Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor

Citation
Kw. Dodson et al., Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor, CELL, 105(6), 2001, pp. 733-743
Citations number
48
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELL
ISSN journal
0092-8674 → ACNP
Volume
105
Issue
6
Year of publication
2001
Pages
733 - 743
Database
ISI
SICI code
0092-8674(20010615)105:6<733:SBOTIO>2.0.ZU;2-C
Abstract
PapG is the adhesin at the tip of the P pilus that mediates attachment of u ropathogenic Escherichia coli to the uroepithelium of the human kidney. The human specific allele of PapG binds to globoside (GbO4), which consists of the tetrasaccharide GalNAc beta1-3Gal alpha1-4Gal beta1-4Glc linked to cer amide. Here, we present the crystal structures of a binary complex of the P apG receptor binding domain bound to GbO4 as well as the unbound form of th e adhesin. The biological importance of each of the residues involved in bi nding was investigated by site-directed mutagenesis. These studies provide a molecular snapshot of a host-pathogen interaction that determines the tro pism of uropathogenic E. coli for the human kidney and is critical to the p athogenesis of pyelonephritis.