Similarity of fine specificity of IgA anti-gliadin antibodies between patients with celiac disease and humanized α1KI mice
| Autor: | Aneta Pekáriková, Thomas Mothes, Pavel Drastich, Ludmila Tučková, Iva Hoffmanová, Armelle Cuvillier, Michel Cogné, Gaël Champier, Daniel Sánchez, Helena Tlaskalova-Hogenova |
|---|---|
| Přispěvatelé: | Physiologie Moléculaire de la Réponse Immune et des Lymphoproliférations (PMRIL), Université de Limoges (UNILIM)-Génomique, Environnement, Immunité, Santé, Thérapeutique (GEIST FR CNRS 3503)-Centre National de la Recherche Scientifique (CNRS), Université de Limoges (UNILIM) |
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Male
Immunoglobulin A MESH: Amino Acid Sequence Gliadin Epitope MESH: Antibodies Monoclonal Epitopes Mice 0302 clinical medicine Antibody Specificity MESH: Animals reproductive and urinary physiology 0303 health sciences biology Antibodies Monoclonal MESH: Gliadin 3. Good health Anti-gliadin antibodies [SDV.IMM]Life Sciences [q-bio]/Immunology Female 030211 gastroenterology & hepatology Antibody General Agricultural and Biological Sciences Adult MESH: Epitopes Adolescent MESH: Mice Transgenic Molecular Sequence Data education Mice Transgenic 03 medical and health sciences Immune system Animals Humans Amino Acid Sequence MESH: Immunoglobulin A MESH: Antibody Specificity MESH: Mice 030304 developmental biology MESH: Adolescent MESH: Humans MESH: Molecular Sequence Data MESH: Adult General Chemistry MESH: Male body regions Celiac Disease Pepscan Humanized mouse Immunology biology.protein MESH: Female MESH: Celiac Disease |
| Zdroj: | Journal of Agricultural and Food Chemistry Journal of Agricultural and Food Chemistry, American Chemical Society, 2011, 59 (7), pp.3092-100. ⟨10.1021/jf1044519⟩ |
| ISSN: | 0021-8561 1520-5118 |
| DOI: | 10.1021/jf1044519⟩ |
| Popis: | International audience; Gliadins, and primarily α-gliadins containing several sequences such as aa 31-49, aa 56-88 (33-mer), aa 57-68, and aa 69-82, are critical in the induction of immune response or toxic reaction leading to the development of celiac disease (CLD). The role of IgA anti-gliadin antibodies (IgA AGA) is unknown. To this end, we prepared several humanized monoclonal IgA AGA using transgenic α1KI mice. Employing Pepscan with overlapping decapeptides of α-gliadin we observed a robust similarity between the specificity of humanized mouse monoclonal IgA AGA and IgA AGA from patients with florid CLD. The common immunodominant region included several sequential epitopes localized in the N-terminal part of α-gliadin (QFQGQQQPFPPQQPYPQPQPFP, aa 29-50, and QPFPSQQPYLQL, aa 47-58). Notably, IgA AGA produced by clones 8D12, 15B9, 9D12, and 18E2 had significant reactivity against sequences localized in the 33-mer, LQLQPFPQPQ (aa 56-65) and PQLPYPQPQPFL (aa 69-80). Humanized mouse monoclonal IgA AGA that have a known specificity are suitable as standard in ELISAs to detect serum IgA AGA of CLD patients and for studying the AGA pathogenic role in CLD, especially for analyzing the translocation of complex of specific IgA antibodies and individual gliadin peptides through enterocyte barrier. |
| Databáze: | OpenAIRE |
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