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Mannan-Binding Lectin of the Sea Urchin Strongylocentrotus nudus |
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| Authors: | Aleksandr A Bulgakov Marina G Eliseikina Svetlana N Kovalchuk Irina Yu Petrova Galina N Likhatskaya Ekaterina V Shamshurina Valery A Rasskazov |
| Institution: | 1. G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch of the Russian Academy of Science, Stoletya Vladivostoku str. 159, Vladivostok, 690022, Russia 2. A.V. Zhirmunsky Institute of Marine Biology, Far Eastern Branch of the Russian Academy of Sciences, Palchevskogo str. 17, Vladivostok, 690059, Russia 4. Division of Cell Biology and Genetics, Far Eastern Federal University, 8, Sukhanova str., Vladivostok, 690950, Russia 3. Interdepartmental Laboratory “Biology of Marine Invertebrates”, Far Eastern Federal University, 8, Sukhanova str., Vladivostok, 690950, Russia |
| Abstract: | A novel lectin specific to low-branched mannans (MBL-SN) was isolated from coelomic plasma of the sea urchin Strongylocentrotus nudus by combining anion-exchange liquid chromatography on DEAE Toyopearl 650 M, affinity chromatography on mannan-Sepharose and gel filtration on the Sephacryl S-200. The molecular mass of MBL-SN was estimated by sodium dodecyl sulphate polyacrylamide gel electrophoresis under non-reducing conditions to be about 34 kDa. MBL-SN was shown to be a dimer with two identical subunits of about 17 kDa. The native MBL-SN exists as a tetramer. The physico-chemical properties of MBL-SN indicate that it belongs to C-type mannan-binding lectins. The cDNA encoding MBL-SN was cloned from the total cDNA of S. nudus coelomocytes and encodes a 17-kDa protein of 144 amino acid residues that contains a single carbohydrate-recognition domain of C-type lectins. Prediction of the MBL-SN tertiary structure using comparative modelling revealed that MBL-SN is an α/β-protein with eight β-strands and two α-helices. Comparison of the MBL-SN model with available three-dimensional structures of C-type lectins revealed that they share a common fold pattern. |
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