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Fine specificity of monoclonal antibodies against celiac disease–inducing peptides in the gluteome^1,2,3

¹ From the Department of Blood Transfusion and Immunohematology, Leiden University Medical Center, Leiden, Netherlands(CM, YK-W, PvV, AdR, JWD, FK, and LD), and the Center for Medical Systems Biology, Leiden University Medical Center, Leiden, Netherlands (PvV and AdR)

Background: In celiac disease patients, peptides derived from dietary gluten are recognized by HLA-DQ2-restricted CD4⁺ T cells, which results in inflammation. Such immune-stimulatory peptides are found in both gliadins and glutenins. Monoclonal antibodies (mAbs) against these peptides can be used to screen food for the presence of such peptides.

Objective: We aimed to determine the specificity of 5 mAbs raised against T cell stimulatory peptides found in - and -gliadins and in low- and high-molecular-weight glutenins and to compare it with the specificity of patient-derived T cells.

Design: The reactivity of the mAbs with gluten peptides, enzymatic gluten digests, and intact gluten proteins was determined and compared with that of gluten-specific T cells by using a combination of immunologic and biochemical techniques. Furthermore, the reactivity of the mAbs with gluten homologues in barley, rye, and oat was determined.

Results: The specificity of the mAbs largely overlaps with that of gluten-specific T cells. Moreover, mAbs detect several homologous peptides present in gluten proteins. All except the LMW-specific mAbs also detect storage proteins present in barley and rye, whereas the -gliadin-specific mAbs also recognize oat proteins.

Conclusion: The mAbs raised against T cell stimulatory peptides in gliadins and glutenins allow a comprehensive screen for the presence of harmful gluten and gluten-like proteins and peptides in food products. They can thus be used to guarantee the safety of food for celiac disease patients.