F9 fimbriae of uropathogenic Escherichia coli are expressed at low temperature and recognise Galβ1-3GlcNAc-containing glycans.

F9 fimbriae of uropathogenic Escherichia coli are expressed at low temperature and recognise Galβ1-3GlcNAc-containing glycans.
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DOI:
10.1371/journal.pone.0093177
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发表时间:
2014
期刊:
影响因子:
3.7
通讯作者:
Schembri MA
Schembri MA
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Wurpel DJ;Totsika M;Allsopp LP;Hartley-Tassell LE;Day CJ;Peters KM;Sarkar S;Ulett GC;Yang J;Tiralongo J;Strugnell RA;Jennings MP;Schembri MA

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尿路致病性大肠杆菌(UPEC)是发达国家尿路感染(UTI)的主要病原体。在UPEC的主要毒力因子中,表面表达的粘附素介导粘附和组织嗜性。UPEC菌株通常具有一系列粘附素,其中1型菌毛和伴侣-usher类的P菌毛最具特征。我们以前确定和表征F9作为一个新的伴侣-引导伞类型,介导生物膜的形成。然而,在野生型临床UPEC菌株的背景下,F9菌毛的调节和特异性作用仍有待确定。在这项研究中,我们评估了f9操纵子在不同的大肠杆菌中的分布和遗传背景。大肠杆菌谱系和致病型,并证明f9基因是显着更保守的UPEC菌株收集相比,明确定义的E.大肠杆菌参考(ECOR)收集。在原型UPEC菌株CFT 073中,全局调节蛋白H-NS通过其直接结合f9启动子区域的能力被鉴定为在37°C下f9基因表达的转录阻遏物。F9菌毛表达在20°C下得到证实,这是野生型E.杆菌最后,聚糖阵列分析表明F9菌毛识别并结合末端Galβ1-3GlcNAc结构。
Uropathogenic Escherichia coli (UPEC) is the leading causative agent of urinary tract infections (UTI) in the developed world. Among the major virulence factors of UPEC, surface expressed adhesins mediate attachment and tissue tropism. UPEC strains typically possess a range of adhesins, with type 1 fimbriae and P fimbriae of the chaperone-usher class the best characterised. We previously identified and characterised F9 as a new chaperone-usher fimbrial type that mediates biofilm formation. However, the regulation and specific role of F9 fimbriae remained to be determined in the context of wild-type clinical UPEC strains. In this study we have assessed the distribution and genetic context of the f9 operon among diverse E. coli lineages and pathotypes and demonstrated that f9 genes are significantly more conserved in a UPEC strain collection in comparison to the well-defined E. coli reference (ECOR) collection. In the prototypic UPEC strain CFT073, the global regulator protein H-NS was identified as a transcriptional repressor of f9 gene expression at 37°C through its ability to bind directly to the f9 promoter region. F9 fimbriae expression was demonstrated at 20°C, representing the first evidence of functional F9 fimbriae expression by wild-type E. coli. Finally, glycan array analysis demonstrated that F9 fimbriae recognise and bind to terminal Galβ1-3GlcNAc structures.
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