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Identification of an Intestinal Neutral Glycosphingolipid as a Phenotype-Specific Receptor for the K88ad Fimbrial Adhesin of Escherichia coli

机译:肠道中性糖鞘脂作为表型特异性受体的大肠杆菌K88ad膜粘附素的鉴定。

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In this study, we identified a receptor for the K88ad fimbrial adhesin of Escherichia coli in neutral glycosphingolipid preparations from intestinal epithelial cells of K88ad-adhesive pigs, which was absent in preparations from K88ad-nonadhesive pigs. Neither K88ab nor K88ac adhesin variants bound to this neutral glycosphingolipid. Because this receptor is an intestinal glycosphingolipid that binds K88ad adhesin, it has been designated IGLad. Carbohydrate compositional analysis of a partially purified preparation of IGLad identified galactose, glucose, andN-acetylglucosamine in a ratio of 1.5:1.0:0.5 as the major monosaccharides. Preliminary characterization experiments using lectins showed that IGLad contains the terminal glycanic structure Galβ1-4GlcNAc. Removal of terminal β-linked galactose residues from IGLad decreased the recognition of IGLad by the K88ad adhesin, indicating that terminal β-linked galactose is an essential component of the K88ad adhesin recognition site on IGLad. Studies with purified glycosphingolipid standards demonstrated that K88ad adhesin binds to neolactotetraosylceramide (nLc4Cer) (Galβ1-4GlcNAcβ1-3Galβ1-4Glcβ1-1Cer), lactotriosylceramide (GlcNAcβ1-3Galβ1-4Glcβ1-1Cer) and lactotetraosylceramide (Galβ1-3GlcNAcβ1-3Galβ1-4Glcβ1-1Cer). Based on these studies, IGLad appears to be nLc4Cer.
机译:在这项研究中,我们鉴定了在不粘附K88ad的猪的肠上皮细胞中,中性糖鞘脂制剂中的大肠杆菌的K88ad纤维粘附蛋白的受体。 K88ab和K88ac粘附素变体均未结合该中性糖鞘脂。由于该受体是结合K88ad粘附素的肠道糖鞘脂,因此已被称为IGLad。对部分纯化的IGLAd制剂的碳水化合物成分分析确定,半乳糖,葡萄糖和 N -乙酰氨基葡萄糖的比例为1.5:1.0:0.5为主要单糖。使用凝集素的初步表征实验表明,IGLAd含有末端聚糖结构Galβ1-4GlcNAc。从IGLad上除去末端β-连接的半乳​​糖残基会降低K88ad粘附素对IGLad的识别,表明末端β-连接的半乳​​糖是IGLad上K88ad粘附素识别位点的重要组成部分。使用纯化的鞘糖脂标准品进行的研究表明,K88ad粘附素与新乳糖四糖基神经酰胺(nLc 4 Cer)(Galβ1-4GlcNAcβ1-3Galβ1-4Glcβ1-1Cer),乳三糖神经酰胺(GlcNAcβ1-3Galβ1-4Glcβ1-1Cer) -3GlcNAcβ1-3Galβ1-4Glcβ1-1Cer)。根据这些研究,IGLAd似乎是nLc 4 Cer。

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