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肺表面活性蛋白D碳水化合物识别结构域的表达及其与革兰氏阴性菌脂多糖结合的证明。

Expression of the carbohydrate recognition domain of lung surfactant protein D and demonstration of its binding to lipopolysaccharides of gram-negative bacteria.

作者信息

Lim B L, Wang J Y, Holmskov U, Hoppe H J, Reid K B

机构信息

Department of Biochemistry, University of Oxford, UK.

出版信息

Biochem Biophys Res Commun. 1994 Aug 15;202(3):1674-80. doi: 10.1006/bbrc.1994.2127.

DOI:10.1006/bbrc.1994.2127
PMID:8060356
Abstract

Surfactant protein D is a collagenous C-type lectin (collectin) that is found almost exclusively in the lung. A recombinant protein, composed of the neck-region and the carbohydrate binding domain of bovine lung surfactant protein D, has been overexpressed in E. coli. The recombinant protein showed the same sugar binding specificity as the native protein and was able to bind to the lipopolysaccharides of several strains of Gram-negative bacteria, such as Klebsiella pneumoniae, Pseudomonas aeruginosa and Escherichia coli, which are known to cause lung infections. The binding was calcium-dependent and was inhibited by maltose. Native bovine surfactant protein D was also shown to be able to bind to these lipopolysaccharides in the same manner.

摘要

表面活性蛋白D是一种几乎仅存在于肺中的胶原性C型凝集素(collectin)。一种由牛肺表面活性蛋白D的颈部区域和碳水化合物结合结构域组成的重组蛋白已在大肠杆菌中过表达。该重组蛋白表现出与天然蛋白相同的糖结合特异性,并且能够结合几种革兰氏阴性菌的脂多糖,如已知会引起肺部感染的肺炎克雷伯菌、铜绿假单胞菌和大肠杆菌。这种结合是钙依赖性的,并被麦芽糖抑制。天然牛表面活性蛋白D也被证明能够以相同的方式结合这些脂多糖。

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