Structural basis for oligosaccharide-mediated adhesion of P. aeruginosa in the lungs of cystic fibrosis patients

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00008868" target="_blank" >RIV/00216224:14310/03:00008868 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Structural basis for oligosaccharide-mediated adhesion of P. aeruginosa in the lungs of cystic fibrosis patients
Original language 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,
Czech name
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Czech description
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Project
<a href="/en/project/LN00A016" target="_blank" >LN00A016: BIOMOLECULAR CENTER</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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