RSL from Ralstonia solanacearum linked to Biotin

RSL from Ralstonia solanacearum linked to Biotin RSL (Ralstonia solanacearum Lectin) linked to Biotin is a biotinylated lectin that binds specifically to fucose and related carbohydrates, making it a valuable tool for studying plant-pathogen interactions, carbohydrate recognition, and bacterial adhesion. Derived from Ralstonia solanacearum , a plant pathogen responsible for bacterial wilt in crops, this lectin is instrumental in understanding host invasion mechanisms. Key Characteristics of RSL: Function : RSL is a fucose-binding lectin with specificity for L-fucose > L-galactose > D-arabinose > D-mannose. It plays a role in bacterial adhesion to plant cells and biofilm formation. It interacts with H and Lewis antigens in glycoproteins, making it useful for studying glycan-mediated interactions in both plant and animal systems. Structural Features : RSL is a small monomeric lectin (~9.9 kDa) with structural similarity to fungal lectins. It forms stable complexes with fucosylated glycans through conserved binding motifs. The lectin’s binding properties are mediated by specific amino acid residues that determine its high affinity for fucose. Biotin Conjugation : Biotin labeling enhances the utility of RSL by enabling: Streptavidin-based detection : Ideal for ELISA assays, Western blotting, and pull-down experiments to study fucose-binding interactions. Quantitative binding studies : Facilitates measurement of carbohydrate-binding kinetics using biotin-streptavidin systems. Microscopy applications : Enables visualization of RSL binding to fucosylated targets when paired with streptavidin-fluorophore conjugates. Applications in Research: Plant-Pathogen Interaction Studies : Tracks RSL’s binding to fucosylated glycans on plant cell surfaces, elucidating mechanisms of bacterial adhesion and colonization during infection. Biofilm Formation Analysis : Visualizes the role of RSL in stabilizing biofilm matrices by crosslinking extracellular polysaccharides, aiding in the study of biofilm architecture and inhibitor screening. Carbohydrate Recognition Studies : Investigates the specificity of RSL for various glycans, providing insights into glycan-mediated signaling pathways in host-pathogen systems. Drug Discovery : Screens inhibitors targeting RSL’s carbohydrate-binding domain to disrupt bacterial adhesion or biofilm formation, particularly in agricultural pathogens. Production and Validation: Recombinantly expressed in E. coli and purified via affinity chromatography. Biotin labeling validated through binding assays with fucosylated ligands and functional studies confirming its carbohydrate specificity and adhesion properties. This biotinylated lectin is a versatile tool for advancing research into Ralstonia solanacearum pathogenesis, glycan recognition mechanisms, and the development of anti-adhesion strategies for crop protection. Meta Description : "Explore RSL from Ralstonia solanacearum , a biotinylated lectin for studying fucose-specific interactions, plant-pathogen adhesion, and biofilm formation. Ideal for glycan recognition research and anti-infection strategies." Citations: https://www.rcsb.org/structure/2chh https://www.rcsb.org/structure/1UQX https://pubmed.ncbi.nlm.nih.gov/12153735/ http://www.xray.cz/setkani/abst2014/pokorny.htm https://pmc.ncbi.nlm.nih.gov/articles/PMC9668655/ https://pmc.ncbi.nlm.nih.gov/articles/PMC10306066/ https://www.jstage.jst.go.jp/article/biochemistry1922/132/2/132_2_353/_pdf https://www.rcsb.org/structure/3zi8