Journal
MARINE BIOTECHNOLOGY
Volume 15, Issue 1, Pages 73-86Publisher
SPRINGER
DOI: 10.1007/s10126-012-9460-5
Keywords
cDNA cloning; Echinoderms immunity; Mannan-binding lectin; Strongylocentrotus nudus
Funding
- Russian Foundation for Basic Research [11-04-01778-a]
- Eastern Branch Russian Academy of Sciences [09-III-A-05-150]
- Russian Federation Government [11.G34.31.0010]
- FEBRAS [12-III-A-05-059]
- Program of the Russian Academy of Science Presidium Molecular and Cellular Biology [12-I-P6-10]
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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 alpha/beta-protein with eight beta-strands and two alpha-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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