Unmet Need
Aberrant glycosylation has been implicated as a mechanism of cancer progression. Accordingly, identifying the differences in glycan structures within clinical specimens, cancer, and normal cells provides a unique opportunity to identify new biomarkers and therapeutic targets. In particular, Tn antigen (Tn) is a simple O-linked glycan structure that is present in numerous cancer types, but typically absent in normal human samples. To date, the methods of detecting Tn glycosylation sites in cancer specimens in research and clinical applications have been limited. This is due to the technical challenges of identifying O-linked glycosylation sites. Consequently, novel methods of detecting Tn antigen in cancer specimens would improve our understanding of cancer pathogenesis and have important clinical applications.
Technology Overview
The inventors have developed a technology that can map Tn-glycosylation sites on a large-scale. This approach, called EXoO-Tn, uses enzymatic digestion and liquid chromatography-mass spectrometry techniques to concurrently tag Tn antigen and map its glycosylation sites. The inventors validated this approach in Jurkat cells and demonstrated that this technology was able to map 947 glycosylation sites on 480 glycoproteins. Importantly, 888 of these Tn-glycosylation were exclusively identified using EXoO-Tn, highlighting the improved capabilities of this technology compared to other approaches.
Stage of Development
The inventors have validated this technology for research and development applications.
Publications
Yang, W et al. EXoO-Tn: Tag-n-Map the Tn Antigen in the Human Proteome. BioRxiv. November 2019. doi: 10.1101/840298.
Yang, W et al. Mapping the O-glycoproteome using site-specific extraction of O-linked glycopeptides (EXoO). Mol Syst Biol. 2018 Nov 20;14(11):e8486. doi: 10.15252/msb.20188486.
