PA-IIL like lectins: společný znak vysoké adaptability některých podmíněných patogenů

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00010504" target="_blank" >RIV/00216224:14310/04:00010504 - 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

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 (PA-IL and PA-IIL) lectins contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients [1]. Moreover, the PA-IIL lectin displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. Database searching in newly sequenced genomes revealed the presence of PA-IIL like proteins within someother opportunistic pathogens. Most of them comes from soil, are phylogenetically related and in past were usually considered as Pseudomonas spp. In addition to the pseudomonas lectin PA-IIL, we have been focused to its homologs coming fr

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 (PA-IL and PA-IIL) lectins contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients [1]. Moreover, the PA-IIL lectin displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. Database searching in newly sequenced genomes revealed the presence of PA-IIL like proteins within someother opportunistic pathogens. Most of them comes from soil, are phylogenetically related and in past were usually considered as Pseudomonas spp. In addition to the pseudomonas lectin PA-IIL, we have been focused to its homologs coming fr

Druh

D - Stať ve sborníku

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)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název statě ve sborníku

Acta Univ. Palacki. Olomouc., Fac. Rer. Nat., Chemica 43S

ISBN

80-244-0353-6

ISSN

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e-ISSN

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Počet stran výsledku

2

Strana od-do

72-73

Název nakladatele

Univerzita Palackého

Místo vydání

Olomouc

Místo konání akce

Olomouc

Datum konání akce

1. 1. 2004

Typ akce podle státní příslušnosti

CST - Celostátní akce

Kód UT WoS článku

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