TWENTY-THIRD ANNUAL EASTERN FISH HEALTH WORKSHOP JOHN CARVER INN, PLYMOUTH, MA 30 MARCH - 2 APRIL, 1998 Purification And Characterization Of A Mannose-Binding Serum Lectin From Atlantic salmon Neil W. Ross, K. Vanya Ewart, Stewart C. Johnson National Research Council of Canada, Institute for Marine Biosciences, 1411 Oxford St., Halifax, Nova Scotia B3H 3Z1 CANADA Our laboratory is investigating aspects of the innate and adaptive immune responses of Atlantic salmon. As part of this initiative we have screened Atlantic salmon serum for the presence of soluble lectins. Lectins are sugar-binding proteins and many have been shown to be a first line of defense during infection in mammals and some other vertebrates. However, the biochemistry of lectins and their roles in fish health are not known. We have isolated a number of mannose-binding proteins from salmon serum by affinity chromatography. One calcium-dependent lectin exists as disulfide-linked multimers of a polypeptide having a relative molecular mass (Mr) of 17,000. The calcium dependence was characterized by EDTA elution of the lectin from mannose affinity column and ruthenium red binding. This lectin binds to the surfaces of Vibrio anguillarum and Aeromonas salmonicida. Binding to the bacteria is inhibited by mannose but not by galactose. N-Terminal peptide sequence analysis does not show similarity to any identified protein sequence. Studies are underway to identify the lectin gene with the goal to examining its regulation in disease.   Return to 23rd Annual Eastern Fish Health Workshop Return to Leetown Science Center Home Page