM), after labelling sections with colloidal gold conjugated lectins, confirmed the presence of mannose and/or glucose in the extracellular sheath. Chitin was present in the conidial ceil wall but not in the extracellular sheath. Enzymatic treatment of the conidial sheath resulted in strongly reduced attachment and changes in the binding of fluorescence-labelled lectins. TEM studies of partially digested conidia revealed that snail enzyme modified only slightly the structure of the sheath, while proteases completely dissolved the fibrillar sheath leaving a comparatively smooth cell wall with no fibrillar structures on its surface. We conclude that a proteinaceous sheath is responsible for the adhesion of Discula umbrinella conidia to the host and that glycoproteins are involved in the recognition and attachment process. This attachment mechanism closely parallels the only other recognition system studied biochemically in endophytes, and is similar to the few analogous cases studied in plant-pathogenic fungi, pointing to the functional relatedness of endophytic and pathogenic interactions.