2007
New approaches to structure and function studies of RS20L lectin from Ralstonia solanacearum
ŠULÁK, Ondřej; Nikola KOSTLÁNOVÁ; Jan ADAM; Edward MITCHELL; Anne IMBERTY et. al.Základní údaje
Originální název
New approaches to structure and function studies of RS20L lectin from Ralstonia solanacearum
Název česky
Nové přístupy ke studiu struktury a funkce lektinu RS20L z bakterie Ralstonia solanacearum
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Vydání
Lubeck (Germany), 14th European Carbohydrate Symposium, EUROCARB 14, s. 147-296, 2007
Nakladatel
Research Center Borstel and the Institute of Chemistry
Další údaje
Jazyk
angličtina
Typ výsledku
Stať ve sborníku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Německo
Utajení
není předmětem státního či obchodního tajemství
Organizační jednotka
Přírodovědecká fakulta
Klíčová slova anglicky
Ralstonia solanacearum - lectin - crystallography
Příznaky
Mezinárodní význam
Změněno: 12. 11. 2007 17:11, prof. RNDr. Michaela Wimmerová, Ph.D.
V originále
Lectins are sugar-binding proteins of non-immune nature that agglutinates cells or precipitates glycoconjugates. Their specificity is usually defined by the monosaccharides or oligosaccharides that are the best at inhibiting the agglutination or precipitation the lectin causes. Lectins are of interest because of their wide variety of properties and potential applications (pharmacology, immunology, cancer therapy, agriculture, etc.). Ralstonia solanacearum is a plant bacterial pathogen, which causes a wilt disease in several economically important agricultural crops, such as potatoes, tomatoes, peppers, eggplant, banana [1]. The bacterium R. solancearum is a widely accepted model organism for the study of pathogenicity in plants. Plant and animal pathogens use protein-carbohydrate interactions in their strategy for host recognition and invasion. The comprehension of the molecular mechanisms, which gives a pathogenic bacterium the ability to invade, colonize and reorient the physiopathology of its host, is a goal of primary importance and such studies may direct the conception of new strategies to fight against these pathogenic agents. As far as we know, the R. solanacearum bacterium has been producing three soluble lectins One of them, lectin RS20L, displays L-fucose and D mannose and D-xylose binding ability. This presentation structurally and functionally describes RS20L, a 20 kDa lectin from R. solanacearum, which has no sequence similarity to any known lectin amino acid sequence, but resolution of crystal structure showed high structural similarity to animal galectins. However it does not display sugar specifity to D-galactose. Further functional studies using surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) allowed to define binding properties (afinity, kinetics) and thermodynamic parameters.
Česky
Lectins are sugar-binding proteins of non-immune nature that agglutinates cells or precipitates glycoconjugates. Their specificity is usually defined by the monosaccharides or oligosaccharides that are the best at inhibiting the agglutination or precipitation the lectin causes. Lectins are of interest because of their wide variety of properties and potential applications (pharmacology, immunology, cancer therapy, agriculture, etc.). Ralstonia solanacearum is a plant bacterial pathogen, which causes a wilt disease in several economically important agricultural crops, such as potatoes, tomatoes, peppers, eggplant, banana [1]. The bacterium R. solancearum is a widely accepted model organism for the study of pathogenicity in plants. Plant and animal pathogens use protein-carbohydrate interactions in their strategy for host recognition and invasion. The comprehension of the molecular mechanisms, which gives a pathogenic bacterium the ability to invade, colonize and reorient the physiopathology of its host, is a goal of primary importance and such studies may direct the conception of new strategies to fight against these pathogenic agents. As far as we know, the R. solanacearum bacterium has been producing three soluble lectins One of them, lectin RS20L, displays L-fucose and D mannose and D-xylose binding ability. This presentation structurally and functionally describes RS20L, a 20 kDa lectin from R. solanacearum, which has no sequence similarity to any known lectin amino acid sequence, but resolution of crystal structure showed high structural similarity to animal galectins. However it does not display sugar specifity to D-galactose. Further functional studies using surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) allowed to define binding properties (afinity, kinetics) and thermodynamic parameters.
Návaznosti
| LC06030, projekt VaV |
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| MSM0021622413, záměr |
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