TITLE

Mutagenesis of the catalytic triad of tissue transglutaminase abrogates coeliac disease serum IgA autoantibody binding

AUTHOR(S)
Byrne, Greg; Ryan, Fergus; Jackson, John; Feighery, Con; Kelly, Jacinta
PUB. DATE
March 2007
SOURCE
Gut;Mar2007, Vol. 56 Issue 3, p336
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Background and aims: Tissue transglutaminase (†TG) is an autoantigen in coeliac disease and the related disorder, dermatitis herpetiformis. The detection of autoantibodies directed against †TG is a highly specific marker of coeliac disease; however, it is unclear if there is a role for these autoantibodies in the disease process. The aim of this study was to investigate whether the catalytic triad of †TG is targeted by coeliac disease autoantibodies. Methods: A full-length wild-type recombinant †TG and a novel site-directed mutagenic variant lacking the catalytic triad were produced in Escherichia coli. Serum samples from 61 biopsy-proven coeliac disease and 10 dermatitis herpetiformis patients were tested for their recognition of both antigens in enzyme-linked immunosorbent assay. Results: Although IgA autoantibodies from sera of patients with coeliac disease and dermatitis herpetiformis bound wild-type †TG well, a dramatic decrease in binding to the mutant †TG was observed with a mean reduction of 79% in coeliac disease and 58% in dermatitis herpetiformis samples. IgG anti-†TG antibodies did not show a similar pattern of reduction, with no overall difference in recognition of the wild-type or mutant †TGs. Conclusions: These results suggest that the IgA anti-†TG response in coeliac disease and dermatitis herpetiformis is focused on the region of †TG responsible for its transamidation and deamidation reactions, whereas the IgG response may target other regions of the enzyme.
ACCESSION #
24528557

 

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