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Nahlédnutí do struktury a funkce lektinu RS20L z bakteriálního fytopatogenu Ralstonia solanacearum

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Title in English Structure and function of the lectin RS20L from bacterial pathogen Ralstonia solanacearum


Year of publication 2007
Type Article in Proceedings
Conference Chem. Listy 101, 425–465 (2007) - VII. Mezioborové setkání mladých biologů, biochemiků a chemiků
MU Faculty or unit

Faculty of Science

Field Biochemistry
Keywords Ralstonia solanacearum - lectin - function - structure
Description Lectins are sugar-binding proteins of non-immunoglobulin nature that agglutinates cells or precipitates glycoconjugates. Their specificity is usually defined by the monosaccharides or oligosaccharides that are 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...). 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. Ralstonia solanacearum is a bacterial pathogen, which causes a wilt disease in several economically important agricultural crops, such as potatoes, tomatoes, peppers, eggplant, banana... Causes of this disease are known as Southern wilt, bacterial wilt, and brown rot of potato. The disease is transmitted through soil, contaminated water, equipment, personnel, and by transplanting infected plants. It is not spread through the air, from plant to plant through the splashing of water. The bacterium R. solancearum is a widely accepted model organism for the study of pathogenicity in plants. 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 20034), which displays mannose and xylose binding ability. This short communication structurally and functionally describes RS20L, a 20kDa 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.
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