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Similarity of fine specificity of IgA anti-gliadin antibodies between patients with celiac disease and humanized α1KI mice
D. Sánchez, G. Champier, A. Cuvillier, M. Cogné, A. Pekáriková, H. Tlaskalová-Hogenová, I. Hoffmanová, P. Drastich, T. Mothes, L. Tučková,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
Grant support
NS9705
MZ0
CEP Register
PubMed
21366336
DOI
10.1021/jf1044519
Knihovny.cz E-resources
- MeSH
- Celiac Disease immunology MeSH
- Adult MeSH
- Epitopes chemistry immunology MeSH
- Gliadin immunology MeSH
- Immunoglobulin A immunology MeSH
- Humans MeSH
- Adolescent MeSH
- Molecular Sequence Data MeSH
- Antibodies, Monoclonal biosynthesis immunology MeSH
- Mice, Transgenic immunology MeSH
- Mice MeSH
- Amino Acid Sequence MeSH
- Antibody Specificity MeSH
- Animals MeSH
- Check Tag
- Adult MeSH
- Humans MeSH
- Adolescent MeSH
- Male MeSH
- Mice MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
References provided by Crossref.org
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