scholarly journals An electrochemical deamidated gliadin antibody immunosensor for celiac disease clinical diagnosis

The Analyst ◽  
2013 ◽  
Vol 138 (7) ◽  
pp. 1956 ◽  
Author(s):  
Marta M. P. S. Neves ◽  
María Begoña González-García ◽  
Henri P. A. Nouws ◽  
Agustín Costa-García
Keyword(s):  
Celiac Disease ◽  
Clinical Diagnosis ◽  
Gliadin Antibody

scholarly journals Celiac Disease

2001 ◽  
Vol 47 (11) ◽  
pp. 2023-2028 ◽  
Author(s):  
Mabel Aleanzi ◽  
Ana María Demonte ◽  
Cecilia Esper ◽  
Silvia Garcilazo ◽  
Marta Waggener
Keyword(s):  
Celiac Disease ◽  
Tissue Transglutaminase ◽  
Gluten Free ◽  
Antibody Recognition ◽  
Modified Peptides ◽  
Gliadin Peptides ◽  
Circulating Antibodies ◽  
Native Peptides ◽  
Gliadin Antibody ◽  
Circulating Antibody

Abstract 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 α-type gliadin; and peptide-2, with residues 134–153 of γ-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.

Mucosal and systemic IgA anti-gliadin antibody in celiac disease

1991 ◽  
Vol 36 (6) ◽  
pp. 743-751 ◽  
Author(s):  
Ciaran P. Kelly ◽  
Conleth F. Feighery ◽  
Richard B. Gallagher ◽  
Michael J. Gibney ◽  
Donald G. Weir
Keyword(s):  
Celiac Disease ◽  
Gliadin Antibody

scholarly journals Diagnostic value of various serum antibodies detected by diverse methods in childhood celiac disease

1996 ◽  
Vol 42 (11) ◽  
pp. 1838-1842 ◽  
Author(s):  
L Sacchetti ◽  
A Ferrajolo ◽  
G Salerno ◽  
P Esposito ◽  
M M Lofrano ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Celiac Disease ◽  
Umbilical Cord ◽  
Diagnostic Value ◽  
Diagnostic Sensitivity ◽  
Antibody Detection ◽  
Human Umbilical Cord ◽  
Iga Antibody ◽  
Monkey Esophagus ◽  
Gliadin Antibody

Abstract The diagnostic performances of antiendomysium IgA detected on monkey esophagus and human umbilical cord smooth muscle, of antireticulin IgA, and of antigliadin IgA and IgG were calculated in 74 children with celiac disease (CD) or other gastrointestinal disorders. We also compared four methods for gliadin antibody detection. With a diagnostic specificity of 100%, diagnostic sensitivity was 94% for antireticulin IgA, 93% for antiendomysium IgA when detected on human umbilical cord smooth muscle, and 97% when detected on monkey esophagus. The diagnostic sensitivity for gliadin antibody was highest with an ELISA procedure, followed by fluorogenic detection (94% for IgG, 91% for IgA, 97% with IgA and IgG combined). Because of its high diagnostic sensitivity and ease and speed of use, the combined antigliadin IgG and IgA antibody assay is suitable for screening large groups of patients. In IgG- or IgA-positive cases, the more demanding and more specific antiendomysium IgA evaluation is required to confirm suspected CD.

scholarly journals Serology of celiac disease in gluten-sensitive ataxia or neuropathy: Role of deamidated gliadin antibody

2011 ◽  
Vol 230 (1-2) ◽  
pp. 130-134 ◽  
Author(s):  
Shahrooz Rashtak ◽  
Shadi Rashtak ◽  
Melissa R. Snyder ◽  
Sean J. Pittock ◽  
Tsung-Teh Wu ◽  
...  
Keyword(s):  
Celiac Disease ◽  
Gliadin Antibody

AGY, a Novel Egg Yolk-Derived Anti-gliadin Antibody, Is Safe for Patients with Celiac Disease

2016 ◽  
Vol 62 (5) ◽  
pp. 1277-1285 ◽  
Author(s):  
Dory A. Sample ◽  
Hoon H. Sunwoo ◽  
Hien Q. Huynh ◽  
Heather L. Rylance ◽  
Cheri L. Robert ◽  
...  
Keyword(s):  
Celiac Disease ◽  
Egg Yolk ◽  
Gliadin Antibody

scholarly journals X6: A Novel Antibody for Potential Use in Gluten Quantification

Molecules ◽  
2020 ◽  
Vol 25 (14) ◽  
pp. 3107
Author(s):  
Aleksandrina Shatalova ◽  
Ivan Shatalov ◽  
Yuri Lebedin
Keyword(s):  
Celiac Disease ◽  
Specific Binding ◽  
Qualitative Assessment ◽  
Disease Manifestation ◽  
Antibody Recognition ◽  
Gliadin Peptides ◽  
Specificity Study ◽  
Highly Correlated ◽  
Gliadin Antibody ◽  
Potential Use

Gliadin is a fraction of gluten, known to trigger celiac disease in susceptible people. To date, the life-long gluten-free diet is used for the prevention of this disease. Hence, methods for gluten control in foods are of significant importance. Being one of the most-used methods used for this purpose, ELISA should use high-affinity antibodies to gliadin peptides involved into celiac process. This study investigates the characteristics of a novel anti-gliadin antibody X6. We found the QXQPFPXP site to be a recognized epitope that provides specific binding of the antibody to cereal prolamins involved in celiac disease manifestation. A specificity study using immunoblotting shows the recognition of wheat, barley and rye proteins—as well as α-gliadin homologs from non-edible cereals (Dasypyrum villosum). Reactivity to avenin was less pronounced, as this protein does not contain the PFP motif most critical for antibody recognition. The proteins of Zea mays and Setaria italica were not recognized by X6. X6-based ELISA highly correlated with R5 and G12, which are Codex Alimentarius standards in the quantitative assessment of gluten content (Pearson’s R = 0.86 and 0.87, respectively). Qualitative assessment revealed no significant differences between R5 and G12 and X6.

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