Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00009310" target="_blank" >RIV/00216224:14310/03:00009310 - 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

Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions

Popis výsledku v původním jazyce

Human pathogenic bacteria Pseudomonas aeruginosa colonize patients with a number of chronic lung diseases and is a major cause of morbidity and mortality in cystic fibrosis patients. Specific oligosaccharide-mediated recognition and adhesion are key points in the initiating steps of the P. aeruginosa infection. The bacterium produces two sugar-recognising proteins PA-IL (LecA) and PA-IIL (LecB), galactose- and fucose-binding lectins respectively, that can play a crucial role in adhesion and specific recognition of a host by the pathogen and contribute to its virulence. Recently, the crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A[1]. P. aeruginosa expresses these lectins under stressed conditions that limit their in vitro production for further structure-functional characterisation. Therefore, both lecA and lecB genes were cloned into pET25 vector, expressed in E.coli BL21(DE3) cells as host organism and purified by affinity chromatography on Sepharose 4B and

Název v anglickém jazyce

Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions

Popis výsledku anglicky

Human pathogenic bacteria Pseudomonas aeruginosa colonize patients with a number of chronic lung diseases and is a major cause of morbidity and mortality in cystic fibrosis patients. Specific oligosaccharide-mediated recognition and adhesion are key points in the initiating steps of the P. aeruginosa infection. The bacterium produces two sugar-recognising proteins PA-IL (LecA) and PA-IIL (LecB), galactose- and fucose-binding lectins respectively, that can play a crucial role in adhesion and specific recognition of a host by the pathogen and contribute to its virulence. Recently, the crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A[1]. P. aeruginosa expresses these lectins under stressed conditions that limit their in vitro production for further structure-functional characterisation. Therefore, both lecA and lecB genes were cloned into pET25 vector, expressed in E.coli BL21(DE3) cells as host organism and purified by affinity chromatography on Sepharose 4B and

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ME%20675" target="_blank" >ME 675: Strukturně- funkční studie lektinů bakteriálních patogenů</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

2003

Kód důvěrnosti údajů

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

Název statě ve sborníku

European Congress of Young Chemists

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

70

Název nakladatele

Chemical Scientific Set "Flogiston", Warsaw University of Technology

Místo vydání

Warsaw

Místo konání akce

Zakopane

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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