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Structural requirements for the glycolipid receptor of human uropathogenic Escherichia coli

Striker, Robert ; Nilsson, Ulf LU ; Stonecipher, Andrea ; Magnusson, Göran LU and Hultgren, Scott J. (1995) In Molecular Microbiology 16(5). p.1021-1029
Abstract

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 (GbO4), were also shown to be important for strong binding. Furthermore, the same five hydroxyl... (More)

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 (GbO4), 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 GbO4 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‐GbO4 interaction will make it possible to design antiadherence therapeutics.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
16
issue
5
pages
9 pages
publisher
Wiley-Blackwell
external identifiers
  • pmid:7476178
  • scopus:0029147944
ISSN
0950-382X
DOI
10.1111/j.1365-2958.1995.tb02327.x
language
English
LU publication?
yes
id
3e3f2b27-5bb6-45e7-b09d-dbde847cc165
date added to LUP
2023-02-07 09:47:13
date last changed
2024-01-03 22:02:27
@article{3e3f2b27-5bb6-45e7-b09d-dbde847cc165,
  abstract     = {{<p>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<sub>4</sub>), 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<sub>4</sub> 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<sub>4</sub> interaction will make it possible to design antiadherence therapeutics.</p>}},
  author       = {{Striker, Robert and Nilsson, Ulf and Stonecipher, Andrea and Magnusson, Göran and Hultgren, Scott J.}},
  issn         = {{0950-382X}},
  language     = {{eng}},
  number       = {{5}},
  pages        = {{1021--1029}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Molecular Microbiology}},
  title        = {{Structural requirements for the glycolipid receptor of human uropathogenic <i>Escherichia coli</i>}},
  url          = {{http://dx.doi.org/10.1111/j.1365-2958.1995.tb02327.x}},
  doi          = {{10.1111/j.1365-2958.1995.tb02327.x}},
  volume       = {{16}},
  year         = {{1995}},
}