About: Structural basis for oligosaccharide-mediated adhesion of P. aeruginosa in the lungs of cystic fibrosis patients     Goto   Sponge   NotDistinct   Permalink

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Description
  • The galactose- and fucose-binding (PA-IL and PA-IIL) lectins of Pseudomonas aeruginosa contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis (CF) patients via chronic lung colonisation. CF gene mutations increase cell surface fucosylation and CF patients also display modifications in their respiratory and salivary mucins with a higher percentage of sialylated and sulphated oligosaccharides. These cystic fibrosis mucins and cell surface glycoconjugates carry fucose as the terminal sugar residue. Since the P. aeruginosa lectins have been characterised to reveal an outstandingly high affinity of PA-IIL for fucose, they can serve as binding targets for binding by PA-IIL [1]. Precise three-dimensional knowledge of the lectin sugar binding site, through protein crystallography at high resolution, has allowed the unusually high affinity to be understood and shown a novel sugar binding mode. Subsequent modelling studies, based on the fuc
  • The galactose- and fucose-binding (PA-IL and PA-IIL) lectins of Pseudomonas aeruginosa contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis (CF) patients via chronic lung colonisation. CF gene mutations increase cell surface fucosylation and CF patients also display modifications in their respiratory and salivary mucins with a higher percentage of sialylated and sulphated oligosaccharides. These cystic fibrosis mucins and cell surface glycoconjugates carry fucose as the terminal sugar residue. Since the P. aeruginosa lectins have been characterised to reveal an outstandingly high affinity of PA-IIL for fucose, they can serve as binding targets for binding by PA-IIL [1]. Precise three-dimensional knowledge of the lectin sugar binding site, through protein crystallography at high resolution, has allowed the unusually high affinity to be understood and shown a novel sugar binding mode. Subsequent modelling studies, based on the fuc (en)
  • The galactose- and fucose-binding (PA-IL and PA-IIL) lectins of Pseudomonas aeruginosa contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis (CF) patients via chronic lung colonisation. CF gene mutations increase cell surface fucosylation and CF patients also display modifications in their respiratory and salivary mucins with a higher percentage of sialylated and sulphated oligosaccharides. These cystic fibrosis mucins and cell surface glycoconjugates carry fucose as the terminal sugar residue. Since the P. aeruginosa lectins have been characterised to reveal an outstandingly high affinity of PA-IIL for fucose, they can serve as binding targets for binding by PA-IIL [1]. Precise three-dimensional knowledge of the lectin sugar binding site, through protein crystallography at high resolution, has allowed the unusually high affinity to be understood and shown a novel sugar binding mode. Subsequent modelling studies, based on the fuc (cs)
Title
  • Structural basis for oligosaccharide-mediated adhesion of P. aeruginosa in the lungs of cystic fibrosis patients
  • Structural basis for oligosaccharide-mediated adhesion of P. aeruginosa in the lungs of cystic fibrosis patients (en)
  • Structural basis for oligosaccharide-mediated adhesion of P. aeruginosa in the lungs of cystic fibrosis patients (cs)
skos:prefLabel
  • Structural basis for oligosaccharide-mediated adhesion of P. aeruginosa in the lungs of cystic fibrosis patients
  • Structural basis for oligosaccharide-mediated adhesion of P. aeruginosa in the lungs of cystic fibrosis patients (en)
  • Structural basis for oligosaccharide-mediated adhesion of P. aeruginosa in the lungs of cystic fibrosis patients (cs)
skos:notation
  • RIV/00216224:14310/03:00008868!RIV08-MSM-14310___
http://linked.open.../vavai/riv/strany
  • 61
http://linked.open...avai/riv/aktivita
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  • P(LN00A016)
http://linked.open...vai/riv/dodaniDat
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  • 629184
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  • RIV/00216224:14310/03:00008868
http://linked.open...riv/jazykVysledku
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  • Pseudomonas aeruginosa; lectin; microcalorimetry; crystal structure; cystic fibrosis (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [67D49A0333C5]
http://linked.open...v/mistoKonaniAkce
  • Grenoble, France
http://linked.open...i/riv/mistoVydani
  • Grenoble, France
http://linked.open...i/riv/nazevZdroje
  • 12th European Carbohydrate Symposium
http://linked.open...in/vavai/riv/obor
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http://linked.open...vavai/riv/projekt
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http://linked.open...iv/tvurceVysledku
  • Imberty, Anne
  • Wimmerová, Michaela
  • Gilboa-Garber, Nechama
  • Wu, Albert M.
  • Sabin, Charles
  • Perez, Serge
  • Gautier, Catherine
  • Mitchell, Edward
  • Houles, Corrine
http://linked.open...vavai/riv/typAkce
http://linked.open.../riv/zahajeniAkce
number of pages
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  • CERMAV-CNRS
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  • 14310
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