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Structural requirements for the glycolipid receptor of human uropathogenic Escherichia coli
Author(s) -
Striker Robert,
Nilsson Ulf,
Stonecipher Andrea,
Magnusson Göran,
Hultgren Scott J.
Publication year - 1995
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1995.tb02327.x
Subject(s) - biology , escherichia coli , glycolipid , microbiology and biotechnology , receptor , biochemistry , gene
Summary The binding of uropathogenic Escherichia coli to the globo series of glycolipids via P pili is a critical step in the infectious process that is mediated by a human‐specific PapG adhesin. Three classes of PapG adhesins exist with different binding specificities to Galα4Gal‐containing glycolipids. The structural basis for PapG recognition of the human glycolipid receptor globoside was investigated by using soluble saccharide analogues as inhibitors of bacterial haemagglutination. The minimum binding epitope was confirmed as the Galα4Gal moiety, but parts of the GalNAcβ and glucose residues, which flank the Galα4Gal in globoside (GbO 4 ), were also shown to be important for strong binding. Furthermore, the same five hydroxyl groups of Galα4Gal in globotriasyl ceramide that were recognized by a previously characterized PapG variant were also recognized by the human‐specific PapG in binding the GbO 4 that dominates In the human kidney. Saccharide analogues that blocked haemagglutination also blocked the adherence of human uropathogenic E. coli to human kidney sections. Knowledge of the molecular details of the PapG‐GbO 4 interaction will make it possible to design antiadherence therapeutics.