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 poznatky ve studiu struktury a funkci lektinu RS20L z bakterie Ralstonia solanacearum
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Vydání
Nové Hrady, Czech Republic, Materials Structure, vol. 14, no. 1 (2007), 6th Discussions in Structural Molecular Biology, od s. 23-34, 30 s. 2007
Nakladatel
Academic and University Center, Nové Hrady
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
Organizační jednotka
Přírodovědecká fakulta
Klíčová slova anglicky
Ralstonia solanacearum - lectin - crystallography
Příznaky
Mezinárodní význam
Změněno: 4. 11. 2007 15:37, Mgr. Ondřej Šulák, Ph.D.
V originále
Lectins are sugar-binding proteins of non-immune nature that play a role in cell agglutination or glycoconjugates precipitation. These lectins bind to sugar moieties in cell walls or membranes and thereby change the physiology of the membrane, thus cause agglutination, mitosis, or other biochemical changes in the cell. Ralstonia solanacearum is a plant bacterial pathogen, which causes a wilt disease in several economically important agricultural crops, such as potatoes, tomatoes, peppers, eggplant, and banana. Plant and animal pathogens use protein-carbohydrate interactions in their strategy for host recognition and invasion. Until our knowledge now, the R. solanacearum bacterium has been producing three soluble lectins. RSL (MW 9900), which exhibits sugar specifity to L-fucose and partial sequence homology to mushroom Aleuria aurantia lectin AAL, RS-IIL (MW 11601) lectin resembles PA-IIL from human pathogen Pseudomonas aeruginosa in structure and properties but differs in sugar specifity. The last one is RS20L (MW 19903), which displays L-fucose and D-mannose and D-xylose binding ability. This presentation describes, structurally and functionally, the RS20L, a 20 kDa lectin, which has no sequence similarity to any known lectin amino acid sequence, but the solution of crystal structure showed high structural similarity to animal galectins. However it does not display any sugar specificity 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 play a role in cell agglutination or glycoconjugates precipitation. These lectins bind to sugar moieties in cell walls or membranes and thereby change the physiology of the membrane, thus cause agglutination, mitosis, or other biochemical changes in the cell. Ralstonia solanacearum is a plant bacterial pathogen, which causes a wilt disease in several economically important agricultural crops, such as potatoes, tomatoes, peppers, eggplant, and banana. Plant and animal pathogens use protein-carbohydrate interactions in their strategy for host recognition and invasion. Until our knowledge now, the R. solanacearum bacterium has been producing three soluble lectins. RSL (MW 9900), which exhibits sugar specifity to L-fucose and partial sequence homology to mushroom Aleuria aurantia lectin AAL, RS-IIL (MW 11601) lectin resembles PA-IIL from human pathogen Pseudomonas aeruginosa in structure and properties but differs in sugar specifity. The last one is RS20L (MW 19903), which displays L-fucose and D-mannose and D-xylose binding ability. This presentation describes, structurally and functionally, the RS20L, a 20 kDa lectin, which has no sequence similarity to any known lectin amino acid sequence, but the solution of crystal structure showed high structural similarity to animal galectins. However it does not display any sugar specificity 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
| GD204/03/H016, projekt VaV |
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| MSM0021622413, záměr |
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