The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks
The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks
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DOI：
10.1099/mic.0.26721-0
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发表时间：
2004-06-01
期刊：
影响因子：
2.8
通讯作者：
Wren, BW
中科院分区：
文献类型：
--
作者：
Karlyshev, AV;Everest, P;Wren, BW
最近的研究表明，肠道病原体空肠弯曲杆菌具有 N 连接的一般蛋白质糖基化途径 (Pgl)，可以修饰该生物体的许多蛋白质。为了确定空肠弯曲菌中 N 连接一般糖基化的作用，作者研究了 pglH 基因，该基因与糖转移酶家族高度相似。在菌株81116和11168H中构建了pglH突变体。两种突变体都被证明在糖基化许多空肠弯曲菌蛋白质的能力方面存在缺陷，但它们的脂寡糖和荚膜不受影响。 pglH突变体粘附和侵入人上皮Caco-2细胞的能力显着降低。此外，81116 pglH 突变体在雏鸡中定植的能力受到严重影响。这些结果表明糖基化对于空肠弯曲菌与人和鸡宿主细胞的附着很重要，并且暗示糖蛋白在空肠弯曲菌的发病机制中的作用。
It has recently been shown that the enteropathogen Campylobacter jejuni has an N-linked general protein glycosylation pathway (Pgl) that modifies many of the organism's proteins. To determine the role of the N-linked general glycosylation in C jejuni, the authors studied the pglH gene, which shows high similarity to a family of sugar transferases. pglH mutants were constructed in strains 81116 and 11168H. Both mutants were shown to be deficient in their ability to glycosylate a number of C. jejuni proteins, but their lipooligosaccharide and capsule were unaffected. The pglH mutants had significantly reduced ability to adhere to and invade human epithelial Caco-2 cells. Additionally, the 81116 pglH mutant was severely affected in its ability to colonize chicks. These results suggest that glycosylation is important for the attachment of C. jejuni to human and chicken host cells and imply a role for glycoproteins in the pathogenesis of C. jejuni.