Glycosylated biomolecules are found all over the biological systems, and glycans play critical roles from extracellular structures to molecular signaling. Abnormality in glycosylation is associated with diseases such as cancer, autoimmune disorders, and infectious diseases. Analyzing glycoprofiles can offer insights into disease mechanisms and potential therapeutic targets. GGI has developed over 100 clones of human cell lines, each with a defined glycotransferase gene knocked out. This is a genetically validated, tractable cell-based glycan display platform for. Our continuous cell line-generation efforts aim to expand this cell line collection to other types of glycogenes, e.g. lectins and key glycoproteins. We aim to apply this total glycogene-KO collection for glycobiology-centric therapeutic target discovery.

Human lectins are critical sensors to translate glycoprofiles into biological cues. Recombinant human lectins serve as versatile tools in probing and enriching biomolecules of specific glycosylated states. At GlycoGenetics, we aim to recombinantly produce a comprehensive collection of human lectins. This lectin collection, in combination with our Glycogene-KO Collection, allows us to curate comprehensive, genetically defined binding profiles of each lectin, and to guide users in choosing the right lectins for their scientific exploration. 

Beyond glycogenomics, GlycoGenetics is a dedicated toolmaker. We have created a recombination-based mutagenesis method called RIFFLE. RIFFLE allows us to capture and shuffle functional DNA fragments in a highly efficient manner. RIFFLE allows us to fuse functional domains of proteins of interest for advanced applications. Beyond protein engineering,  RIFFLE is capable of shuffling large DNA fragments, enabling pathway engineering strain optimization for synthetic biology.