ยท
K.W. Dodson, J.S. Pinkner, T. Rose, G. Magnusson, S.J. Hultgren, and G.
Waksman.
Structural basis of the interaction of the pyelonephritic E. coli adhesin for
its human kidney receptor
Cell. 105:733-743. (2001)
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 GalNAcbeta1-
3Galalpha1-4Galbeta1-4Glc linked to ceramide. Here, we present the crystal
structure of a binary complex of the PapG receptor-binding domain bound to GbO4
as well as that of the unbound form of the protein. 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 selectivity of uropathogenic E. coli for the
human kidney and is critical to the pathogenesis of pyelonephritis.