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Listeria monocytogenes internalins bind to the human intestinal mucin MUC2.

机译:单核细胞增生李斯特氏菌内毒素与人肠道粘蛋白MUC2结合。

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摘要

Listeria monocytogenes cross the intestinal barrier causing systemic infections with high mortality rates. Intestinal infection triggers release of intestinal mucus. We show that three L. monocytogenes internalins, InlB, InlC and InlJ all bound to MUC2 (the major component of intestinal mucus), but not to the cell surface mucin MUC1. Binding was strongest to InlB>InlC>InlJ (P < 0.001). Listerial internalins are characterized by their internalin domain, composed by leucine rich repeats (LRR) followed by an immunogloblin-like region. We report here that the internalin domain of the InlJ protein also bound MUC2, suggesting that an internalin domain is sufficient to bind to MUC2.
机译:单核细胞增生李斯特菌穿过肠道屏障,导致全身感染,死亡率高。肠道感染触发肠道粘液释放。我们显示三个单核细胞增生李斯特菌internalins,InlB,InlC和InlJ都与MUC2(肠道粘液的主要成分)结合,但不与细胞表面粘蛋白MUC1结合。与InlB> InlC> InlJ的结合最强(P <0.001)。李斯特菌内毒素的特征在于其内毒素结构域,该结构域由富含亮氨酸的重复序列(LRR)和免疫球蛋白样区域组成。我们在这里报告,InlJ蛋白的internalin结构域也结合了MUC2,这表明internalin结构域足以结合MUC2。

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