Wheat gluten confers superior baking
quality to wheat based products
but elicits a pro-inflammatory immune response in patients with celiac
disease. Transamidation of gluten by microbial transglutaminase (mTG)
and tissue transglutaminase (tTG) reduces the immunogenicity of gluten;
however, little information is available on the minimal modification
sufficient to eliminate gliadin immunogenicity nor has the effectiveness
of transamidation been studied with T-cell clones from patients. Here
we demonstrate that mTG can efficiently couple three different acyl-acceptor
molecules, l-lysine, glycine ethyl ester, and hydroxylamine,
to gliadin peptides and protein. While all three acyl-acceptor molecules
were cross-linked to the same Q-residues, not all modifications were
equally effective in silencing T-cell reactivity. Finally, we observed
that tTG can partially reverse the mTG-catalyzed transamidation by
its isopeptidase activity. These results set the stage to determine
the impact of these modifications on the baking quality of gluten
proteins and in vivo immunogenicity of such food products.