A novel lectin was isolated and purified from the culture filtrate o f the PO Box 12, Rehovot 76100, Israel column with the flow-through, whereas all the non-agglutinating proteins present in the crude preparation remained bound t o the column until elution in a NaCl gradient. SDS-PAGE analysis o f the agglutinating fraction revealed a single band corresponding to a protein with a molecular mass of approximately 45 kDa. Agglutination o f Escherichia coli cells by the purified lectin was not inhibited by any o f the mono-or disaccharides tested, whereas the glycoproteins mr.icin and asialomucin did inhibit agglutination. Proteases, as well as 1,3-/?-glucanase, were found t o be totally destructive t o agglutination activity, indicating that both protein and 1,3-/?-glucan are necessary for agglutination. Using a biomimetic system based on binding o f the lectin to the surface o f inert nylon fibres revealed that the presence o f the purified agglutinin on the surface of the fibres specifically induced mycoparasitic behaviour in Trichoderma harzianum. Trichoderma formed tightly adhering coils, which were significantly more frequent with the purified agglutinin-treated fibres than with untreated ones or with those treated with non-agglutinating extracellular proteins from 5. rolfsii. Other mycoparasite-related structures, such as appressorium-like bodies and hyphal loops, were only observed in the interaction between T. harzianum and the purified agglutinin-treated fibres.