Mannan-Binding Lectin of the Sea Urchin Strongylocentrotus nudus

被引：11

作者：

Bulgakov, Aleksandr A. ^{[1
]}

Eliseikina, Marina G. ^{[2
]}

Kovalchuk, Svetlana N. ^{[1
,4
]}

Petrova, Irina Yu ^{[2
]}

Likhatskaya, Galina N. ^{[1
]}

Shamshurina, Ekaterina V. ^{[2
,3
]}

Rasskazov, Valery A. ^{[1
]}

机构：

[1] Russian Acad Sci, GB Elyakov Pacific Inst Bioorgan Chem, Far Eastern Branch, Vladivostok 690022, Russia

[2] Russian Acad Sci, AV Zhirmunsky Inst Marine Biol, Far Eastern Branch, Vladivostok 690059, Russia

[3] Far Eastern Fed Univ, Interdept Lab Biol Marine Invertebrates, Vladivostok 690950, Russia

[4] Far Eastern Fed Univ, Div Cell Biol & Genet, Vladivostok 690950, Russia

来源：

MARINE BIOTECHNOLOGY | 2013年 / 15卷 / 01期

基金：

俄罗斯基础研究基金会;

关键词：

cDNA cloning; Echinoderms immunity; Mannan-binding lectin; Strongylocentrotus nudus; C-TYPE LECTINS; STRUCTURAL BASIS; SWISS-MODEL; PROTEIN; COMPLEMENT; RECOGNITION; ACTIVATION; BIOLOGY; ENVIRONMENT; COLLECTINS;

D O I：

10.1007/s10126-012-9460-5

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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.

引用

页码：73 / 86

页数：14

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