The solution structure of PapGII from uropathogenic Escherichia coli and its recognition of glycolipid receptors.

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 Rep

journal_title

EMBO reports

authors

Sung MA,Fleming K,Chen HA,Matthews S

doi

10.1093/embo-reports/kve133

keywords:

subject

Has Abstract

pub_date

2001-07-01 00:00:00

pages

621-7

issue

7

eissn

1469-221X

issn

1469-3178

pii

kve133

journal_volume

2

pub_type

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