Our proprietary technology platform enables the development of antibodies with unrivaled tumor-specificity

Our antibodies target specific tumor-associated carbohydrate structures or protein/carbohydrate combined glyco-epitopes (GlycoTargets). Targeting these specific antigens enables broad indication range, long-term treatment potential and reduced on-target/off tumor toxicity, which is key for highly potent therapies. Based on this unrivalled tumor-specificity, our antibodies are highly suitable for a multi-function platform approach with independent modes of action to provide a tailored therapy format for as many patients as possible.

The pioneer of this concept is our lead antibody GT-00A which is developed in multiple different formats, including an antibody-drug-conjugate (ADC) developed by Daiichi-Sankyo, an IL-15-based immune-cytokine (internal development), or in the field of cellular therapies such as CAR-T (undisclosed partner) or CAR-NK by ONK Therapeutics. In addition to GT-00A and its various formats, Glycotope is currently developing novel antibodies against additional early targets.

GlycoTarget Discovery:

GlycoTargets are tumor-associated carbohydrate structures or combined epitopes consisting of a protein backbone and a tumor-associated carbohydrate structure. By combining the advantages of classical protein antigens and the high tumor specificity of cancer-associated glycan structures a unique class of highly-tumor specific antigens is obtained.

We have set up a unique multiparameter approach consisting of cellular screenings, bioinformatics and mass spectrometry to identify proteins with cancer-specific glycopeptide epitopes (GlycoTargets). Glycotope has to date discovered in excess of 150 GlycoTargets with antibodies against several of these targets currently under development.

Glycosylated proteins in cancer therapy:

The ideal tumor antigen is constitutively expressed by the tumor and absent on healthy tissue. Glycans tend to elicit superior tumor specificity as compared to proteins, since glycosylation is strongly altered in cancer, reflecting the drastic changes in tumor metabolism. The changes in glycosylation are mostly due to mutated or mislocated glycosyltransferases and glycosidases, giving rise to highly fucosylated, highly sialylated and truncated glycans. These glycans carry tumor-associated epitopes like the Thomsen-Friedenreich (TF) and the Thomsen novelle (Tn) antigen as well as their respective sialylated forms sTF and sTn. Additionally, glycans present on a subset of blood cells can be expressed by solid tumors. We use these altered glyco-structures to develop highly tumor-specific antibodies for cancer therapy.