RSL from Ralstonia solanacearum linked to Fluorescein
RSL (Ralstonia solanacearum Lectin) linked to Fluorescein is a fluorescently labeled lectin used to study carbohydrate-mediated interactions in plant-pathogen systems. Derived from the soil-borne pathogen Ralstonia solanacearum, which causes bacterial wilt in crops like tomatoes and potatoes, this lectin plays a role in bacterial adhesion and virulence.
Key Characteristics of RSL:
Function:
RSL is a 9.9 kDa monomeric lectin related to fungal lectins, with affinity for fucose and other glycans. Unlike its homolog RS-IIL, which prefers mannose, RSL’s binding profile suggests a role in early host recognition, though its exact biological function in pathogenesis remains under investigation.
Structural Features:
Shares structural motifs with fungal lectins but lacks the calcium-dependent binding seen in RS-IIL.
Forms stable complexes with fucosylated glycans, aiding in bacterial adhesion to plant surfaces.
Fluorescein Conjugation:
The fluorescein tag enables visualization of carbohydrate-binding activity in applications such as:
Fluorescence microscopy to map lectin distribution during plant infection.
Competitive binding assays to screen glycan-based inhibitors.
Analysis of biofilm matrix components in R. solanacearum.
Applications in Research:
Plant-Pathogen Interaction Studies:
Tracks RSL’s binding to plant cell surface glycans, elucidating mechanisms of bacterial adhesion and colonization.
Biofilm Dynamics:
Visualizes lectin-mediated stabilization of extracellular polysaccharides (EPS) in biofilms, critical for bacterial persistence.
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