Immune response to Thomsen-Friedenreich disaccharide and glycan engineering

IRAZOQUI FERNANDO J; SENDRA VICTOR G; LARDONE RICARDO D; NORES GUSTAVO A

IMMUNOLOGY AND CELL BIOLOGY

Blackwell Publishing

Lugar: Oxford; Año: 2005 vol. 83 p. 405 - 405

0818-9641

p class="abstract">Cancer-associated mucins show frequent alterations of their oligosaccharide chain profile, with a switch to unmask normally cryptic O-glycan backbone and core regions. Epithelial tumour cells typically show overexpression of the uncovered Gal(beta)1-3GalNAc(alpha)-O-Ser/Thr (Core 1) structure, known as the T antigen or the Thomsen-Friedenreich antigen, the oligosaccharide chain of which is called the Thomsen-Friedenreich disaccharide (TFD). T antigen expression has been associated with immunosuppression, metastasis dissemination, and the proliferation of cancer cells. Several different strategies have been used to trigger a specific immune response to TFD. Natural T antigen and synthetic TFD residues have low immunodominance. In the T antigen, flexibility of the glycosidic bond reduces the immunogenicity of the sugar residue. Enhanced rigidity should favour certain glycan conformations and thereby improve TFD immunotargeting. We propose the term ´glycan engineering´