Monoclonal IgM Antibody from Entirely Carbohydrate Construct Binds and Kills Human Tumor Cells


Project ID: D2015-13


Truncated patterns of oligosaccharides on the surfaces of cancer cells can serve as biomarkers that help to distinguish tumor cells from healthy ones. These are known as tumor-associated carbohydrate antigens (TACAs). A significant portion of cancer antigens have been identified as TACAs. Thus TACAs can be exploited for cancer immunotherapy. However, the immunological nature of carbohydrate epitopes renders TACAs unable to elicit strong T cell-dependent immune responses. TACAs have also failed to induce class switching for high affinity IgG antibodies and memory B cells. Antigen carriers can be used to overcome this hurdle. However, bacterial-based glycoprotein conjugates may suffer from epitope suppression as well as heterogeneities and ambiguities in chemical composition due to non-site specific coupling. Protein conjugation may also still result in epitope suppression and unwanted immune response to non-natural hydrocarbon linkers. It is essential to develop new immunogen strategies that target glycosides. The Thomsen-nouveau (Tn) cluster provides enough surface area for binding due to the strong avidity of monoclonal IgM antibodies.


Invention Description

Researchers from The University of Toledo have developed a novel IgM antibody that is specific and selective for the carbohydrate portion of the Tn antigen. This monoclonal antibody (mAb) has demonstrated exceptional binding to the glycoside portion of the Tn and Thomsen-Friedenreich (TF) antigens in ELISA. The mAb has been shown to bind to known cancer cells in flow cytometry and demonstrates complement-mediated killing of human tumor cells both in vivo and in vitro.   



•       The technology may be used for the diagnosis and prognosis of carcinomas

•       The monoclonal antibody may be used for cancer immunotherapy



•       The monoclonal IgM antibody is specific and selective for the Tn cancer antigen

•       The mAb demonstrates exceptional binding to the glycoside portion of the Tn antigens in ELISA

•       As compared to commercial monoclonal antibodies, the IgM can specifically recognize the Tn antigen without assistance from peptides or proteins or a combination of both

•       The mAb offers greater avidity because of multiple fragment antigen-binding sites


IP Status:  Patent Pending


Publications:       Trabbic KR, et al., Immunological evaluation of the entirely carbohydrate-based Thomsen-Friedenreich-PS B conjugate. Organic & Biomolecular Chemistry, 2016, 3350-3355

              Shi M, et al., Sialyl-Tn polysaccharide A1 as an entirely carbohydrate immunogen: Synthesis and immunological evaluation. Journal of American Chemical Society, 2016, 14264-14272


Patent Information:
For Information, Contact:
Stephen Snider
AVP Tech Transfer
The University of Toledo
419 530 6225
Peter Andreana
Kevin Trabbic
Mengchao Shi
Jean Bourgault