A streamlined high-throughput platform for engineering glycosyltransferases and glucosidases
Background:
Glycosyltransferases are enzymes that commonly transfer monosaccharides to proteins and lipid scaffolds. These enzymes constitute ~2% of the coding human genome, representing over 200 proteins. Mutations in glycosyltransferases lead to disease; dysregulated glycosyltransferase expression occurs in metabolic diseases including cancers; modifications of glycosyltransferases offer therapeutic applications; and activity manipulations create novel biocatalysts. This technology provides a streamlined high-throughput platform for engineering glycosyltransferases and glycosidases.
Technology Overview:
This University of Buffalo technology offers a streamlined platform to perform scanning mutagenesis of arbitrary glycosyltransferases using a novel surface-display platform, creating enzymes with modified activity for biotechnology and therapeutic development. This system allows immobilization of mammalian glycosyltransferase as type-II transmembrane proteins while incorporating a click-chemistry process for quantitating enzyme activity on single cells using natural substrates as acceptors.
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Advantages:
Applications:
Intellectual Property Summary:
US Provisional Patent Application 63/812,831 filed on May 27, 2025.
Stage of Development:
Proven application using multiple human sialyltransferases as well as sialyltransferases from species spanning evolutionary progress (fish, sea urchin, frog, monkey, pig, and human). Creation of a library of 1680 human glycosyltransferases to select for specific desired enzymatic properties, with high activity molecules deemed super-enzymes. Implementation continues to generate novel molecular species for clinical and commercial applications.
Licensing Status:
Available for licensing or collaboration.
Publications: