Lack of Cross–Reactivity between Casein and Gliadin in Sera from Coeliac Disease Patients

1998 ◽  
Vol 117 (2) ◽  
pp. 152-154
Author(s):  
Svetlana Paranos ◽  
Goran Nikolic
Keyword(s):  
Coeliac Disease ◽  
Cross Reactivity

scholarly journals Identification of common epitopes on gliadin, enterocytes, and calreticulin recognised by antigliadin antibodies of patients with coeliac disease

Gut ◽  
1999 ◽  
Vol 44 (2) ◽  
pp. 168-173 ◽  
Author(s):  
S Krupičková ◽  
L Tučková ◽  
Z Flegelová ◽  
M Michalak ◽  
J R F Walters ◽  
...  
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Affinity Chromatography ◽  
Coeliac Disease ◽  
Central Region ◽  
Inhibitory Effect ◽  
Cross Reactivity ◽  
Competitive Elisa ◽  
Terminal Region ◽  
Antigliadin Antibodies

BackgroundSera 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.AimsTo characterise the antigenic structures of gliadin, enterocytes, and calreticulin recognised by AGA from patients with active coeliac disease.MethodsAGA were isolated from sera of nine patients by affinity chromatography and tested by competitive ELISA using 40 α-gliadin synthetic dodecapeptides (A1–F6).ResultsReactivity 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.ConclusionsAGA of patients with coeliac disease react with similar structures on gliadin and potential autoantigens on enterocytes.

Relation of antigenic structure of cereal proteins to their toxicity in coeliac patients

1985 ◽  
Vol 53 (1) ◽  
pp. 39-45 ◽  
Author(s):  
P. J. Ciclitira ◽  
H. J. Ellis ◽  
D. J. Evans ◽  
E. S. Lennox
Keyword(s):  
Coeliac Disease ◽  
Competitive Inhibition ◽  
Double Diffusion ◽  
Cross Reactivity ◽  
Antigenic Structure ◽  
Partial Identity ◽  
Cereal Proteins

1. Unfractionated gliadin and its α-, β-, γ- and ω-gliadin subfractions were used as rabbit immunogens. The antisera were characterized by (1) Ouchterlony double diffusion, (2) binding of 125I-labelled gliadin subfractions, (3) inhibition by several gliadin subfractions of binding between γgliadin antiserum and 125I-labeIled γgliadin.2. Double diffusion showed identical cross-reactivity between the antisera and the gliadin subfractions with the exception of ω-gliadin. Precipitin lines of partial identity with gliadin were observed against rye secalins and barley hordeins but not oat avenins or maize zeins.3. Binding was observed between unfractionated 125I-labelledα-, β-, γ- and ω-gliadins and all the antisera. There was binding of 125I-labelled ω-gliadin to the ω-gliadin antiserum but poor binding of 125I-labelled ω-gliadin to unfractionated α-, β- and γ-gliadin antisera. Competitive inhibition of binding between 125I-labelled γ-gliadin and γ-gliadin antiserum diluted 1:250 (v/v) demonstrated similar competition between α-, β- and γ-gliadins and this antiserum but poor competition between ω-gliadin, wheat glutenins, albumins and globulins, rye secalins, barley hordeins and oat avenins.4. These findings suggest that there is a good correlation between the antigenic structure of gliadin proteins and their toxicity to patients with coeliac disease.

A Radioimmunoassay for α-and β-Gliadins

1983 ◽  
Vol 64 (6) ◽  
pp. 655-659 ◽  
Author(s):  
P. J. Ciclitira ◽  
E. S. Lennox
Keyword(s):  
Staphylococcus Aureus ◽  
Coeliac Disease ◽  
Wheat Flour ◽  
Cross Reactivity ◽  
Competitive Binding ◽  
Gluten Free ◽  
Wheat Proteins ◽  
Specific Radioimmunoassay ◽  
Special Value ◽  
Antigen Antibody

