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001-es BibID:BIBFORM100414
035-os BibID:(cikkazonosító)2498 (scopus)85125084009 (wos)000772754000001
Első szerző:Diós Ádám (molekuláris biológus)
Cím:Changes in Non-deamidated versus Deamidated Epitope Targeting and Disease Prediction during the Antibody Response to Gliadin and Transglutaminase of Infants at Risk for Celiac Disease / Ádám Diós, Bharani Srinivasan, Judit Gyimesi, Katharina Werkstetter, Rudolf Valenta, Sibylle Koletzko, Ilma R. Korponay-Szabó
ISSN:1661-6596 1422-0067
Megjegyzések:Celiac disease (CeD) is a conditional autoimmune disorder with T-cell mediated immune response to gluten coupled with antibody production to gliadin and the self-protein tissue transglutaminase (TG2). TG2 contributes to CeD pathomechanism by deamidating gliadin, thereby generating more immunogenic peptides. Anti-gliadin antibodies may appear before the autoantibody production. The scope of this study was to dissect these early antibody responses by investigating serum sam-ples collected during the PreventCD prospective double-blind study (, where infants with high CeD risk were randomized to 200 mg daily gluten intake or to placebo from 4 to 6 months of age, then followed by frequent blood testing on regular gluten consumption in both groups. After primary gluten intake, children with or without later CeD produced IgA and IgG antibodies which preferentially recognized non-deamidated gliadin peptides. At CeD development with anti-TG2 seroconversion, there was a significant increase in the antibody reac-tion toward deamidated gliadin peptides (DGP) with maturation in the binding strength for the PEQPFP gamma-gliadin core peptide. The earliest produced autoantibodies targeted TG2's celiac epitope 2. Our results reveal a qualitative change in the gliadin-directed humoral immune re-sponse at the time when anti-TG2 antibodies appear, but anti-DGP antibodies in the absence of anti-TG2 antibodies are not disease-predictive.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
celiac disease
deamidated gliadin peptides
transglutaminase antibody
Megjelenés:International Journal Of Molecular Sciences. - 23 : 5 (2022), p. 1-16. -
További szerzők:Srinivasan, Bharani Gyimesi Judit Werkstetter, Katharina (gyermekgyógyász, gasztroenterológus) Valenta, Rudolf Koletzko, Sibylle Korponay-Szabó Ilma (1959-) (gyermekgyógyász)
Pályázati támogatás:NKFIH 120392
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat


001-es BibID:BIBFORM096052
Első szerző:Diós Ádám (molekuláris biológus)
Cím:Gamma-gliadin specific celiac disease antibodies recognize p31-43 and p57-68 alpha gliadin peptides in deamidation related manner as a result of cross-reaction / Ádám Diós, Rita Elek, Ildikó Szabó, Szilvia Horváth, Judit Gyimesi, Róbert Király, Katharina Werkstetter, Sibylle Koletzko, László Fésüs, Ilma R. Korponay-Szabó
ISSN:0939-4451 1438-2199
Megjegyzések:Celiac disease (CeD) is a T-cell-dependent enteropathy with autoimmune features where tissue transglutaminase (TG2)- mediated posttranslational modifcation of gliadin peptides has a decisive role in the pathomechanism. The humoral immune response is reported to target mainly TG2-deamidated γ-gliadin peptides. However, α-gliadin peptides, like p57-68, playing a crucial role in the T-cell response, and p31-43, a major trigger of innate responses, also contain B-cell gliadin epitopes and γ-gliadin like motifs. We aimed to identify if there are anti-gliadin-specifc antibodies in CeD patients targeting the p31-43 and p57-68 peptides and to examine whether deamidation of these peptides could increase their antigenicity. We explored TG2-mediated deamidation of the p31-43 and p57-68 peptides, and investigated serum antibody reactivity toward the native and deamidated α and γ-gliadin peptides in children with confrmed CeD and in prospectively followed infants at increased risk for developing CeD. We afnity-purifed antibody populations utilizing diferent single peptide gliadin antigens and tested their binding preferences for cross-reactivity in real-time interaction assays based on bio-layer interferometry. Our results demonstrate that there is serum reactivity toward p31-43 and p57-68 peptides, which is due to cross-reactive γ-gliadin specifc antibodies. These γ-gliadin specifc antibodies represent the frst appearing antibody population in infancy and they dominate the serum reactivity of CeD patients even later on and without preference for deamidation. However, for the homologous epitope sequences in α-gliadins shorter than the core QPEQPFP heptapeptide, deamidation facilitates antibody recognition. These fndings reveal the presence of cross-reactive antibodies in CeD patients recognizing the disease-relevant α-gliadins.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Celiac disease
Serum reactivity
Megjelenés:Amino Acids. - 53 : 7 (2021), p. 1051-1063. -
További szerzők:Elek Rita Szabó Ildikó (1981-) (biológus) Horváth Szilvia Gyimesi Judit Király Róbert (1975-) (biológus) Werkstetter, Katharina (gyermekgyógyász, gasztroenterológus) Koletzko, Sibylle Fésüs László (1947-) (orvos biokémikus) Korponay-Szabó Ilma (1959-) (gyermekgyógyász)
Internet cím:Szerző által megadott URL
Intézményi repozitóriumban (DEA) tárolt változat
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