BC2LA from Burkholderia cenocepacia linked to Biotin

BC2LA from Burkholderia cenocepacia linked to Biotin BC2L-A from Burkholderia cenocepacia linked to Biotin is a biotinylated bacterial lectin used for studying mannose-specific carbohydrate interactions, bacterial adhesion, and biofilm formation. This conjugate enables precise detection and quantification of BC2L-A activity in experimental systems utilizing biotin-streptavidin-based assays. Key Characteristics of BC2L-A: Function : BC2L-A is a mannose-specific C-type lectin that plays a crucial role in biofilm structure and morphology of B. cenocepacia . It binds to mannose-containing glycans, contributing to bacterial aggregation and biofilm stabilization. Structural Features : Forms a dimeric assembly of 13.8 kDa monomers, in contrast to its homolog LecB from Pseudomonas aeruginosa which forms tetramers. Contains a LecB-like domain with calcium-dependent binding sites for α-D-mannose and L- glycero -D- manno -heptose. Highly selective for D-mannose-based ligands with an absolute requirement for the hydroxyl group at C6. Biotin Conjugation : Biotin labeling enhances the versatility of BC2L-A in research applications by enabling: Streptavidin-based detection for various assays and imaging techniques. Quantitative binding studies using biotin-streptavidin systems. Visualization of BC2L-A interactions in biofilms and host-pathogen studies. Applications in Research: Biofilm Studies : BC2L-A is essential for maintaining biofilm structural integrity under flow conditions. Biotinylated BC2L-A can be used to visualize and analyze biofilm architecture. Inhibitor Development : Useful for screening potential anti-biofilm compounds targeting BC2L-A's mannose-binding sites. Host-Pathogen Interactions : Investigates BC2L-A's role in bacterial adhesion to host glycans and its contribution to virulence in cystic fibrosis infections. Regulation and Production: Expression is regulated by quorum sensing systems, including the Burkholderia diffusible signal factor (BDSF) system and CepR. Recombinantly produced in E. coli and validated via calcium-dependent binding assays. This tool is pivotal for advancing research into B. cenocepacia infections, particularly in understanding biofilm formation and developing anti-virulence strategies against this opportunistic pathogen. Citations: https://pubs.rsc.org/de/content/getauthorversionpdf/C5MD00557D https://en.wikipedia.org/wiki/index.html?curid=8235178 https://academic.oup.com/glycob/article/22/10/1387/1988347?login=false