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首页> 外文期刊>Infection and immunity >Proteus mirabilis mannose-resistant, Proteus-like fimbriae: MrpG is located at the fimbrial tip and is required for fimbrial assembly.
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Proteus mirabilis mannose-resistant, Proteus-like fimbriae: MrpG is located at the fimbrial tip and is required for fimbrial assembly.

机译：变形杆菌对甘露糖有抗性，变形杆菌样菌毛：MrpG位于菌毛尖端，是菌丝组装所必需的。

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摘要

The mannose-resistant, Proteus-like (MR/P) fimbria, responsible for mannose-resistant hemagglutination, is a virulence factor for uropathogenic Proteus mirabilis. Based on known fimbrial gene organization, we postulated that MrpG, a putative minor subunit of the MR/P fimbria, functions as an adhesin responsible for hemagglutination, while MrpA serves as the major structural subunit for the filamentous structure. To test this hypothesis, an mrpG mutant was constructed by allelic-exchange mutagenesis and verified by PCR and Southern blotting. The mrpG mutant was found to be negative for hemagglutination, while wild-type strain H14320 and the complemented mutant were positive. Western blots with antiserum raised against an overexpressed MrpG'-His6 fusion protein showed that MrpG was present in the fimbrial preparations of both the wild-type strain and the complemented mutant but absent in that of the mrpG mutant. The mrpG mutant was significantly less virulent in a CBA mouse model of ascending urinary tract infection. Western blots with antiserum to whole MR/P fimbriae showed that MrpA protein was also missing from the fimbrial preparation of the mrpG mutant. Using immunogold electron microscopy, we found that the normal MR/P-fimbrial structure was absent in the mrpG mutant, suggesting that MrpG is essential for initiation of normal fimbrial formation. In the wild-type strain, MrpG protein was localized to the tips of the fimbriae or at the surface of the cell when antiserum raised against overexpressed MrpG was used. Given the tip localization, MrpG may be required for initiation of assembly of MR/P fimbriae but does not appear to be the fimbrial adhesin.
机译：抗甘露糖，类变形杆菌（MR / P）菌毛负责抗甘露糖的血凝反应，是尿路致病性变形杆菌变形杆菌的致病因子。基于已知的纤维基因组织，我们推测MrpG是MR / P菌毛的假定的次要亚基，起负责血凝作用的粘附素的作用，而MrpA则是丝状结构的主要结构亚基。为了验证该假设，通过等位基因交换诱变构建了mrpG突变体，并通过PCR和Southern印迹进行了验证。发现mrpG突变体血凝反应阴性，而野生型菌株H14320和互补突变体为阳性。用针对过度表达的MrpG'-His6融合蛋白产生的抗血清进行的蛋白质印迹表明，MrppG存在于野生型菌株和互补突变体的纤维制品中，但在mrpG突变体的纤维制品中均不存在。在升尿路感染的CBA小鼠模型中，mrpG突变体的毒性明显较低。对整个MR / P菌毛有抗血清的蛋白质印迹表明，mrpG突变体的纤维制品中也缺少MrpA蛋白。使用免疫金电子显微镜，我们发现在mrpG突变体中不存在正常的MR / P膜结构，这表明MrpG对于启动正常的纤维形成至关重要。在野生型菌株中，当使用针对过度表达的MrpG的抗血清时，MrpG蛋白位于菌毛尖端或细胞表面。给定尖端的定位，可能需要MrpG来启动MR / P菌毛的组装，但它似乎不是纤维粘附素。

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