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001-es BibID:BIBFORM096524
035-os BibID:(cikkazonosító)131148 (WoS)000715095400003 (Scopus)85118350160
Első szerző:Birinyi Zsófia
Cím:Immunoanalytic investigation of grain proteins antigenic for celiac disease patients in an einkorn collection / Birinyi Zsófia, Réder Dalma, Diós Ádám, Korponay-Szabó Ilma R., Hunyadi-Gulyás Éva, George Florides Christakis, Juhász Angéla, Gell Gyöngyvér
Dátum:2022
ISSN:0308-8146
Megjegyzések:Our study focuses on the complex characterization of the wild and cultivated einkorn collection of the Cereal Gene Bank of Agriculture Research Institute in Hungary, using proteomics, immune analytics and bioinformatics analyses. In serological ELISA pre-screen of 208 different Triticum monococcum L. ssp. monococcum and Triticum monococcum L. ssp. aegilopoides genotypes with celiac disease samples high diversity was observed in the immune response. Based on the immune analytic results, four genotypes with significantly reduced immune reactivity were selected for detailed proteomics characterization. Our results confirm the benefits of high-throughput/large scale pre-screening and the use of a complex examination platform to get relevant information about the genetic diversity of celiac disease-relevant proteins in the analyzed einkorn genotypes. These genotypes cannot be incorporated into the daily diet of celiac patients; however, they may represent candidates ? especially in combination with enzymatic treatments - to improve the lifestyle of individuals suffering from other clinical conditions like non-celiac gluten sensitivity.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
einkorn
celiac disease
prolamin
ELISA
LC-MS
HPLC
Megjelenés:Food Chemistry. - 371 (2022), p. 1-11. -
További szerzők:Réder Dalma Diós Ádám (1994-) (molekuláris biológus) Korponay-Szabó Ilma (1959-) (gyermekgyógyász) Hunyadi-Gulyás Éva Florides, Christakis George Juhász Angéla Gell Gyöngyvér
Pályázati támogatás:PD 115641
OTKA
NKFIH120392
NKFIH
GINOP-2.3.2-15-2016-00028
GINOP
GINOP 2.3.2-15-2016-00015
GINOP
GINOP 2.3.2-15-2016-00001
GINOP
ÚNKP-18- 568 4-BME-393
Egyéb
ÚNKP-19-4-BME-417
Egyéb
ÚNKP-20-5-BME-292
Egyéb
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

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
Dátum:2022
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 (www.preventcd.com), 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
folyóiratcikk
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
OTKA
EFOP-3.6.1-16-2016-00022
EFOP
DTP3-571-1.2
Egyéb
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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3.

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
Dátum:2021
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
folyóiratcikk
Celiac disease
Gliadin
Deamidation
Antibody
Serum reactivity
Cross-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)
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