Specificity and affinity modulation of PA-IIL lectin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F11%3A00050179" target="_blank" >RIV/00216224:14740/11:00050179 - 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

Specificity and affinity modulation of PA-IIL lectin

Popis výsledku v původním jazyce

Pseudomonas aeruginosa is a clinically important pathogen, which is responsible for numerous nosocomial infections in immunocompromised patients. The bacterium colonises patients with chronic lung diseases and its infection is fatal in cystic fibrosis patients. P. aeruginosa produces high levels of D galactose and L-fucose binding lectins, PA-IL (LecA) and PA-IIL (LecB) respectively, which are associated with its cytotoxic virulence and could be involved in primary recognition of the host organism and in biofilm formation.Additional experiments have been performed to order to understand the molecular basis of both specificity and affinity of PA-IIL for monosaccharides. Three single point mutants in position 22-23-24 have prepared and structure-functioned characterized. The mutated amino acids belong to the ?specificity-binding loop?. The in vitro mutagenesis in combination with computational methods allowed the key importance of amino acid 22 for the specificity of the lectin to be ide

Název v anglickém jazyce

Specificity and affinity modulation of PA-IIL lectin

Popis výsledku anglicky

Pseudomonas aeruginosa is a clinically important pathogen, which is responsible for numerous nosocomial infections in immunocompromised patients. The bacterium colonises patients with chronic lung diseases and its infection is fatal in cystic fibrosis patients. P. aeruginosa produces high levels of D galactose and L-fucose binding lectins, PA-IL (LecA) and PA-IIL (LecB) respectively, which are associated with its cytotoxic virulence and could be involved in primary recognition of the host organism and in biofilm formation.Additional experiments have been performed to order to understand the molecular basis of both specificity and affinity of PA-IIL for monosaccharides. Three single point mutants in position 22-23-24 have prepared and structure-functioned characterized. The mutated amino acids belong to the ?specificity-binding loop?. The in vitro mutagenesis in combination with computational methods allowed the key importance of amino acid 22 for the specificity of the lectin to be ide

Druh

O - Ostatní výsledky

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GPP207%2F11%2FP185" target="_blank" >GPP207/11/P185: Příprava lektinů s vysokou specifitou a afinitou</a><br>

Návaznosti

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

Rok uplatnění

2011

Kód důvěrnosti údajů

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