Polyporus Squamosus Lectin Production Service

Polyporus squamosus lectin (PSL) is a Natural Lectin with high specificity. It is composed of two identical 28 kDa subunits, connected by non-covalent bonds. PSL binds the β-D-galactoside, carrying an extended binding site. This site has a strong specificity and affinity for Neu5acα2,6Galβ1,4Glc/Glc/GlcNAc but does not bind to the mucin-derived O-chain Neu5Acα2-6GalNAc sequence. In addition, PSL agglutinates human A, B, O, and rabbit erythrocytes. Currently, PSL has been a valuable tool for glycobiology research in biomedical and cancer research.

PSL Extraction and Purification Service at CD BioGlyco

We provide a complete set of fungal lectin production services, including extraction, isolation, purification and characterization, etc. For PSL, we obtain a high-purity PSL by double-column purification. Notably, all extractions and purifications are operated at low temperatures. The specific services are as follows:

Collection of the fruiting body of the Polyporus squamosus, which grows naturally in rotting conditions. Surface dust is removed and cleaned. We homogenize the specimens and collect supernatants by centrifugation. Let stand for the night by adding a steady dose of ammonium sulfate. The residue is removed by centrifugation. The supernatant is purified using a galactose affinity chromatography column. Collection of affinity adsorbed lectins under the elution of the buffer. To obtain a crude lectin product, the fractions are collected by dialysis and lyophilized.
The crude product is dissolved in phosphate buffer and purified using a DEAE-ion exchange column. Collection of target components in absorbance-monitored states. Dialysis with distilled water, and freeze-drying to obtain pure product.

PSL Analysis Service at CD BioGlyco

An in-depth analysis of PSL is essential to understand its specificity and, meanwhile, expands its application as a diagnostic tool. With bovine serum albumin as the standard, we provide the protein content detection service. Moreover, we provide precise molecular mass and molecular structure analysis services, amino acid composition analysis services, N-terminal sequence analysis services, quantitative precipitation, and hapten inhibition assay services. Notably, we offer a wide range of PSL Couplers.

Fig.1 Schematic diagram of PSL production services. (CD BioGlyco)

Publication

Paper Title: Structure and binding analysis of Polyporus squamosus lectin in complex with the Neu5Acα2-6Galβ1-4GlcNAc human-type influenza receptor

Technology: X-ray crystallography; Computational simulations; Protein Interfaces; Surfaces and Assemblies (PISA)

Journal: Glycobiology

IF: 5.594

Published: 2011

Results: The C-terminal structural domain of PSL consists of three parts. A five-stranded β-sheet in the center, flanked by three α-helices, and a short chain at the top. The Gal-binding motifs in the PSL are only two and located in the β and γ. The β subdomain is the most probable binding site in the N-terminal domain. The γ domain probably retains the affinity for Gal binding but has a weaker binding capacity than the β subdomain. The high affinity of PSL to Neu5Ac residues is formed by the interaction of a loop in the adjacent subdomains of the typical gal binding subdomain, and a key serine residue (Ser 32 in PSL) interacts with the carboxylate group of the Neu5Ac residue. This finding facilitated the development of PSL in the emerging field of glucomimetic drug design.

Fig.2 Stereoscopic view of the hydrogen bonding network in a complex. (Kadirvelraj, et al., 2011) Fig.2 Stereoscopic view of the hydrogen bonding network in a complex. (Kadirvelraj, et al., 2011)

Applications of PSL

PSL plays a key role in the screening and separation of glucuronidated sugar conjugates.
PSL is particularly suited for histological investigation of associated influenza adherence.
PSA binding site for more than one carbohydrate moiety. This specificity makes PSL an invaluable tool for glycobiology research, especially for cancer research and diagnostics.
Notably, the unique glycan conformation of PSA allows it to play an important role in glycomimetic drug design.

CD BioGlyco is a specialized glycobiology company. We have state-of-the-art instrumentation and a team of well-trained personnel to provide comprehensive Lectin Production Services to our clients. Please feel free to contact us.

References

Mo, H.; et al. Purification and characterization of a Neu5Acalpha2-6Galbeta1-4Glc/GlcNAc-specific lectin from the fruiting body of the polypore mushroom Polyporus squamosus. J Biol Chem. 2000, 275(14): 10623-9.
Kadirvelraj, R.; et al. Structure and binding analysis of Polyporus squamosus lectin in complex with the Neu5Acα2-6Galβ1-4GlcNAc human-type influenza receptor. Glycobiology. 2011, 21(7): 973-84.

This service is for Research Use Only, not intended for any clinical use.