1. A rapid, sensitive specific radioimmunoassay for α- and β-gliadin has been developed using an antiserum raised in rabbits to A-gliadin, a component of α-gliadin. 2. The antigen used in the assay was α-gliadin labelled with 125I; antigen-antibody complexes were collected after adsorption to Staphylococcus aureus in suspension. 3. The sensitivity of the assay, as judged by competitive binding with unlabelled antigen, was 1 ng of α- or β-gliadin, which show complete cross-reaction with this antiserum. 4. Cross-reactivity to other wheat proteins was < 1% and no cross-reactivity to extracts of rye, barley or oats was observed. 5. This radioimmunoassay for α- and β-gliadin has been used to measure their amount in different varieties of wheat flour, several foods prepared from flour, e.g. bread, biscuits and products prepared as ‘gluten free’. The possibility of assaying for α-gliadin in prepared foods is of special value since α-, β-, γ- and ω-gliadin have been shown to exacerbate coeliac disease.

Characterisation of clinical and immune reactivity to barley and rye ingestion in children with coeliac disease

Gut ◽  
2019 ◽  
Vol 69 (5) ◽  
pp. 830-840 ◽  
Author(s):  
Melinda Y Hardy ◽  
Amy K Russell ◽  
Catherine Pizzey ◽  
Claerwen M Jones ◽  
Katherine A Watson ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Coeliac Disease ◽  
Single Cells ◽  
T Cell Responses ◽  
Cross Reactivity ◽  
T Cell Response ◽  
Immune Reactivity ◽  
Clinical Effects ◽  
Cell Responses

ObjectiveBarley and rye are major components of the Western diet, and historic feeding studies indicate that they cause clinical effects in patients with coeliac disease (CD). This toxicity has been attributed to sequence homology with immunogenic wheat sequences, but in adults with CD, these cereals stimulate unique T cells, indicating a critical contribution to gluten immunity independent of wheat. Clinical and immune feeding studies with these grains in children with CD are sparse. We undertook a barley and rye feeding study to characterise the clinical and T-cell responses in children with CD.Design42 children with human leucocyte antigen (HLA)-DQ2.5+ (aged 3–17 years) consumed barley or rye for 3 days. Blood-derived gluten-specific T cells were tested for reactivity against a panel of barley (hordein) and rye (secalin) peptides. Hordein and secalin-specific T-cell clones were generated and tested for grain cross-reactivity. T-cell receptor sequencing was performed on sorted single cells. T-cell responses were compared with those observed in adults with CD.Results90% of the children experienced adverse symptoms, mostly GI, and 61% had detectable gluten-specific T-cell responses targeting peptides homologous to those immunogenic in adults. Deamidation was important for peptide reactivity. Homozygosity for HLA-DQ2.5 predicted a stronger T-cell response. Gluten-specific T cells showed striking similarities in their cross-reactivity between children and adults.ConclusionsBarley and rye induce a consistent range of clinical and T-cell responses in children with CD. The findings highlight the importance of a series of dominant hordein and secalin peptides pathogenic in children with CD, some independent of wheat, which closely correspond to those seen in adults.

Improving the diagnosis of coeliac disease in anaemic women

2000 ◽  
Vol 111 (3) ◽  
pp. 898-901 ◽  
Author(s):  
D. J. Unsworth ◽  
R. J. Lock ◽  
R. F. Harvey
Keyword(s):  
Coeliac Disease

HLA-DQ2 and/or-DQ9 is associated with coeliac disease specific autoantibodies to tissue transglutaminase in families with thyrold autoimmunity

2001 ◽  
Vol 120 (5) ◽  
pp. A393-A393
Author(s):  
D SCHUPPAN ◽  
W DIETERICH ◽  
S HOFMANN ◽  
M HUEFNER ◽  
K USADEL ◽  
...  
Keyword(s):  
Coeliac Disease ◽  
Tissue Transglutaminase ◽  
Disease Specific ◽  
Hla Dq2

Refractory coeliac disease type I and II; Pilot-treatment with azathioprine and predinison

2001 ◽  
Vol 120 (5) ◽  
pp. A131-A131 ◽  
Author(s):  
C MULDER ◽  
P WAHAB ◽  
A TAN ◽  
J MEIJER
Keyword(s):  
Coeliac Disease ◽  
Disease Type ◽  
Type I ◽  
Refractory Coeliac Disease
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