Publication details
New approaches to structure and function studies of RS20L lectin from Ralstonia solanacearum
| Authors | |
|---|---|
| Year of publication | 2007 |
| Type | Article in Proceedings |
| Conference | 14th European Carbohydrate Symposium, EUROCARB 14 |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | Ralstonia solanacearum - lectin - crystallography |
| Description | 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. |
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