Identification of common epitopes on gliadin, enterocytes, and calreticulin recognised by antigliadin antibodies of patients with coeliac disease
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
9895374
PubMed Central
PMC1727378
DOI
10.1136/gut.44.2.168
Knihovny.cz E-resources
- MeSH
- Autoantigens immunology MeSH
- Autoimmune Diseases immunology MeSH
- Celiac Disease immunology MeSH
- Chromatography, Affinity MeSH
- Adult MeSH
- Enzyme-Linked Immunosorbent Assay MeSH
- Epitopes analysis MeSH
- Gliadin chemistry immunology MeSH
- Calreticulin MeSH
- Rats MeSH
- Humans MeSH
- Peptide Fragments immunology MeSH
- Rats, Wistar MeSH
- Calcium-Binding Proteins immunology MeSH
- Antibodies blood MeSH
- Ribonucleoproteins immunology MeSH
- Intestines immunology MeSH
- Cross Reactions MeSH
- Animals MeSH
- Check Tag
- Adult MeSH
- Rats MeSH
- Humans MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Autoantigens MeSH
- Epitopes MeSH
- Gliadin MeSH
- Calreticulin MeSH
- Peptide Fragments MeSH
- Calcium-Binding Proteins MeSH
- Antibodies MeSH
- Ribonucleoproteins MeSH
BACKGROUND: Sera of patients with coeliac disease, containing IgA and IgG antigliadin antibodies (AGA) and various IgA autoantibodies, react with isolated enterocytes. AGA cross react with enterocyte antigens, one of which has been identified as calreticulin. AIMS: To characterise the antigenic structures of gliadin, enterocytes, and calreticulin recognised by AGA from patients with active coeliac disease. METHODS: AGA were isolated from sera of nine patients by affinity chromatography and tested by competitive ELISA using 40 alpha-gliadin synthetic dodecapeptides (A1-F6). RESULTS: Reactivity of gliadin with all purified AGA tested was inhibited by peptide A4 at the N-terminal region; by C2, C3, and D4 at the central region; and by F3 and F4 at the C-terminal region of the gliadin molecule. AGA cross reactivity with enterocytes was inhibited by peptides A4, D1-D4, and F6 and with calreticulin by peptides A4, D3, and D4. As dominant epitopes AGA of coeliac patients recognise similar structures corresponding to peptides A4, D3, D4, and F6 present on gliadin, enterocytes, and calreticulin. Substitution of glutamine in the A4 peptide by glutamic acid caused loss of inhibitory capacity. Shortening of peptide A4 on the N-terminal by three amino acids increased its inhibitory effect. CONCLUSIONS: AGA of patients with coeliac disease react with similar structures on gliadin and potential autoantigens on enterocytes.
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