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
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