Lectins are a superfamily of carbohydrate-binding proteins that are widely distributed throughout living organisms. In earlier work, we identified lily-type lectin (SmLTL) in the skin mucus of turbot Scophthalmus maximus, and we characterized the protein in the present study. Results from qRT-PCR indicated that SmLTL was expressed highly in skin, intestine and gill tissue. Changes in SmLTL expression occurred in these tissues in response to environmental stressors including ciliate infection, high temperature and salinity. Recombinant SmLTL purified from Escherichia coli was able to haemagglutinate mouse erythrocytes in the absence of calcium, and was inhibited by d-mannose. In addition, SmLTL displayed selective binding to bacterial species including Edwardsiella tarda and Vibrio anguillarum, and exhibited toxicity towards Philasterides dicentrarchi, with a mortality of over 60% after 24 h at a concentration of only 100 μgml−1. To investigate this toxicity further, we measured binding of SmLTL after incubating the ciliate in FITC-SmLTL solution. Surface fluorescence decreased substantially in the presence of 400 mM d-mannose. Together these results suggest that lily-type lectins serve as the first line of defence against microbial attack and play a pivotal role in the mucosal immune system.