PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria

Kód výsledku v IS VaVaI

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Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria

Popis výsledku v původním jazyce

Enormous potential of sugar structures gives them a crucial importance in recognition and signalling events. Carbohydrate-mediated recognition plays an important role in the ability of parasitic organisms to adhere to the surface of the host cell in thefirst step of their invasion and infectivity. For example, Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients [1,2]. Moreover, the PA-IIL lectin displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. This characteristics is correlated to the remarkable presence of two calcium ions in the binding siteof the protein [3]. Database searching in newly sequenced bacterial genomes revealed the presence of PA-IIL like proteins within a limited number of other opportunistic pathogens. All of them are soil inhabitants, are phylogenetically rel

Název v anglickém jazyce

PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria

Popis výsledku anglicky

Enormous potential of sugar structures gives them a crucial importance in recognition and signalling events. Carbohydrate-mediated recognition plays an important role in the ability of parasitic organisms to adhere to the surface of the host cell in thefirst step of their invasion and infectivity. For example, Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients [1,2]. Moreover, the PA-IIL lectin displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. This characteristics is correlated to the remarkable presence of two calcium ions in the binding siteof the protein [3]. Database searching in newly sequenced bacterial genomes revealed the presence of PA-IIL like proteins within a limited number of other opportunistic pathogens. All of them are soil inhabitants, are phylogenetically rel

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název statě ve sborníku

Chemica 43S

ISBN

80-244-0882-1

ISSN

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e-ISSN

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Počet stran výsledku

2

Strana od-do

72-73

Název nakladatele

Ceska spolecnost pro biochemii a molekularni biologii

Místo vydání

Olomouc

Místo konání akce

Olomouc

Datum konání akce

31. 8. 2004

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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