Burkholderia cenocepacia BC2L-C: A Super Lectin with Dual Specificity
Author Information
Author(s): Šulák Ondřej, Cioci Gianluca, Lameignère Emilie, Balloy Viviane, Round Adam, Gutsche Irina, Malinovská Lenka, Chignard Michel, Kosma Paul, Aubert Daniel F., Marolda Cristina L., Valvano Miguel A., Wimmerová Michaela, Imberty Anne
Primary Institution: CERMAV-CNRS- UPR5301 affiliated to Université Joseph Fourier, Grenoble, France
Hypothesis
BC2L-C is a novel superlectin with multiple specificities and biological functions.
Conclusion
BC2L-C is a hexameric superlectin that binds to both mannose/heptose glycoconjugates and fucosylated human histo-blood group epitopes, triggering IL-8 production in airway epithelial cells.
Supporting Evidence
- BC2L-C has two distinct domains with unique specificities and biological activities.
- The N-terminal domain is a novel TNF-α-like fucose-binding lectin.
- The C-terminal domain displays specificity for mannose and l-glycero-d-manno-heptose.
- BC2L-C binds independently to mannose/heptose glycoconjugates and fucosylated human histo-blood group epitopes.
- BC2L-C triggers IL-8 production in cultured airway epithelial cells in a carbohydrate-independent manner.
- The unique architecture of BC2L-C correlates with multiple functions including bacterial cell cross-linking and adhesion to human epithelia.
Takeaway
This study found a special protein from bacteria that can stick to sugars in our body and might cause inflammation, which is important for understanding infections in people with cystic fibrosis.
Methodology
The study characterized the structure and specificity of the C-terminal domain of BC2L-C using techniques like electron microscopy, small angle X-ray scattering, and microcalorimetry.
Digital Object Identifier (DOI)
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