Publication details
Novel two - domain superlectin from the human opportunistic pathogen Bukholderia cenocepacia
| Authors | |
|---|---|
| Year of publication | 2009 |
| Type | Article in Proceedings |
| Conference | Cukrblik 2009 |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | Superlectin; X ray; Isothermal titration callorimetry; Burkolderia cenocepacia |
| Description | 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. Burkholderia cenocepacia is a Gram-negative bacterium that can be found throughout the environment.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. Further sequence analysis showed two distinct domains in the protein structure. The C-terminal part coding lectin domain shows partial homology to the PA-IIL lectin, as mentioned above, and the N-terminal part is unknown. Both domains were also cloned separately. The results indicated the unusual binding activity of the protein. The C-terminal domain recognizes D-mannosylated saccharides with high affinity. Interestingly, the N-terminal domain also displays sugar-binding activity with a strong preference for L-fucosylated oligosaccharides, the Lewis type determinants. |
| Related projects: |