2004
PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria
WIMMEROVÁ, Michaela, Edward P. MITCHELL, Martina BUDOVA, Charles SABIN, Nikola KOSTLÁNOVÁ et. al.Základní údaje
Originální název
PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria
Název česky
PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria
Autoři
WIMMEROVÁ, Michaela (203 Česká republika, garant), Edward P. MITCHELL (250 Francie), Martina BUDOVA (203 Česká republika), Charles SABIN (250 Francie), Nikola KOSTLÁNOVÁ (203 Česká republika), Stephanie PERRET (250 Francie), Gianluca CIOCI (250 Francie), Nechama GILBOA-GARBER (376 Izrael) a Anne IMBERTY (250 Francie)
Vydání
2004. vyd. Olomouc, Chemica 43S, od s. 72-73, 2 s. 2004
Nakladatel
Ceska spolecnost pro biochemii a molekularni biologii
Další údaje
Jazyk
angličtina
Typ výsledku
Stať ve sborníku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Česká republika
Utajení
není předmětem státního či obchodního tajemství
Kód RIV
RIV/00216224:14310/04:00021355
Organizační jednotka
Přírodovědecká fakulta
ISBN
80-244-0882-1
Klíčová slova anglicky
lectin; pathogen; saccharide
Štítky
Změněno: 25. 7. 2005 11:19, Mgr. Martina Pokorná, Ph.D., MBA
V originále
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 the first 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 site of 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 related and in past were usually considered as Pseudomonas spp. At the present time, PA-IIL like gene have been identified in the genomes of phytopathogen Ralstonia solanacearum and of human opportunistic pathogens Chromobacterium violaceum and Burholderia cenocepacia. The latter was found to cause life threatening pulmonary infections in cystic fibrosis patients at a mortality rate of 80% [4]. PA-IIL like proteins from R. Solanacearum (RS-IIL) and C. Violaceum (CV-IIL) have been fully characterized. RS-IIL has been purified from bacteria by affinity chromatography [4] whereas CV-IIL has been obtained in the recombinant form. The three lectins have been compared for their specificity (enzyme amplification method), their affinity for monosaccharides (isothermal titration microcalorimetry experiments) and their crystal structures. Comparison of the structures of the PA-IIL/fucose and RS-IIL/mannose complexes allow us to rationalize the basis of the unusual high specificity of both proteins for monosaccharides and the importance of three amino acid motif for fine tuning of the lectin specificity.
Česky
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 the first 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 site of 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 related and in past were usually considered as Pseudomonas spp. At the present time, PA-IIL like gene have been identified in the genomes of phytopathogen Ralstonia solanacearum and of human opportunistic pathogens Chromobacterium violaceum and Burholderia cenocepacia. The latter was found to cause life threatening pulmonary infections in cystic fibrosis patients at a mortality rate of 80% [4]. PA-IIL like proteins from R. Solanacearum (RS-IIL) and C. Violaceum (CV-IIL) have been fully characterized. RS-IIL has been purified from bacteria by affinity chromatography [4] whereas CV-IIL has been obtained in the recombinant form. The three lectins have been compared for their specificity (enzyme amplification method), their affinity for monosaccharides (isothermal titration microcalorimetry experiments) and their crystal structures. Comparison of the structures of the PA-IIL/fucose and RS-IIL/mannose complexes allow us to rationalize the basis of the unusual high specificity of both proteins for monosaccharides and the importance of three amino acid motif for fine tuning of the lectin specificity.
Návaznosti
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