Termodynamika a struktura lektinu Pseudomonas aeruginosa a jejich interakce s lidskými glykokonjugáty

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00021389" target="_blank" >RIV/00216224:14310/05:00021389 - isvavai.cz</a>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Thermodynamic and structures of Pseudomonas aeruginosa lectins and their interaction with complex human glycoconjugates

Popis výsledku v původním jazyce

Carbohydrate-mediated recognition plays an important role in the ability of pathogenic bacteria to adhere to the surface of the host cell in the first step of their invasion and infectivity. Together with carbohydrate receptors located on pili and flagellum, Pseudomonas aeruginosa also expresses soluble galactose- and fucose-binding lectins (PA-IL and PA-IIL). Complexes between both lectins and their monosaccharide ligands have been characterized by a variety of methods, including enzyme-amplification (ELLA), titration microcalorimetry, x-ray crystallography and molecular modeling. PA-IIL displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. These characteristics are correlated to the remarkable presence of twocalcium ions in the binding site of the protein. When searching for ligands of biological interest, PA-IIL lectin displays highest affinity for lewis a, a trisaccharide located on epithelial cell glycoconjugates of CF patients, and human

Název v anglickém jazyce

Thermodynamic and structures of Pseudomonas aeruginosa lectins and their interaction with complex human glycoconjugates

Popis výsledku anglicky

Carbohydrate-mediated recognition plays an important role in the ability of pathogenic bacteria to adhere to the surface of the host cell in the first step of their invasion and infectivity. Together with carbohydrate receptors located on pili and flagellum, Pseudomonas aeruginosa also expresses soluble galactose- and fucose-binding lectins (PA-IL and PA-IIL). Complexes between both lectins and their monosaccharide ligands have been characterized by a variety of methods, including enzyme-amplification (ELLA), titration microcalorimetry, x-ray crystallography and molecular modeling. PA-IIL displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. These characteristics are correlated to the remarkable presence of twocalcium ions in the binding site of the protein. When searching for ligands of biological interest, PA-IIL lectin displays highest affinity for lewis a, a trisaccharide located on epithelial cell glycoconjugates of CF patients, and human

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

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

Název periodika

Glycoconjugate Journal

ISSN

0282-0080

e-ISSN

—

Svazek periodika

22

Číslo periodika v rámci svazku

4/5/6

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

1

Strana od-do

278-278

Kód UT WoS článku

—

EID výsledku v databázi Scopus

—