Deamidated Gliadin Peptides Form Epitopes That Transglutaminase Antibodies Recognize
  • Metaadatok
Tartalom: http://dx.doi.org/10.1097/MPG.0b013e31815ee555
Archívum: MTA Könyvtár
Gyűjtemény: Status = Published


Type = Article
Cím:
Deamidated Gliadin Peptides Form Epitopes That Transglutaminase Antibodies Recognize
Létrehozó:
Korponay-Szabó, Ilma Rita
Vecsei, Zsófia
Király, Róbert
Dahlbom, Ingrid
Chirdo, Fernando
Nemes, Éva
Fésüs, László
Maki, Markku
Kiadó:
Lippincott, Williams and Wilkins
Dátum:
2008
Téma:
RC Internal medicine / belgyógyászat
RJ Pediatrics / gyermekgyógyászat
Tartalmi leírás:
Objective: Deamidated gliadin peptides are efficient antigens in diagnostic tests for celiac disease, and results correlate better with transglutaminase 2-based assays than those with native gliadin. We investigated whether deamidated gliadin antigens are structurally similar to transglutaminase 2 or could mimic transglutaminase epitopes.
Patients and Methods: Serum samples from 74 celiac and 65 control patients, and 13 different transglutaminase 2-specific monoclonal mouse antibodies were investigated for their binding to commercially available deamidated gliadin peptides using enzyme-linked immunosorbent assay, competition studies, and molecular modelling.
Results: The enzyme-linked immunosorbent assay with deamidated gliadin peptides had 100% sensitivity and 98.5% specificity in patients. Deamidated gliadin epitopes also were recognized by 3 transglutaminase-specific monoclonal antibodies, and antibodies affinity-purified with deamidated gliadin peptides from celiac patient sera reacted with transglutaminase but did not show endomysial binding. The binding of the monoclonal antibodies to deamidated gliadin was inhibited dose dependently by full-length recombinant human transglutaminase, its fragments containing the binding sites of these monoclonal antibodies, or by celiac patient antibodies. Deamidated gliadin peptides decreased the binding of transglutaminase-specific monoclonal antibodies to transglutaminase. Three different cross-reacting transglutaminase epitopes were found, of which 2 are located in the C-terminal domain and I is conformational. The binding of celiac serum samples to deamidated gliadin peptides could not be abolished by transglutaminase or by any of the transglutaminase-specific monoclonals, indicating that celiac sera also contain additional antibodies to gliadin epitopes different from transglutaminase.
Conclusions: Certain deamidated gliadin-derived peptides and transglutaminase 2 epitopes have similar 3-dimensional appearance. This homology may contribute to the induction of transglutaminase autoantibodies by molecular mimicry.
Típus:
Article
PeerReviewed
Formátum:
application/pdf
Azonosító:
Korponay-Szabó, Ilma Rita and Vecsei, Zsófia and Király, Róbert and Dahlbom, Ingrid and Chirdo, Fernando and Nemes, Éva and Fésüs, László and Maki, Markku (2008) Deamidated Gliadin Peptides Form Epitopes That Transglutaminase Antibodies Recognize. Journal of Pediatric Gastroenterology and Nutrition, 46 (3). pp. 253-261. ISSN 0277-2116 (print), 1536-4801 (online)
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