Agaricus Bisporus Lectin Production Service

Agaricus bisporus lectin (ABL) is derived from the edible mushroom with a molecular weight of 6.4 kDa. ABL has the ability to significantly bind to Thomsen Friedenreich antigen or T antigen. It has two distinct carbohydrate-binding sites, one that specifically binds to N-Acetamide-based glucose. ABL is a tetrameric structure with point group symmetry. Two binding sites are located in monomeric species of tetramers and are independent of each other.

ABL Extraction and Purification Service at CD BioGlyco

Remove all stains and dust from the surface of an Agaricus bisporus mushroom, and slice it. The sliced mushrooms are soaked in phosphate buffer overnight, homogenized, and extracted. The filtrate is centrifuged for supernatant extraction following filtration. Add ammonium sulfate salt to the mixture, collecting a precipitate fraction. For desalination, the precipitated part is dialyzed. Concentration and purification using DEAE-agarose columns. Collect in separate tubes. Tube-by-tube determination of hemagglutination activity and just collection of active components. The collected fractions are purified using an affinity chromatography column. After the collection, the active components are detected tube by tube. Collect target fractions, concentrate, and lyophilize.

ABL Analysis Service at CD BioGlyco

For the purification of lectins, it is necessary to carry out further studies on their active ingredients. CD BioGlyco has a robust glycobiology platform and trained technicians to help our clients analyze ABL quickly and accurately.

Relative molecular weight determination Three-dimensional structural analysis	Isoelectric focusing electrophoresis analysis Analysis of immunization mechanisms
Live cell agglutination activity analysis	Stability analysis (temperature, pH, metal ions)
Lectin gene amplification service	Activity services
Amino Acid Sequence	Lectin Microarray Assay

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

Publication

Paper Title: Edible mushroom (Agaricus bisporus) lectin inhibits human retinal pigment epithelial cell proliferation in vitro

Journal: Wound Repair and Regeneration

IF: 3.4

Published: 2003

Results: Studies have shown that ABL inhibits cell proliferation of a variety of cells by intervening in the cell division process without cytotoxicity. Lectins block the entry of the nuclear proteins by interfering with the nuclear pore. In addition, ABL binds to cytosolic proteins. In control cells, immunoreactive mitogen-activated protein kinases (MAPK) were found to be mainly localized to the nucleus with an insufficient effect on the MAPK input pathway. Thus, ABL inhibited the nuclear localization sequence (NLS) pathway but the cells were still able to survive.

Fig.2 Cellular observation plot of the effect of ABL on MAPK nuclear translocation. (Kent, et al., 2003) Fig.2 Cellular observation plot of the effect of ABL on MAPK nuclear translocation. (Kent, et al., 2003)

Applications of ABL

ABL is involved in the cell development process and significantly reversibly inhibits the proliferation of malignant epithelial cell lines.
ABL stimulates the immune system by increasing macrophage proliferation and has antiproliferative activity against breast cancer cells, which is used as a target for anticancer drug development.
ABL has a potent anti-proliferative effect on malignant colonocytes, this property confers its important therapeutic potential as an antitumor agent.
Notably, ABL inhibits the growth of cancer cells but has no effect on normal cells. It could be a potential tool for cancer therapy.

CD BioGlyco provides high-purity Lectin Production Services to clients with the support of trained technicians. Our services involve natural lectins from Plants, Animals, and Fungi. Our conscientious and professional services are recognized by our clients. Please feel free to contact us.

References

Kent, D.; et al. Edible mushroom (Agaricus bisporus) lectin inhibits human retinal pigment epithelial cell proliferation in vitro. Wound Repair Regen. 2003, 11(4): 285-91.
Carrizo, M.E.; et al. The antineoplastic lectin of the common edible mushroom (Agaricus bisporus) has two binding sites, each specific for a different configuration at a single epimeric hydroxyl. J Biol Chem. 2005, 280(11): 10614-23.

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