ŠULÁK, Ondřej, Nikola KOSTLÁNOVÁ, Edvard MITCHELL, Anne IMBERTY a Michaela WIMMEROVÁ. Galectin-like protein from Ralstonia solanacearum. In Current chemistry and biochemistry of saccharides - Cukrblik 2007. Praha: Czech Academy of Sciences, 2007, s. 46-95.
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Základní údaje
Originální název Galectin-like protein from Ralstonia solanacearum
Název česky Galectin-like protein from Ralstonia solanacearum
Autoři ŠULÁK, Ondřej, Nikola KOSTLÁNOVÁ, Edvard MITCHELL, Anne IMBERTY a Michaela WIMMEROVÁ.
Vydání Praha, Current chemistry and biochemistry of saccharides - Cukrblik 2007, s. 46-95, 2007.
Nakladatel Czech Academy of Sciences
Další údaje
Originální 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
Štítky Ralstonia solanacearum - lectin
Příznaky Mezinárodní význam
Změnil Změnil: Mgr. Ondřej Šulák, Ph.D., učo 54790. Změněno: 2. 11. 2007 16:29.
Anotace
Ralstonia solanacearum is a Gram-negative bacterial pathogen that causes several diseases in a wide range of plants (tomatoes, peppers, eggplant, banana etc.) [1]. Lectins are carbohydrate-binding proteins or glycoproteins, which are highly specific for their sugar moieties in cell walls or membranes and thereby change the physiology of the membrane. Lectins are known for their ability to agglutinate erythrocytes in vitro. Plant and animal pathogens use these protein-carbohydrate interactions in their strategy for host recognition and invasion. Since there are not any known treatments of resistant plant species, identifying target molecules for the bacterium in host plants could help to develop a strategy against its infection. As far as we know, the R. solanacearum bacterium has been producing three soluble lectins, RSL (9.9 kDa) [2], RS-IIL (11.6 kDa) [3] and newly discovered RS20L (20 kDa) This contribution structurally and functionally describes RS20L, which has no sequence similarity to any known amino acid sequence. Although resolution of crystal structure showed high structural similarity to animal galectins, it does not display sugar specifity to D-galactose.
Anotace česky
Ralstonia solanacearum is a Gram-negative bacterial pathogen that causes several diseases in a wide range of plants (tomatoes, peppers, eggplant, banana etc.) [1]. Lectins are carbohydrate-binding proteins or glycoproteins, which are highly specific for their sugar moieties in cell walls or membranes and thereby change the physiology of the membrane. Lectins are known for their ability to agglutinate erythrocytes in vitro. Plant and animal pathogens use these protein-carbohydrate interactions in their strategy for host recognition and invasion. Since there are not any known treatments of resistant plant species, identifying target molecules for the bacterium in host plants could help to develop a strategy against its infection. As far as we know, the R. solanacearum bacterium has been producing three soluble lectins, RSL (9.9 kDa) [2], RS-IIL (11.6 kDa) [3] and newly discovered RS20L (20 kDa) This contribution structurally and functionally describes RS20L, which has no sequence similarity to any known amino acid sequence. Although resolution of crystal structure showed high structural similarity to animal galectins, it does not display sugar specifity to D-galactose.
Návaznosti
GD204/03/H016, projekt VaVNázev: Strukturní biofyzika makromolekul
Investor: Grantová agentura ČR, Strukturní biofyzika makromolekul
LC06030, projekt VaVNázev: Biomolekulární centrum
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum
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