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Antibody responses to deamidated gliadin peptide show high specificity and parallel antibodies to tissue transglutaminase in developing coeliac disease.
Clin Exp Immunol 2007; 150(2):285-93CE

Abstract

Coeliac disease (CD) is an enteropathy induced in genetically susceptible individuals by gluten components, gliadin, hordein and secalin, polypeptides present in cereals such as wheat, barley and rye, respectively. Although the disease starts as intolerance to gliadins, antibodies to tissue transglutaminase (tTG) in the gut epithelium are characteristic of the disease. Whereas serum autoantibodies against tTG (tTGA) are highly specific for CD, antibodies to gliadin are less informative as they can also be detected in other enteropathies, and even in healthy individuals. However, it was shown recently that antibodies to certain gliadin peptides occur with high specificity in CD patient sera. We developed a solid phase lanthanide-based immunofluorometric assay for simultaneous detection of serum IgA and IgG antibodies to a synthetic peptide derived from gamma gliadin of wheat comprising amino acids 86-103. Three glutamine residues of this native 18-mer peptide were replaced by glutamic acids and the peptide was biotinylated. Sera from 87 individuals who had undergone duodenal biopsy and were diagnosed with CD and from 81 healthy individuals were analysed for the presence of both IgA and IgG anti-gliadin peptide antibodies. The performance of the peptide AGA assay was excellent, showing a specificity and sensitivity of 90% and 92% for IgA, and 98% and 75% for IgG, respectively. The corresponding values for conventional anti-gliadin antibody (AGA) enzyme-linked immunosorbent assay (ELISA) tests were 72% specificity and 87% sensitivity for IgA, and 64% specificity and 78% sensitivity for IgG. In a prospective study, almost all the tTGA-positive sera drawn from children who later developed CD were also positive for gliadin peptide antibodies.

Authors+Show Affiliations

Department of Biochemistry and Pharmacy, Abo Akademi University, Turku, Finland.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Evaluation Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17803713

Citation

Ankelo, M, et al. "Antibody Responses to Deamidated Gliadin Peptide Show High Specificity and Parallel Antibodies to Tissue Transglutaminase in Developing Coeliac Disease." Clinical and Experimental Immunology, vol. 150, no. 2, 2007, pp. 285-93.
Ankelo M, Kleimola V, Simell S, et al. Antibody responses to deamidated gliadin peptide show high specificity and parallel antibodies to tissue transglutaminase in developing coeliac disease. Clin Exp Immunol. 2007;150(2):285-93.
Ankelo, M., Kleimola, V., Simell, S., Simell, O., Knip, M., Jokisalo, E., ... Hinkkanen, A. E. (2007). Antibody responses to deamidated gliadin peptide show high specificity and parallel antibodies to tissue transglutaminase in developing coeliac disease. Clinical and Experimental Immunology, 150(2), pp. 285-93.
Ankelo M, et al. Antibody Responses to Deamidated Gliadin Peptide Show High Specificity and Parallel Antibodies to Tissue Transglutaminase in Developing Coeliac Disease. Clin Exp Immunol. 2007;150(2):285-93. PubMed PMID: 17803713.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Antibody responses to deamidated gliadin peptide show high specificity and parallel antibodies to tissue transglutaminase in developing coeliac disease. AU - Ankelo,M, AU - Kleimola,V, AU - Simell,S, AU - Simell,O, AU - Knip,M, AU - Jokisalo,E, AU - Tarkia,M, AU - Westerlund,A, AU - He,Q, AU - Viander,M, AU - Ilonen,J, AU - Hinkkanen,A E, Y1 - 2007/09/04/ PY - 2007/9/7/pubmed PY - 2007/12/19/medline PY - 2007/9/7/entrez SP - 285 EP - 93 JF - Clinical and experimental immunology JO - Clin. Exp. Immunol. VL - 150 IS - 2 N2 - Coeliac disease (CD) is an enteropathy induced in genetically susceptible individuals by gluten components, gliadin, hordein and secalin, polypeptides present in cereals such as wheat, barley and rye, respectively. Although the disease starts as intolerance to gliadins, antibodies to tissue transglutaminase (tTG) in the gut epithelium are characteristic of the disease. Whereas serum autoantibodies against tTG (tTGA) are highly specific for CD, antibodies to gliadin are less informative as they can also be detected in other enteropathies, and even in healthy individuals. However, it was shown recently that antibodies to certain gliadin peptides occur with high specificity in CD patient sera. We developed a solid phase lanthanide-based immunofluorometric assay for simultaneous detection of serum IgA and IgG antibodies to a synthetic peptide derived from gamma gliadin of wheat comprising amino acids 86-103. Three glutamine residues of this native 18-mer peptide were replaced by glutamic acids and the peptide was biotinylated. Sera from 87 individuals who had undergone duodenal biopsy and were diagnosed with CD and from 81 healthy individuals were analysed for the presence of both IgA and IgG anti-gliadin peptide antibodies. The performance of the peptide AGA assay was excellent, showing a specificity and sensitivity of 90% and 92% for IgA, and 98% and 75% for IgG, respectively. The corresponding values for conventional anti-gliadin antibody (AGA) enzyme-linked immunosorbent assay (ELISA) tests were 72% specificity and 87% sensitivity for IgA, and 64% specificity and 78% sensitivity for IgG. In a prospective study, almost all the tTGA-positive sera drawn from children who later developed CD were also positive for gliadin peptide antibodies. SN - 1365-2249 UR - https://www.unboundmedicine.com/medline/citation/17803713/Antibody_responses_to_deamidated_gliadin_peptide_show_high_specificity_and_parallel_antibodies_to_tissue_transglutaminase_in_developing_coeliac_disease_ L2 - https://doi.org/10.1111/j.1365-2249.2007.03487.x DB - PRIME DP - Unbound Medicine ER -