Abstract:
: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.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Sung MA,Fleming K,Chen HA,Matthews Sdoi
10.1093/embo-reports/kve133keywords:
subject
Has Abstractpub_date
2001-07-01 00:00:00pages
621-7issue
7eissn
1469-221Xissn
1469-3178pii
kve133journal_volume
2pub_type
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