Identification of a pathogen-binding lectin in salmon serum.

A mannose-binding lectin was isolated from the blood serum of Atlantic salmon (Salmo salar). Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing and non-reducing conditions revealed a multimeric structure composed of 17000 Mr subunits. Hexosamine analysis and glycosidase digestion showed that the lectin is not glycosylated and amino acid analysis revealed no unusual compositional features. Using ruthenium red staining, the lectin was shown to bind Ca2+ ions. N-terminal sequencing by Edman degradation gave: H2N-TGAKGAEEGVVPAETRNQXPTGWFQFGS. A database search revealed no similarity to protein sequences deposited to date. Binding experiments using biotinylated lectin revealed that it specifically recognizes and binds to mannose on the surfaces of two salmon pathogens, Vibrio anguillarum and Aeromonas salmonicida, implying an immunological role for this lectin in Atlantic salmon.