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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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001-es BibID:	BIBFORM129426
035-os BibID:	(scopus)85217646339 (wos)001418597500001
Első szerző:	Korponay-Szabó Ilma (gyermekgyógyász)
Cím:	Development of Cell-Assembled Human Endomysial-Type Biomatrix Substrate for the Detection of Celiac Disease Autoantibodies / Korponay-Szabó Ilma R., Király Róbert, Gyimesi Judit, Mäki Markku
Dátum:	2025
ISSN:	1661-6596 1422-0067
Megjegyzések:	The endomysial antibody (EMA) immunofluorescent test is a highly specific method to detect disease-specific autoantibodies in celiac disease (CD) by their binding to natural transglutaminase-2 autoantigen in tissue sections, and it is used as a compulsory confirmatory test in the non-invasive diagnosis of CD. The classical EMA substrates are the monkey esophagus and the human umbilical cord. It is increasingly difficult to use these tissues due to ethical concerns and animal welfare regulations. In this study, we developed, in cell culture, an endomysium-type extracellular biomatrix assembled by human umbilical cord vein-derived endothelial cells which binds CD antibodies in a similar pattern as monkey esophagus and has similar macromolecular composition. Evaluating retrospectively and prospectively tested patient cohorts, including 130 CD cases and 105 non-celiac controls, IgA-class celiac antibody detection on the biomatrix was equally specific (100%) as EMA testing on tissues, and had higher sensitivity (95.6% versus 91.2%). Both EMA tests were less sensitive, but more specific than transglutaminase-based ELISA measurements. The decellularization of the biomatrix improved sensitivity, enabled the detection of IgG-class celiac antibodies, and allowed for simple reading without previous training. This easily available cell-assembled biomatrix substrate may replace substrate tissues in diagnostic EMA testing in the future.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk endomysial antibodies transglutaminase antibodies celiac disease diagnostic accuracy monkey esophagus
Megjelenés:	International Journal Of Molecular Sciences. - 26 : 3 (2025), p. 1-18. -
További szerzők:	Király Róbert (1975-) (biológus) Gyimesi Judit Mäki, Markku
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001-es BibID:	BIBFORM121546
Első szerző:	Korponay-Szabó Ilma (gyermekgyógyász)
Cím:	Search for gluten non-dependent prospective biomarkers for in vitro diagnostic use : 16th International Coeliac Disease Symposium 21-24 June 2015, Prague / Korponay-Szabó I. R., Kerekes-Tóth B., Gyimesi J., Barta-Tóth B., Bogáti R., Király R., Caja Galan S., Nadalutti C., Lindfors K., Maki M., Fésüs L.
Dátum:	2015
Tárgyszavak:	Orvostudományok Klinikai orvostudományok nem besorolt egyéb
További szerzők:	Kerekes-Tóth B. Gyimesi Judit Bartáné Tóth Beáta (1970-) (molekuláris biológus) Kissné Bogáti Réka (1988-) (tudományos segédmunkatárs) Király Róbert (1975-) (biológus) Caja, Sergio Nadalutti, Cristina Lindfors, Katri Mäki, Markku Fésüs László (1947-) (orvos biokémikus)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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