Abstract:
:Human thyroperoxidase (TPO) ectodomain is successively made of myeloperoxidase-, complement control protein repeat-, and epidermal growth factor-like gene modules. However, the TPO immunodominant region targeted by autoantibodies from patients with an autoimmune thyroid disease has not been mapped on the molecule. Here, we used two purified recombinant TPO peptides produced in eukaryotic cells, which correspond to the major first and the further two gene modules of TPO. We compared by ELISA their respective immunoreactivity with that of the recombinant soluble TPO containing all the three gene modules. We used well-characterized murine and human TPO monoclonal antibodies and human autoantibodies affinity-purified from a large pool of patients' sera. We found that the TPO immunodominant region was susceptible to denaturation and required the integrity of the molecule to be correctly expressed. We concluded that TPO B-cell autoepitopes are made by amino acids from the three gene modules, which fold in one highly conformational immunodominant region.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Blanchin S,Estienne V,Guo J,Rapoport B,McLachlan SM,Carayon P,Ruf Jdoi
10.1016/s0006-291x(02)00827-6subject
Has Abstractpub_date
2002-08-02 00:00:00pages
1118-24issue
5eissn
0006-291Xissn
1090-2104pii
S0006291X02008276journal_volume
295pub_type
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