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

Kód výsledku v 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>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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,

Název v anglickém jazyce

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

Popis výsledku anglicky

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,

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2003

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

12th European Carbohydrate Symposium

ISBN

—

ISSN

—

e-ISSN

—

Počet stran výsledku

1

Strana od-do

61

Název nakladatele

CERMAV-CNRS

Místo vydání

Grenoble, France

Místo konání akce

Grenoble, France

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

—