MOLECULAR CLONING AND ANALYSIS OF A SALMON SERUM C-TYPE LECTIN

• Main Authors: Robert C. Richards, David Hudson, Pierre Thibault, K. Vanya Ewart
• Other Authors: The Pennsylvania State University CiteSeerX Archives
• Format: Text
• Language: English
• Subjects: Atlantic salmon; Salmo salar
• Online Access: http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.512.6283; http://www-heb.pac.dfo-mpo.gc.ca/congress/2002/disruptors/richards.pdf

Innate immunity involves the direct recognition and destruction of a pathogen without prior exposure. Fish have a relatively variable capacity for antibody-mediated immunity (reviewed elsewhere). Therefore, the role of innate immunity, including humoral events such as complement activation and cellular systems such as phagocytosis by macrophages, is expected to be very important in fish, particularly under conditions in which antibody-mediated immunity might be compromised. Innate immunity hinges on the recognition of non-self cells and this frequently occurs by means of the distinct carbohydrate patterns on their surfaces. In chicken and in several mammals, C-type (Ca2+-dependent) lectins can play this role. For example, the human mannose-binding lectin plays a key role in resistance to common diseases and lectin deficiency is linked to increased susceptibility to infection (Turner and Hamvas, 2000). To determine whether similar immune-active lectins might be present in fish, mannose-binding proteins were purified from serum of healthy Atlantic salmon (Salmo salar) and the most abundant protein was characterised. This multimeric