BC2LC-Nt from Burkholderia cenocepacia linked to Fluorescein

BC2LC-Nt from Burkholderia cenocepacia linked to Fluorescein BC2LC-Nt from Burkholderia cenocepacia linked to Fluorescein is a fluorescently labeled lectin domain used to study fucose-mediated host-pathogen interactions and proinflammatory signaling in chronic infections like cystic fibrosis. Derived from the N-terminal domain of the BC2L-C superlectin, this TNF-α-like lectin binds fucosylated glycans and triggers immune responses independently of carbohydrate recognition. Key Characteristics of BC2LC-Nt: Function : Fucose-specific binding : Targets α1-2/3/4-linked fucose in human histo-blood group antigens (e.g., Lewis^x, H-type 1) to mediate bacterial adhesion to epithelial cells. Proinflammatory activity : Stimulates IL-8 secretion in airway cells via a carbohydrate-independent mechanism, amplifying inflammation in B. cenocepacia infections. Structural role : Forms TNF-α-like trimers that contribute to BC2L-C’s hexameric architecture, enabling dual lectin functionality. Structural Features : TNF-α-like fold : Unique among bacterial lectins, resembling human TNF-α but retaining fucose-binding specificity. Flexible oligomerization : Integrates into BC2L-C’s hexameric structure, flanking calcium-dependent C-terminal domains. Molecular weight: ~15–18 kDa (monomer), forming stable trimers post-Fluorescein labeling. Fluorescein Conjugation : Labeling with fluorescein isothiocyanate (FITC) enables: Visualization of fucose-binding sites in host tissues via fluorescence microscopy. Quantification of lectin-glycan interactions using fluorescence polarization or flow cytometry. High-throughput screening of fucose analogs to block bacterial adhesion or inflammation. Applications in Research: Host-Pathogen Adhesion Studies : Tracks BC2LC-Nt binding to fucosylated epitopes on airway epithelia, elucidating mechanisms of cenocepacia colonization. Inflammatory Response Analysis : Investigates IL-8 induction in cystic fibrosis models, linking lectin activity to neutrophil recruitment and tissue damage. Anti-Virulence Drug Development : Screens inhibitors targeting BC2LC-Nt’s fucose-binding site or TNF-α-like signaling to reduce bacterial persistence. Production and Validation: Recombinantly expressed in E. coli with affinity tags for purification. Fluorescein labeling validated via: Binding assays with fucosylated glycans (e.g., Lewis^x). Cell-based assays confirming IL-8 induction in airway epithelial cultures. This tool bridges structural biology and immunology, offering insights into B. cenocepacia ’s dual strategies of glycan recognition and immune evasion. Meta Description : "Explore BC2LC-Nt from Burkholderia cenocepacia , a fluorescently labeled TNF-α-like lectin for studying fucose-mediated adhesion and proinflammatory signaling. Ideal for cystic fibrosis research and anti-virulence drug discovery." Citations: https://en.wikipedia.org/wiki/index.html?curid=8235178 https://pmc.ncbi.nlm.nih.gov/articles/PMC3164656/ https://pubmed.ncbi.nlm.nih.gov/21909279/