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首页> 外文期刊>Infection and immunity >Characterization of porcine intestinal receptors for the K88ac fimbrial adhesin of Escherichia coli as mucin-type sialoglycoproteins.
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Characterization of porcine intestinal receptors for the K88ac fimbrial adhesin of Escherichia coli as mucin-type sialoglycoproteins.

机译：大肠杆菌K88ac纤维粘附素的猪肠受体表征为粘蛋白型唾液糖蛋白。

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摘要

We have previously identified two K88ac adhesion receptors (210 and 240 kDa) which are present in membrane preparations from adhesive but not nonadhesive porcine intestinal brush border cells; these adhesin receptors are postulated to be important determinants of the susceptibility of pigs to K88ac+ enterotoxigenic Escherichia coli infections (A.K. Erickson, J.A. Willgohs, S.Y. McFarland, D.A. Benfield, and D.F. Francis, Infect. Immun. 60:983-988, 1992). We now describe a procedure for the purification of these two receptors. Receptors were solubilized from adhesive intestinal brush border vesicles using deoxycholate and were purified by gel filtration chromatography on Sepharose CL-4B and then by hydroxyapatite chromatography. Amino acid compositional analyses indicated that the two receptors have similar amino acid compositions. The most distinguishing characteristic of both receptors is a high percentage of threonine and proline residues. Neuraminidase treatment caused the K88ac adhesin receptors to migrate with a slower mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels, indicating that these receptors are sialoglycoproteins. Results from lectin-binding studies indicated that the receptors contain O-linked oligosaccharides composed of galactosyl (beta-1,3)N-acetylgalactosamine, alpha-linked fucose, galactosyl(beta-1,4)N-acetylglucosamine, sialic acid, galactose, and N-acetylgalactosamine. Collectively, these characteristics indicate that the K88ac adhesin receptors are mucin-type sialoglycoproteins.
机译：我们以前已经确定了两种K88ac粘附受体（210和240 kDa），它们存在于粘附性而不是非粘附性猪肠刷缘细胞的膜制剂中。这些粘附素受体被认为是猪对K88ac +肠毒素性大肠杆菌感染的易感性的重要决定因素（A.K. Erickson，J.A. Willgohs，S.Y. McFarland，D.A. Benfield，and D.F. Francis，Infect。Immun。60：983-988，1992）。现在我们描述纯化这两种受体的方法。使用脱氧胆酸盐从粘性肠刷缘小泡中溶解受体，并通过在Sepharose CL-4B上的凝胶过滤色谱法和然后通过羟基磷灰石色谱法纯化。氨基酸组成分析表明两种受体具有相似的氨基酸组成。两种受体的最显着特征是高百分比的苏氨酸和脯氨酸残基。神经氨酸酶处理导致K88ac粘附素受体以十二烷基硫酸钠-聚丙烯酰胺凝胶电泳凝胶上的较慢迁移率迁移，表明这些受体是唾液酸糖蛋白。凝集素结合研究的结果表明，该受体含有由半乳糖基（β-1,3）N-乙酰半乳糖胺，α-连接岩藻糖，半乳糖基（β-1,4）N-乙酰葡糖胺，唾液酸，半乳糖组成的O-连接寡糖。和N-乙酰半乳糖胺。这些特征共同表明，K88ac粘附素受体是粘蛋白型唾液糖蛋白。

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