Burkholderia cenocepacia and its novel two domain superlectin
| Authors | |
|---|---|
| Year of publication | 2009 |
| Type | Article in Proceedings |
| Conference | the FEBS Journal |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | Burkholderia cenocepacia; lectin; structure function characterisation; |
| Description | Burkholderia cenocepacia is a Gram-negative bacterium that can be found throughout the environment. It is a part of "Burkholderia cepacia complex", which causes potentially deadly problems to patients suffering from cystic fibrosis and chronic granulomatous diseases. A goal of primary importance of this study is the understanding of the molecular mechanisms, especially protein-carbohydrate interactions, which give pathogenic bacterium the ability to invade and colonize its host. Four genes coding protein homologues to the lectin PA-IIL from Pseudomonas aeruginosa have been found in the genome of B. cenocepacia. One of them, BclC, is a 28 kDa protein. The results indicated the unusual binding activity of the protein. The C-terminal domain recognizes D-mannosylated saccharides. Interestingly, the N-terminal domain also displays sugar-binding activity with a strong preference for L-fucosylated oligosaccharides, the Lewis type determinants. The structural basis of the protein affinity towards different saccharides could serve as a starting point in the design of new and efficient ligand analogs and inhibitors. Such studies may direct the conception of new strategies to fight against pathogenic agents. |
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