Gluten derived from wheat and related Triticeae can induce gluten sensitivity as well as celiac disease. Consequently, gluten content in foods labeled "gluten-free" is regulated. Determination of potential contamination in such foods is achieved using immunoassays based on monoclonal antibodies (mAbs) that recognize specific epitopes present in gluten. However, food-processing measures can affect epitope recognition. In particular, preparation of wheat protein isolate through deamidation of glutamine residues significantly limits the ability of commercial gluten testing kits in their ability to recognize gluten. Adding to this concern, evidence suggests that deamidated gluten imparts more pathogenic potential in celiac disease than native gluten. To address the heightened need for antibody-based tools that can recognize deamidated gluten, we have generated a novel mAb, 2B9, and subsequently developed it as a rapid lateral flow immunoassay. Herein, we report the ability of the 2B9-based lateral flow device (LFD) to detect gluten from wheat, barley, and rye and deamidated gluten down to 2 ppm in food as well as its performance in food testing.
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http://dx.doi.org/10.1021/acs.jafc.5b06085 | DOI Listing |
Scand J Gastroenterol
December 2024
Norwegian Coeliac Disease Research Centre, Institute of Clinical Medicine, University of Oslo, Oslo, Norway.
Objectives: Concurrent type 1 diabetes (T1D) and celiac disease (CeD) pose challenges in insulin dosage adjustments and gluten-free dietary adherence. Urine testing for gluten immunogenic peptides (GIP) is a new method to detect gluten exposure within the last 3-12 h. Our aims were to compare gluten-free dietary adherence between T1D + CeD and CeD individuals and evaluate urinary GIP testing in an outpatient setting.
View Article and Find Full Text PDFChemMedChem
December 2024
Molecular Cell Biology, Faculty of Medicine, Ruhr University Bochum, Universitätsstr. 150, 44801, Bochum, Germany.
The 33-mer gliadin peptide and its deamidated derivative, known as 33-mer DGP, are proteolytically resistant peptides central to the pathomechanism of celiac disease (CeD), the autoimmune presentation of gluten-related disorders (GRD). Both peptides can form spontaneous oligomers in the nanomolar concentration, leading to the formation of nanostructures. In other protein-related diseases, oligomers and aggregates are central in their pathomechanism; therefore, it was hypothesized that the oligomerization of proteolytical-resistant 33-mer gliadin peptides could be an underrecognized disease trigger.
View Article and Find Full Text PDFAliment Pharmacol Ther
October 2024
Department of Pediatric Research, Faculty of Medicine, University of Oslo, Oslo, Norway.
Proc Natl Acad Sci U S A
July 2024
Department of Chemistry, Stanford University, Stanford, CA 94305.
Mammalian transglutaminases, a family of Ca-dependent proteins, are implicated in a variety of diseases. For example, celiac disease (CeD) is an autoimmune disorder whose pathogenesis requires transglutaminase 2 (TG2) to deamidate select glutamine residues in diet-derived gluten peptides. Deamidation involves the formation of transient γ-glutamyl thioester intermediates.
View Article and Find Full Text PDFNat Immunol
July 2024
Celiac Disease Research Center, Faculty of Medicine and Health Technology, Tampere University and Tampere University Hospital, Tampere, Finland.
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