...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Infection and immunity >The Established Intimin Receptor Tir and the Putative Eucaryotic Intimin Receptors Nucleolin and β1 Integrin Localize at or near the Site of Enterohemorrhagic Escherichia coli O157:H7 Adherence to Enterocytes In Vivo
【24h】

The Established Intimin Receptor Tir and the Putative Eucaryotic Intimin Receptors Nucleolin and β1 Integrin Localize at or near the Site of Enterohemorrhagic Escherichia coli O157:H7 Adherence to Enterocytes In Vivo

机译：建立的Intimin受体Tir和推定的真核细胞内Intimin受体Nucleolin和β1整联蛋白位于肠出血性大肠杆菌O157：H7或与肠道细胞粘附的部位附近

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

For enterohemorrhagic Escherichia coli (EHEC) O157:H7 to adhere tightly to the intestinal epithelium and produce attach and efface (A/E) lesions, the organism must express the adhesin intimin and insert the bacterially encoded translocated intimin receptor Tir into the plasma membrane of the host enterocyte. Additionally, some reports based on tissue culture experiments indicate that intimin has affinity for the eucaryotic proteins nucleolin and β1 integrin. To address the potential biological relevance of these eucaryotic proteins in the infection process in vivo, we sought to compare the proximity of Tir, nucleolin, and β1 integrin to regions of EHEC O157:H7 attachment in intestinal sections from three different inoculated animals: piglets, neonatal calves, and mice. Piglets and neonatal calves were chosen because intimin-mediated adherence of EHEC O157:H7 and subsequent A/E lesion formation occur at high levels in these animals. Mice were selected because of their ease of manipulation but only after we first demonstrated that in competition with the normal mouse gut flora, an EHEC O157:H7 strain with a nonpolar deletion in the intimin gene was cleared faster than strains that produced wild-type or hybrid intimin. In all three animal species, we noted immunostained Tir beneath and stained nucleolin closely associated with adherent bacteria in intestinal sections. We also observed immunostained β1 integrin clustered at locations of bacterial adherence in porcine and bovine tissue. These findings indicate that nucleolin and β1 integrin are present on the luminal surface of intestinal epithelia and are potentially accessible as receptors for intimin during EHEC O157:H7 infection.
机译：为了使肠出血性大肠杆菌（EHEC）O157：H7紧密粘附在肠上皮上并产生 a ttatta和 e fface（A / E）病灶，生物体必须表达粘附素内膜素，并将细菌编码的 t 重新定位的 i ntimin r 受体Tir插入宿主肠上皮细胞的质膜。此外，一些基于组织培养实验的报道表明，intimin对真核蛋白核仁素和β1整联蛋白具有亲和力。为了解决这些真核蛋白在体内感染过程中的潜在生物学相关性，我们试图比较Tir，核仁素和β1整合素与EHEC O157：H7附着区域之间的距离，这些区域来自三种不同接种动物的肠段：仔猪，新生小牛和老鼠。之所以选择仔猪和小牛犊，是因为这些动物中内因素介导的EHEC O157：H7依从性和随后的A / E病变形成率很高。选择小鼠的原因是它们易于操作，但只有在我们首先证明与正常小鼠肠道菌群竞争后，内膜素基因中非极性缺失的EHEC O157：H7菌株的清除速度比产生野生型或野生型的小鼠要快。混合内膜蛋白。在所有这三种动物中，我们注意到肠道切片下方的免疫染色Tir和染色的核仁素与粘附细菌密切相关。我们还观察到免疫染色的β1整联蛋白聚集在猪和牛组织中细菌粘附的位置。这些发现表明，核仁蛋白和β1整联蛋白存在于肠上皮的腔表面，在EHEC O157：H7感染期间可能作为内膜素的受体被利用。

著录项

相似文献

  • 外文文献
  • 中文文献
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号