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1
Cátedra de Bioquímica Básica de Macromoléculas, INTEBIO, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Pje. el Pozo. CC 242, 3000 Santa Fe, Argentina.
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Hospital de Niños Dr Orlando Alassia de Santa Fe, G. de Lamadrid, 3000 Santa Fe, Argentina.
aAuthor for correspondence. Fax 54-342-457522; e-mail maleanzi{at}fbcb.unl.edu.ar.
Background: Selective deamidation of glutamine residues by tissue transglutaminase (tTG) turns gliadin peptides into stronger activators of T cells from celiac disease (CD) patients. We examined the possibility that these modified peptides could be more specific epitopes for circulating antibodies than are native peptides.
Methods: Two native synthetic peptides and their respective modified sequences were used as antigens for ELISA assays: peptide-1, with residues 56–75 of 
-type gliadin; and peptide-2, with residues 134–153 of 
-type gliadin. We examined 40 CD patients [31 not being treated with a gluten-free diet (GFD) and 9 being treated with a GFD] and 30 non-CD patients.
Results: An enhanced response against deamidated peptides was observed in 4 (IgA) and 22 (IgG) of 31 untreated CD patients for peptide-1 and in 25 (IgA) and 29 (IgG) patients for peptide-2. Higher anti-gliadin antibody and anti-tTG IgA concentrations correlated with increased IgA reactivity to modified peptides. Among the nine treated CD patients, eight also displayed an improved IgG signal for the deamidated sequence. Deamidation of peptides did not increase the reactivity of non-CD sera.
Conclusions: Selective deamidation specifically increases circulating antibody recognition of gliadin peptides in CD patients. This suggests that deamidated gliadin peptides are more specific CD B-cell epitopes than native peptides; this finding may be relevant for designing improved diagnostic tests.
The following articles in journals at HighWire Press have cited this article:
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  T. Matysiak-Budnik, I. C. Moura, M. Arcos-Fajardo, C. Lebreton, S. Menard, C. Candalh, K. Ben-Khalifa, C. Dugave, H. Tamouza, G. van Niel, et al. Secretory IgA mediates retrotranscytosis of intact gliadin peptides via the transferrin receptor in celiac disease J. Exp. Med., January 21, 2008; 205(1): 143 - 154. [Abstract] [Full Text] [PDF]
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 S. Niveloni, E. Sugai, A. Cabanne, H. Vazquez, J. Argonz, E. Smecuol, M. L. Moreno, F. Nachman, R. Mazure, Z. Kogan, et al. Antibodies against Synthetic Deamidated Gliadin Peptides as Predictors of Celiac Disease: Prospective Assessment in an Adult Population with a High Pretest Probability of Disease Clin. Chem., December 1, 2007; 53(12): 2186 - 2192. [Abstract] [Full Text] [PDF]
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 W Dieterich, B Esslinger, D Trapp, E Hahn, T Huff, W Seilmeier, H Wieser, and D Schuppan Cross linking to tissue transglutaminase and collagen favours gliadin toxicity in coeliac disease Gut, April 1, 2006; 55(4): 478 - 484. [Abstract] [Full Text] [PDF]
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 H. E. Prince Evaluation of the INOVA Diagnostics Enzyme-Linked Immunosorbent Assay Kits for Measuring Serum Immunoglobulin G (IgG) and IgA to Deamidated Gliadin Peptides Clin. Vaccine Immunol., January 1, 2006; 13(1): 150 - 151. [Abstract] [Full Text] [PDF]
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E. Schwertz, F. Kahlenberg, U. Sack, T. Richter, M. Stern, K. Conrad, K.-P. Zimmer, and T. Mothes Serologic Assay Based on Gliadin-Related Nonapeptides as a Highly Sensitive and Specific Diagnostic Aid in Celiac Disease Clin. Chem., December 1, 2004; 50(12): 2370 - 2375. [Abstract] [Full Text] [PDF]
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E A L Bateman, B L Ferry, A Hall, S A Misbah, R Anderson, and P Kelleher IgA antibodies of coeliac disease patients recognise a dominant T cell epitope of A-gliadin Gut, September 1, 2004; 53(9): 1274 - 1278. [Abstract] [Full Text] [PDF]
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