PA-IIL lektin z Pseudomonas aeuruginosa:klonování, exprese, mutageneze, krystalizace a termodynamická charakterizace

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00010509" target="_blank" >RIV/00216224:14310/04:00010509 - 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

Pseudomonas aeruginosa lectin PA-IIL: cloning, expression, mutation, crystallisation and thermodynamic characterisation

Popis výsledku v původním jazyce

Pseudomonas aeruginosa is an opportunistic pathogen. Chronic lung colonisation by the bacterium is the major cause of morbidity and mortality in cystic fibrosis patients. Identification of the molecules involved in this pathogen specific recognition of the modified host cell components is of therapeutic interest. 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 [1]. For further structure-functional characterisation, the lecB gene was cloned into pET25 vector, the recombinant protein was expressed in E. coli BL21(DE3) cells and purified byaffinity chromatography. Isothermal titration microcalorimetry experiments confirmed unusually high affinity of the PA-IIL lectin for monosaccharides (KA = 0.3 x 106 M-1 for L-fucose). Crystal structure of the PA-IIL/fucose complex reveal

Název v anglickém jazyce

Pseudomonas aeruginosa lectin PA-IIL: cloning, expression, mutation, crystallisation and thermodynamic characterisation

Popis výsledku anglicky

Pseudomonas aeruginosa is an opportunistic pathogen. Chronic lung colonisation by the bacterium is the major cause of morbidity and mortality in cystic fibrosis patients. Identification of the molecules involved in this pathogen specific recognition of the modified host cell components is of therapeutic interest. 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 [1]. For further structure-functional characterisation, the lecB gene was cloned into pET25 vector, the recombinant protein was expressed in E. coli BL21(DE3) cells and purified byaffinity chromatography. Isothermal titration microcalorimetry experiments confirmed unusually high affinity of the PA-IIL lectin for monosaccharides (KA = 0.3 x 106 M-1 for L-fucose). Crystal structure of the PA-IIL/fucose complex reveal

Druh

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

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 periodika

European Journal of Biochemistry

ISSN

0014-2956

e-ISSN

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Svazek periodika

Supplement

Číslo periodika v rámci svazku

S1

Stát vydavatele periodika

PL - Polská republika

Počet stran výsledku

2

Strana od-do

154-155

Kód UT WoS článku

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EID výsledku v databázi Scopus

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