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Quantitative studies of the binding of the class II PapG adhesin from uropathogenic Escherichia coli to oligosaccharides.

Larsson, A; Ohlsson, Jörgen LU ; Dodson, K W; Hultgren, S J; Nilsson, Ulf LU and Kihlberg, J (2003) In Bioorganic & Medicinal Chemistry 11(10). p.2255-2261
Abstract
Binding of the class II PapG adhesin, found at the tip of filamentous pili on Escherichia coli, to the carbohydrate moiety of globoseries glycolipids in the human kidney is a key step in development of pyelonephritis, a severe form of urinary tract infection. An assay based on surface plasmon resonance for quantification of the binding of the class II PapG adhesin to oligosaccharides has been developed. Using this assay dissociation constants ranging from 80 to 540 M were determined for binding of the PapG adhesin to di-pentasaccharide fragments from the globoseries of glycolipids. A series of galabiose derivatives, modified at the anomeric position, O-2′ or O-3′, was also investigated. The anomeric position appeared to be the most... (More)
Binding of the class II PapG adhesin, found at the tip of filamentous pili on Escherichia coli, to the carbohydrate moiety of globoseries glycolipids in the human kidney is a key step in development of pyelonephritis, a severe form of urinary tract infection. An assay based on surface plasmon resonance for quantification of the binding of the class II PapG adhesin to oligosaccharides has been developed. Using this assay dissociation constants ranging from 80 to 540 M were determined for binding of the PapG adhesin to di-pentasaccharide fragments from the globoseries of glycolipids. A series of galabiose derivatives, modified at the anomeric position, O-2′ or O-3′, was also investigated. The anomeric position appeared to be the most promising for development of improved inhibitors of PapG-mediated adhesion of E. coli. p-Methoxyphenyl galabioside was found to be most potent (Kd=140 M), and binds to PapG almost as well as the Forssman pentasaccharide. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Bioorganic & Medicinal Chemistry
volume
11
issue
10
pages
2255 - 2261
publisher
Elsevier
external identifiers
  • wos:000182794200014
  • pmid:12713835
  • scopus:0344490325
ISSN
0968-0896
DOI
10.1016/S0968-0896(03)00114-7
language
English
LU publication?
yes
id
a23df687-bbf6-47d8-aec1-7129e2253830 (old id 127945)
date added to LUP
2007-07-10 12:25:35
date last changed
2018-01-07 05:47:06
@article{a23df687-bbf6-47d8-aec1-7129e2253830,
  abstract     = {Binding of the class II PapG adhesin, found at the tip of filamentous pili on Escherichia coli, to the carbohydrate moiety of globoseries glycolipids in the human kidney is a key step in development of pyelonephritis, a severe form of urinary tract infection. An assay based on surface plasmon resonance for quantification of the binding of the class II PapG adhesin to oligosaccharides has been developed. Using this assay dissociation constants ranging from 80 to 540 M were determined for binding of the PapG adhesin to di-pentasaccharide fragments from the globoseries of glycolipids. A series of galabiose derivatives, modified at the anomeric position, O-2′ or O-3′, was also investigated. The anomeric position appeared to be the most promising for development of improved inhibitors of PapG-mediated adhesion of E. coli. p-Methoxyphenyl galabioside was found to be most potent (Kd=140 M), and binds to PapG almost as well as the Forssman pentasaccharide.},
  author       = {Larsson, A and Ohlsson, Jörgen and Dodson, K W and Hultgren, S J and Nilsson, Ulf and Kihlberg, J},
  issn         = {0968-0896},
  language     = {eng},
  number       = {10},
  pages        = {2255--2261},
  publisher    = {Elsevier},
  series       = {Bioorganic & Medicinal Chemistry},
  title        = {Quantitative studies of the binding of the class II PapG adhesin from uropathogenic Escherichia coli to oligosaccharides.},
  url          = {http://dx.doi.org/10.1016/S0968-0896(03)00114-7},
  volume       = {11},
  year         = {2003},
}