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

Karen W. Dodson, Jerome S. Pinkner, Thierry Rose, Goran Magnusson, Scott J. Hultgren, Gabriel Waksman

Research output: Contribution to journalArticlepeer-review

211 Scopus citations

Abstract

PapG is the adhesin at the tip of the P pilus that mediates attachment of uropathogenic Escherichia coli to the uroepithelium of the human kidney. The human specific allele of PapG binds to globoside (GbO4), which consists of the tetrasaccharide GalNAcβ1-3Galα1-4Galβ1-4Glc linked to ceramide. Here, we present the crystal structures of a binary complex of the PapG receptor binding domain bound to GbO4 as well as the unbound form of the adhesin. The biological importance of each of the residues involved in binding was investigated by site-directed mutagenesis. These studies provide a molecular snapshot of a host-pathogen interaction that determines the tropism of uropathogenic E. coli for the human kidney and is critical to the pathogenesis of pyelonephritis.

Original languageEnglish
Pages (from-to)733-743
Number of pages11
JournalCell
Volume105
Issue number6
DOIs
StatePublished - Jun 15 2001

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