BC2LC-Nt from Burkholderia cenocepacia

BC2LC-Nt from Burkholderia cenocepacia

Introduction

BC2LC-Nt is the N-terminal domain of the BC2L-C lectin, a superlectin produced by Burkholderia cenocepacia, an opportunistic Gram-negative bacterium known for causing severe infections, particularly in patients with cystic fibrosis or immunocompromised conditions. This lectin plays a crucial role in bacterial adhesion and biofilm formation, contributing to the virulence of B. cenocepacia.

Structure and function 

• Domain Structure : BC2L-C, the parent lectin of BC2LC-Nt, consists of two distinct domains: an N-terminal TNF-α-like domain and a C-terminal domain similar to calcium-dependent bacterial lectins. The N-terminal domain (BC2LC-Nt) specifically binds to fucosylated human histo-blood group epitopes, while the C-terminal domain binds to mannose and L-glycero-D-manno-heptose.
• Biological Activity : BC2LC-Nt triggers IL-8 production in cultured airway epithelial cells in a carbohydrate-independent manner, contributing to a dysregulated proinflammatory response during infections.

Characteristics

• Molecular Weight : The BC2LC-Nt monomer has a molecular weight of approximately 19.26 kDa.
• Production : BC2LC-Nt is commonly produced in E. coli for research purposes and is not intended for human or animal use.

Role in infection

• Adhesion and Biofilm Formation : BC2LC-Nt, as part of BC2L-C, facilitates the adhesion of B. cenocepacia to human epithelial cells, promoting biofilm formation and enhancing bacterial virulence.
• Target for Therapeutic Developments : The interaction between BC2LC-Nt and its target fucosylated oligosaccharides is being explored for the development of glycomimetic antagonists to inhibit bacterial adhesion and biofilm formation, offering a potential therapeutic strategy against B. cenocepacia infections.

Research Applications 

BC2LC-Nt is used as a laboratory reagent for studying bacterial adhesion mechanisms and developing anti-adhesive therapies. Its structural and functional characteristics make it an important model for understanding the pathogenicity of B. cenocepacia and for designing novel therapeutic agents