Strukturni zaklad interakci mezi proteinem PA-IIL z Pseudomona aeruginosa a mlecnymi oligosacharidy

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00013769" target="_blank" >RIV/00216224:14310/05:00013769 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Structural basis for the interaction between human milk oligosaccharides and a bacterial protein, Pseudomonas aeruginosa lectin PA-IIL,

Popis výsledku v původním jazyce

One of the mechanisms contributing to breast-feeding protection of the newborn against enteric diseases is related to the ability of human milk oligosaccharides to prevent attachment of pathogenic bacteria to the duodenual epithelium. Indeed, a variety of fucosylated oligosaccharides, specific to human milk, form part of the innate immune system. In this study, we demonstrate the specific blocking of PA-IIL, a fucose-binding lectin of the human pathogen Pseudomonas aeruginosa by milk oligosaccharides. Two fucosylated epitopes, Lewis a and 3-fucosyllactose (Lewis x glucose analogue) bind to the lectin with dissociation constants of 2.2 10-7 M and 3.6 10-7 M, respectively. Thermodynamic studies indicate that these interactions are dominated by enthalpy.The entropy contribution is slightly favourable when binding to fucose and to the highest affinity ligand, Lewis a. The high resolution X-ray structures of two complexes of PA-IIL with milk oligosaccharides allow the precise determination

Název v anglickém jazyce

Structural basis for the interaction between human milk oligosaccharides and a bacterial protein, Pseudomonas aeruginosa lectin PA-IIL,

Popis výsledku anglicky

One of the mechanisms contributing to breast-feeding protection of the newborn against enteric diseases is related to the ability of human milk oligosaccharides to prevent attachment of pathogenic bacteria to the duodenual epithelium. Indeed, a variety of fucosylated oligosaccharides, specific to human milk, form part of the innate immune system. In this study, we demonstrate the specific blocking of PA-IIL, a fucose-binding lectin of the human pathogen Pseudomonas aeruginosa by milk oligosaccharides. Two fucosylated epitopes, Lewis a and 3-fucosyllactose (Lewis x glucose analogue) bind to the lectin with dissociation constants of 2.2 10-7 M and 3.6 10-7 M, respectively. Thermodynamic studies indicate that these interactions are dominated by enthalpy.The entropy contribution is slightly favourable when binding to fucose and to the highest affinity ligand, Lewis a. The high resolution X-ray structures of two complexes of PA-IIL with milk oligosaccharides allow the precise determination

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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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)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

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

Název periodika

Biochemical Journal

ISSN

0264-6021

e-ISSN

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Svazek periodika

389

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

325-332

Kód UT WoS článku

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EID výsledku v databázi Scopus

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