PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00021355" target="_blank" >RIV/00216224:14310/04:00021355 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria

Original language description

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 lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients [1,2]. Moreover, the PA-IIL lectin displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. This characteristics is correlated to the remarkable presence of two calcium ions in the binding siteof the protein [3]. Database searching in newly sequenced bacterial genomes revealed the presence of PA-IIL like proteins within a limited number of other opportunistic pathogens. All of them are soil inhabitants, are phylogenetically rel

Czech name

PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria

Czech description

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 lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients [1,2]. Moreover, the PA-IIL lectin displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. This characteristics is correlated to the remarkable presence of two calcium ions in the binding siteof the protein [3]. Database searching in newly sequenced bacterial genomes revealed the presence of PA-IIL like proteins within a limited number of other opportunistic pathogens. All of them are soil inhabitants, are phylogenetically rel

Type

D - Article in proceedings

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2004

Confidentiality

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

Article name in the collection

Chemica 43S

ISBN

80-244-0882-1

ISSN

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e-ISSN

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Number of pages

2

Pages from-to

72-73

Publisher name

Ceska spolecnost pro biochemii a molekularni biologii

Place of publication

Olomouc

Event location

Olomouc

Event date

Aug 31, 2004

Type of event by nationality

EUR - Evropská akce

UT code for WoS article

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