Open AccessAntigen‐specific T cell recognition of affinity‐purified and recombinant thyroid peroxidase in autoimmune thyroid disease
Author(s) -
EWINS D. L.,
BARNETT P. S.,
RATANACHAIYAVONG S.,
SHARROCK C.,
LANCHBURY J.,
McGREGOR A. M.,
BANGA J. P.
Publication year - 1992
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.1992.tb05838.x
Subject(s) - recombinant dna , epitope , thyroid peroxidase , antigen , microbiology and biotechnology , t cell , affinity chromatography , immunology , fusion protein , biology , thyroglobulin , thyroid , autoimmune disease , antibody , extracellular , biochemistry , endocrinology , immune system , enzyme , gene
SUMMARY TheTcell proliferative responses of peripheral blood lymphocytes from 20 patients with autoimmune thyroid disease (AITD) and 20 healthy controls were analysed to immunoaffinity‐purified thyroid peroxidase (TPO) and recombinant antigen preparations generated in Escherichia coli as glutathione‐s‐transferase fusion proteins. The epitope specificity of the T cell response was investigated using a selection of eight discrete recombinant fragments encompassing the whole of the extracellular region of the TPO molecule. Significant differences in the proliferative responses between patients and controls were observed to the full length, affinity‐purified TPO molecule ( P < 0.002) as well as to the recombinant fragments Rlc (residues 145–250)( P <0.001) and R2b(residues 457–589)(P<0.001) suggesting the presence of at least two distinct T cell determinants on this autoantigen. One of these T cell epitopes, localized within the region Rlc, has not previously been identified by studies with synthetic peptides.