Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity
| Authors | |
|---|---|
| Year of publication | 2011 |
| Type | Article in Periodical |
| Magazine / Source | PLoS Pathogens |
| MU Faculty or unit | |
| Citation | |
| Web | http://www.plospathogens.org/article/info%3Adoi%2F10.1371%2Fjournal.ppat.1002238 |
| Doi | http://dx.doi.org/10.1371/journal.ppat.1002238 |
| Field | Biochemistry |
| Keywords | bacterial lectin;Burkholderia cenocepacia;calcium-dependent bacterial lectins;TNF;inflammation |
| Description | Lectins and adhesins are involved in bacterial adhesion to host tissues and mucus during early steps of infection. We report the characterization of BC2L-C, a soluble lectin from the opportunistic pathogen Burkholderia cenocepacia. The N-terminal domain is a novel TNF-a-like fucosebinding lectin, while the C-terminal part is similar to a superfamily of calcium-dependent bacterial lectins. The C-terminal domain displays specificity for mannose and L-glycero-D-manno-heptose. BC2L-C is therefore a superlectin that binds independently to mannose/heptose glycoconjugates and fucosylated human histo-blood group epitopes. We propose that BC2L-C binds to the bacterial surface in a mannose/heptose-dependent manner via the C-terminal domain. The TNF-a-like domain triggers IL-8 production in cultured airway epithelial cells in a carbohydrate-independent manner, and is therefore proposed to play a role in the dysregulated proinflammatory response observed in B. cenocepacia lung infections. |
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