The Celiac-Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model.
Angew Chem Int Ed Engl
; 63(21): e202317552, 2024 05 21.
Article
in En
| MEDLINE
| ID: mdl-38497459
ABSTRACT
Celiac disease (CeD) is an autoimmune disorder triggered by gluten proteins, affecting approximately 1 % of the global population. The 33-mer deamidated gliadin peptide (DGP) is a metabolically modified wheat-gluten superantigen for CeD. Here, we demonstrate that the 33-mer DGP spontaneously assembles into oligomers with a diameter of approximately 24â
nm. The 33-mer DGP oligomers present two main secondary structural motifs-a major polyproline II helix and a minor ß-sheet structure. Importantly, in the presence of 33-mer DGP oligomers, there is a statistically significant increase in the permeability in the gut epithelial cell model Caco-2, accompanied by the redistribution of zonula occludens-1, a master tight junction protein. These findings provide novel molecular and supramolecular insights into the impact of 33-mer DGP in CeD and highlight the relevance of gliadin peptide oligomerization.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Celiac Disease
/
Enterocytes
/
Gliadin
Limits:
Humans
Language:
En
Journal:
Angew Chem Int Ed Engl
/
Angew. Chem. (Int. ed., Internet)
/
Angewandte Chemie (International ed. Internet)
Year:
2024
Document type:
Article
Affiliation country:
Germany
Country of publication:
Germany