Aberrant glycosylation is a universal feature of cancer and contributes to the ability of malignant cells to evade the immune system, but the mechanism by which this occurs is not well understood. Elucidating how glycosylation can affect the immune system is key to designing cancer immunotherapies that would trigger the immune system to specifically target and kill cancer cells. My research incorporates glycobiology and mass spectrometry to identify glycosylated targets on tumor cells that contribute to immune activation or suppression. To do this, enrichment protocols and instrumentation methods were developed to characterize glycopeptides presented by the MHC class I and II processing pathways. These techniques are now being extended to identify sialic-acid containing ligands on the surface of tumor cells.

Investigating aberrant glycosylation in cancer using mass spectrometry: Insight for cancer immunotherapy design

253rd National Meeting (2017)

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