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Clinical Chemistry 50: 2370-2375, 2004. First published October 7, 2004; 10.1373/clinchem.2004.036111
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(Clinical Chemistry. 2004;50:2370-2375.)
© 2004 American Association for Clinical Chemistry, Inc.

Clinical Immunology

Serologic Assay Based on Gliadin-Related Nonapeptides as a Highly Sensitive and Specific Diagnostic Aid in Celiac Disease

Elke Schwertz1, Franka Kahlenberg1, Ulrich Sack2, Thomas Richter3, Martin Stern4, Karsten Conrad5, Klaus-Peter Zimmer6 and Thomas Mothes1,a

1 Institute of Laboratory Medicine, Clinical Chemistry and Molecular Diagnostics, and 2 Institute of Clinical Immunology, University Hospital, Leipzig, Germany.
3 Department of Paediatrics, St. George’s Hospital, Leipzig, Germany.
4 Children’s Hospital, University of Tübingen, Tübingen, Germany.
5 Institute of Immunology, Technical University of Dresden, Dresden, Germany.
6 Department of Paediatrics, University of Münster, Münster, Germany.

aAddress correspondence to this author at: Institut für Laboratoriumsmedizin, Klinische Chemie und Molekulare Diagnostik, Universitätsklinikum A. ö. R., Liebigstrasse 27, D-04103 Leipzig, Germany. Fax 49-341-9722209; e-mail mothes{at}medizin.uni-leipzig.de.

Background: Celiac disease (CD) is induced by wheat gliadins and related cereal proteins. Anti-gliadin antibodies (AGAs) are present in the serum of CD patients, but these antibodies have lower diagnostic specificity and sensitivity than autoantibodies [anti-endomysium antibodies (AEmAs) and anti-tissue transglutaminase antibodies (AtTGAs)]. Recently, AGAs from CD patients were found to recognize deamidated gliadin peptides, probably formed by the action of tissue transglutaminase.

Methods: We synthesized several gliadin peptides and their glutamine-glutamic acid-substituted counterparts on cellulose membranes and tested their recognition by IgA in sera of 52 AEmA-positive CD patients and 76 AEmA-negative controls in a luminescence assay. For comparison, we assayed IgA concentrations of AGAs, AtTGAs, and AEmAs. For measurement of AtTGAs, we used the human recombinant antigen.

Results: We identified several nonapeptides that were detected with high specificity by IgA in CD patients. Diagnostic accuracy of the peptide antibody assay was highest when peptide PLQPEQPFP was used in combination with peptide PEQLPQFEE within one assay. AGAs were above the cutoff in 14 of the controls, but only 5 of the controls were positive for peptide antibodies. For comparison, 82% and 94% of samples were correctly classified by AGAs and the combination nonapeptide assay, respectively (P = 0.007), and the AtTGAs correctly classified 98%.

Conclusion: The peptide antibody assay has higher diagnostic accuracy than AGAs for distinguishing patients with CD from controls, and has diagnostic accuracy similar to that of AtTGAs.




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