Burkholderia cenocepacia and its novel two domain superlectin

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Authors

ŠULÁK Ondřej DELIA Monia IMBERTY Anne WIMMEROVÁ Michaela

Year of publication 2009
Type Article in Proceedings
Conference the FEBS Journal
MU Faculty or unit

Faculty of Science

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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