Galectin-like protein from Ralstonia solanacearum
| Authors | |
|---|---|
| Year of publication | 2007 |
| Type | Article in Proceedings |
| Conference | Current chemistry and biochemistry of saccharides - Cukrblik 2007 |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | Ralstonia solanacearum - lectin |
| Description | 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. |
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