LecB (PA-IIL) from Pseudomonas aeruginosa linked to Fluorescein
LecB (PA-IIL) from Pseudomonas aeruginosa linked to Fluorescein is a fluorescently labeled bacterial lectin used for research applications to study host-pathogen interactions and carbohydrate recognition. This product combines the fucose-binding lectin LecB with fluorescein, enabling visualization of lectin-glycan binding in experimental settings.
Key Characteristics of LecB (PA-IIL):
Function:
LecB is a tetrameric fucose-binding lectin with exceptionally high affinity for α-L-fucose and related glycans. It acts as a virulence factor in P. aeruginosa infections by disrupting epithelial wound healing, promoting biofilm formation, and facilitating bacterial adhesion through interactions with host receptors like β1-integrin.
Structural Features:
Molecular weight: ~11.9 kDa (monomer).
Binds fucose via calcium-dependent interactions, with structural details resolved in multiple X-ray crystallography studies (e.g., 1.5–2.1 Å resolution).
Forms stable complexes with fucosylated peptides and glycoconjugates.
Fluorescein Conjugation:
The fluorescein tag allows real-time tracking of LecB binding to fucosylated substrates, making it suitable for:
Fluorescence microscopy of bacterial adhesion
Flow cytometry-based glycan profiling
Competitive binding assays.
Applications in Research:
Host-Pathogen Interaction Studies:
Investigates LecB’s role in disrupting insulin-like growth factor-1 receptor signaling and keratinocyte function.
Biofilm Analysis:
Visualizes lectin-mediated retention of extracellular polymeric substances (e.g., Psl) in aeruginosa biofilms.
Anti-Infective Drug Screening:
Facilitates high-throughput testing of fucose analogs or inhibitors targeting LecB’s carbohydrate-binding sites.
Production and Quality:
Recombinantly produced in E. coli with affinity purification.
Maintains functional activity post-labeling, validated by structural and binding assays
This tool is critical for advancing studies on bacterial adhesion mechanisms, biofilm formation, and therapeutic interventions targeting lectin-mediated infections.
Reviews
There are no reviews yet.