RSL from Ralstonia solanacearum

RSL (Ralstonia Solanacearum Lectin) is indeed a high-purity laboratory reagent designed for research and development purposes only, not intended for human or animal use7. This lectin is known for its specific carbohydrate-binding properties and is widely used in studies related to bacterial adhesion, host-pathogen interactions, and glycobiology.

Key characteristics of RSL include:

1. Molecular weight: 9.9 kDa per monomer7

2. Structure: Forms a trimeric structure, generating a six-bladed β-propeller architecture1

3. Binding specificity: High affinity for L-fucose and its derivatives, particularly α-Fuc1-2Gal and α-Fuc1-6Gal epitopes1

RSL has been extensively studied for its role in plant pathogenesis:

1. It is produced by Ralstonia solanacearum, a bacterium that causes lethal wilt in many agricultural crops worldwide1

2. The lectin is involved in host recognition, attachment, and invasion strategies of the pathogen1

3. It has an unusually high affinity for α-Fuc1-2Gal-containing oligosaccharides, with a dissociation constant (KD) of 2.5 × 10^-7 M for 2-fucosyllactose1

Recent research has provided insights into the structure and function of RSL:

1. X-ray crystallography has revealed that each monomer consists of two small four-stranded anti-parallel β-sheets1

2. The lectin has been crystallized with various ligands, including methyl-α-L-fucoside and 2-fucosyllactose16

3. Computational studies have been conducted to calculate the absolute binding free energy of RSL in complex with methyl-α-L-fucoside6

RSL’s potential biological target may be xyloglucan, a fucosylated polysaccharide found in the primary cell wall of plants1. This interaction could play a crucial role in the pathogen’s ability to colonize and infect host plants.

In summary, RSL is a valuable tool for researchers studying plant-pathogen interactions, bacterial adhesion mechanisms, and carbohydrate-protein interactions in various biological systems.