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Structural basis for gluten intolerance in celiac sprue.

Lu Shan1, Øyvind Molberg, Isabelle Parrot

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A specific gluten peptide triggers Celiac Sprue (an autoimmune intestinal disease) by resisting digestion and activating immune cells. Bacterial enzymes may offer a therapeutic detoxification strategy.

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Area of Science:

  • Gastroenterology and Immunology
  • Autoimmune Diseases
  • Molecular Biology

Background:

  • Celiac Sprue is a common autoimmune disorder affecting the small intestine.
  • Gluten exposure in genetically susceptible individuals triggers the disease.
  • The precise initiating factor of the inflammatory response remains under investigation.

Purpose of the Study:

  • To identify the primary initiator peptide of the inflammatory response in Celiac Sprue.
  • To investigate the peptide's stability, interaction with autoantigens, and immunogenicity.
  • To explore potential therapeutic strategies for Celiac Sprue.

Main Methods:

  • Identification and characterization of a specific 33-mer peptide from gluten.
  • In vitro and in vivo studies assessing peptide stability against digestive proteases.
  • Assays measuring peptide reactivity with tissue transglutaminase and induction of T cell responses.

Main Results:

  • A 33-mer peptide was identified as resistant to breakdown by gastric, pancreatic, and intestinal proteases.
  • This peptide selectively reacted with tissue transglutaminase, a key autoantigen in Celiac Sprue.
  • The peptide potently induced gut-derived T cell lines from all tested Celiac Sprue patients and is present in toxic grains.

Conclusions:

  • The identified 33-mer peptide is likely the primary initiator of gluten-induced inflammation in Celiac Sprue.
  • Its stability and interaction with tissue transglutaminase contribute to its pathogenicity.
  • Detoxification using bacterial prolyl endopeptidase suggests a potential oral therapy for Celiac Sprue.