| Literature DB >> 26703475 |
Cheuk Wun Li1, Francesca Menconi1, Roman Osman2, Mihaly Mezei2, Eric M Jacobson1, Erlinda Concepcion1, Chella S David3, David B Kastrinsky2, Michael Ohlmeyer2, Yaron Tomer4.
Abstract
We previously showed that an HLA-DR variant containing arginine at position 74 of the DRβ1 chain (DRβ1-Arg74) is the specific HLA class II variant conferring risk for autoimmune thyroid diseases (AITD). We also identified 5 thyroglobulin (Tg) peptides that bound to DRβ1-Arg74. We hypothesized that blocking the binding of these peptides to DRβ1-Arg74 could block the continuous T-cell activation in thyroiditis needed to maintain the autoimmune response to the thyroid. The aim of the current study was to identify small molecules that can block T-cell activation by Tg peptides presented within DRβ1-Arg74 pockets. We screened a large and diverse library of compounds and identified one compound, cepharanthine that was able to block peptide binding to DRβ1-Arg74. We then showed that Tg.2098 is the dominant peptide when inducing experimental autoimmune thyroiditis (EAT) in NOD mice expressing human DRβ1-Arg74. Furthermore, cepharanthine blocked T-cell activation by thyroglobulin peptides, in particular Tg.2098 in mice that were induced with EAT. For the first time we identified a small molecule that can block Tg peptide binding and presentation to T-cells in autoimmune thyroiditis. If confirmed cepharanthine could potentially have a role in treating human AITD.Entities:
Keywords: cell surface protein; endocrinology; major histocompatibility complex (MHC); peptides; small molecule; structural model; thyroglobulin; thyroid; thyroid hormone; thyroiditis
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Year: 2015 PMID: 26703475 PMCID: PMC4759184 DOI: 10.1074/jbc.M115.694687
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157