The recombinant glycan-binding protein Ab-Y3, found in an edible, common mushroom, is useful for detecting, isolating, purifying, and screening proteins with specific N-glycans of medical significance, such as immunoglobins or IgG proteins. Glycan binding proteins are critical for a number of biological functions and are promising drug candidates and tools for the detection and treatment of cancer and many other diseases. Recombinant glycoprotein therapies are becoming increasingly common, including in applications to fight COVID-19, and the market for profiling and characterizing glycosylated molecules should reach $2.5 billion by 2030. Due to limitations in analytical techniques, high structural diversity, and rapid evolution of glycans, knowledge of glycan-binding proteins is generally limited to only a handful of proteins.
Researchers at the University of Florida have developed a system for producing a glycan-binding protein to detect, isolate, and purify certain N-glycosylated proteins. The glycan-binding protein detects unique glycosylation patterns and can screen for therapeutic proteins.
Glycan binding protein derived from low-cost mushrooms to isolate, purify, and screen for certain therapeutic proteins with N-glycans
This yeast expression system produces high yields of the glycan-binding protein, Agaricus bisporus lectin, occurring naturally in the common mushroom species, Agaricus bisporus. The produced glycan-binding protein has a unique binding specificity for glycans with Man3GlcNAc2 core structure and Gal-GlcNAc branches in human cell line-expressed recombinant proteins. Agaricus bisporus lectin can be useful for detecting, isolating, and purifying therapeutic proteins and antibodies with medically important complex N-glycans.
