Abstract
We studied whether celiac disease (CD) patients produce antibodies against a novel gliadin peptide specifically generated in the duodenum of CD patients by a previously described pattern of CD-specific duodenal proteases. Fingerprinting and ion-trap mass spectrometry of CD-specific duodenal gliadin-degrading protease pattern revealed a new 8-mer gliadin-derived peptide. An ELISA against synthetic deamidated 8-mer peptides (DGP 8-mer) was used to study the presence of IgA anti-DGP 8-mer antibodies in plasma samples from 81 children (31 active CD patients (aCD), 17 CD patients on a gluten-free diet (GFD), 10 healthy controls (C) and 23 patients with other gastrointestinal pathology (GP)) and 101 adults (16 aCD, 12 GFD, 27 C and 46 GP-patients). Deamidation of the 8-mer peptide significantly increased the reactivity of the IgA antibodies from CD patients against the peptide. Significant IgA anti-DGP 8-mer antibodies levels were detected in 93.5% of aCD-, 11.8% of GFD- and 4.3% of GP-patients in children. In adults, antibodies were detected in 81.3% of aCD-patients and 8.3% of GFD-patients while were absent in 100% of C- and GP-patients. Duodenal CD-specific gliadin degrading proteases release an 8-mer gliadin peptide that once deamidated is an antigen for specific IgA antibodies in CD patients which may provide a new accurate diagnostic tool in CD.
Highlights
Celiac disease (CD) is a gluten-sensitive enteropathy that develops in genetically susceptible individuals following exposure to dietary wheat gluten and similar proteins from barley, rye and some varieties of oats [1,2,3] (Highlights S1).Prolamins constitute eighty percent of total gluten proteins
In order to study the possible implication of these proteases, independently of their origin, in the development of CD, here we studied whether a 8-mer gliadin peptide released by the action of duodenal CD-specific gliadin-degrading proteases could be specific epitopes of IgA antibodies found in the plasma of CD patients
In this manuscript we report for the first time to our knowledge an 8-mer gliadin-derived peptide generated in the CD duodenum, that likely deamidated by tissue transglutaminase (tTG), is an epitope of specific IgAs found in plasma samples from CD patients, providing a potential utility as diagnostic biomarkers and/or markers to monitor glutenfree diet (GFD) compliance
Summary
Celiac disease (CD) is a gluten-sensitive enteropathy that develops in genetically susceptible individuals following exposure to dietary wheat gluten and similar proteins from barley, rye and some varieties of oats [1,2,3] (Highlights S1). In order to study the possible implication of these proteases, independently of their origin, in the development of CD, here we studied whether a 8-mer gliadin peptide released by the action of duodenal CD-specific gliadin-degrading proteases could be specific epitopes of IgA antibodies found in the plasma of CD patients. We studied if deamidation of the 8mer gliadin peptide increased its reactivity against the IgA Abs and if the latter were altered in CD patients following a GFD In this manuscript we report for the first time to our knowledge an 8-mer gliadin-derived peptide generated in the CD duodenum, that likely deamidated by tTG, is an epitope of specific IgAs found in plasma samples from CD patients, providing a potential utility as diagnostic biomarkers and/or markers to monitor GFD compliance
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