Sung M A, Fleming K, Chen H A, Matthews S
Centre for Structural Biology and Department of Biochemistry, Imperial College of Science, Technology and Medicine, Exhibition Road, South Kensington, London SW7 2AY, UK.
EMBO Rep. 2001 Jul;2(7):621-7. doi: 10.1093/embo-reports/kve133. Epub 2001 Jul 3.
Uropathogenic Escherichia coli (UPEC) is the primary cause of symptomatic urinary tract infection. The P-pili, a bacterial surface organelle, mediates the bacterial host--cell adhesion. The PapG adhesin has generated much interest in recent years, not only because of its clinical value, i.e. in the prevention of microbial adherence, but also because of its ability to promote virulence. Using multidimensional nuclear magnetic resonance (NMR) and deuteration we have determined the solution structure of the adhesin domain from PapGII (PapGII-198). The novel structure of PapGII-198 is composed of a large elongated jellyroll motif. Despite an automated search of the structural database failing to reveal any similar proteins, PapGII adhesin shares some structural similarities with FimH. Furthermore, interpretation of NMR-titration data has enabled us to identify the putative binding site for the globoseries of oligosaccharides. This work provides insight into UPEC pathogenesis as well as aiding the development of preventative therapies and the guidance of future mutagenesis programmes.
尿路致病性大肠杆菌（UPEC）是有症状性尿路感染的主要病因。P菌毛作为一种细菌表面细胞器，介导细菌与宿主细胞的黏附。近年来，PapG黏附素引起了广泛关注，这不仅是因为其临床价值，即预防微生物黏附，还因为其促进毒力的能力。利用多维核磁共振（NMR）和氘化技术，我们确定了PapGII（PapGII-198）黏附素结构域的溶液结构。PapGII-198的新结构由一个大的细长果冻卷基序组成。尽管对结构数据库进行自动搜索未能发现任何相似蛋白质，但PapGII黏附素与FimH在结构上有一些相似之处。此外，对NMR滴定数据的解释使我们能够确定寡糖球系列的假定结合位点。这项工作有助于深入了解UPEC的发病机制，以及辅助预防性治疗的开发和指导未来的诱变计划。
