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Molecular diversity of skin mucus lectins in fish
Authors:Suzuki Yuzuru  Tasumi Satoshi  Tsutsui Shigeyuki  Okamoto Masaki  Suetake Hiroaki
Institution:Fisheries Laboratory, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Maisaka, Shizuoka 431-0211, Japan
Abstract:Among lectins in the skin mucus of fish, primary structures of four different types of lectin have been determined. Congerin from the conger eel Conger myriaster and AJL-1 from the Japanese eel Anguilla japonica were identified as galectin, characterized by its specific binding to β-galactoside. Eel has additionally a unique lectin, AJL-2, which has a highly conserved sequence of C-type lectins but displays Ca2+-independent activity. This is rational because the lectin exerts its function on the cutaneous surface, which is exposed to a Ca2+ scarce environment when the eel is in fresh water. The third type lectin is pufflectin, a mannose specific lectin in the skin mucus of pufferfish Takifugu rubripes. This lectin showed no sequence similarity with any known animal lectins but, surprisingly, shares sequence homology with mannose-binding lectins of monocotyledonous plants. The fourth lectin was found in the ponyfish Leiognathus nuchalis and exhibits homology with rhamnose-binding lectins known in eggs of some fish species. These lectins, except ponyfish lectin, showed agglutination of certain bacteria. In addition, pufflectin was found to bind to a parasitic trematode, Heterobothrium okamotoi. Taken together, these results demonstrate that skin mucus lectins in fish have wide molecular diversity.
Keywords:Fish  Skin mucus  Lectin  Galectin  C-type lectin  Lily-type lectin  Rhamnose-binding lectin  Molecular diversity
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