Studies on thyroid cross-reactivity have focused primarily on pathogens and dietary proteins. We also determined that elevated levels of bisphenol-A bound to HSA significantly increases the risk for Parkinson’s disease and correlates with alpha-synuclein antibodies. Further research identified that these chemicals conjugated to HSA are associated with antibodies to neurological tissue involved in multiple sclerosis. In a study we published of 400 subjects, between 8–22% of individuals exhibited elevated levels of commonly exposed chemicals bound to human serum albumin. Ĭonjugation of chemicals bound to human serum albumin (HSA) is found with blood samples of healthy human blood donors. This leads to neoantigen formation, resulting in systemic T-cell or antibody immune responses against the haptens and self-proteins. Chemical molecules can bind directly or indirectly to circulating proteins after hepatic or extrahepatic conversion from prohapten to haptens, generating hapten–protein adducts. The alteration of protein topography leads to the binding of the antibody to the protein in the target sites. In addition, the binding of chemicals to self-proteins such as albumin, globulin, or hemoglobin leads to protein misfolding and induces a conformational change in the macromolecule. Reactivity of antibodies with chemicals bound to proteins has the potential to play a cross-reactive role in autoimmune thyroid disease and thyroid metabolism disruption. Cross-reactive interactions with various target sites of the thyroid axis may also lead to thyroid metabolism disruption. Furthermore, many antibody binding sites are polyfunctional and can accommodate more than one antigenic epitope and play a role in autoimmune disease. Cross-reactive antibodies from various infections have been found to play a role in autoimmune thyroid disease and thyroid metabolism dysfunction by binding to multiple target sites of the thyroid axis via cross-reactivity. These molecular interactions with the antigen–antibody binding sites can occur from a diverse list of antigen-promoted antibodies. Cross-reactivity of various antigens with self-tissue proteins can induce tissue-specific autoimmune diseases in susceptible subjects. The interactions of multiple antigenic antibodies with the same binding site are known as cross-reactivity. Immunological cross-reactivity is expressed when antibodies with similar amino acid homology or similar antibody surface topology bind to the same binding site. This laboratory analysis of immune reactivity between thyroid target sites and chemicals bound to HSA antibodies identifies a new mechanism by which chemicals can disrupt thyroid function. A significant decline in these reactions was observed. For demonstration of specificity of thyroid antibody binding to various haptenic chemicals bound to HSA, both serial dilution and inhibition studies were performed and proportioned to the dilution. Our study identified a new mechanism through which chemicals bound to circulating serum proteins lead to structural protein misfolding that creates neoantigens, resulting in the development of antibodies that bind to key target proteins of the thyroid axis through protein misfolding. We found that specific monoclonal or polyclonal antibodies developed against thyroid-stimulating hormone (TSH) receptor, 5′-deiodinase, thyroid peroxidase, thyroglobulin, thyroxine-binding globulin (TBG), thyroxine (T4), and triiodothyronine (T3) bound to various chemical HSA compounds. We investigated how antibodies made against thyroid target sites may bind to various chemical–albumin compounds where binding of the chemical has induced human serum albumin (HSA) misfolding. Alteration of peptides that share topological equivalence with alternating side chains can lead to the formation of binding surfaces that may mimic the antigenic structure of a variant peptide or protein. ![]() Cross-reactivity then can occur if epitopes of the protein share surface topology to similar binding sites. In some instances, when chemicals bind to proteins, they have the potential to induce a conformational change in the macromolecule that may misfold in such a way that makes it similar to the various target sites or act as a neoantigen without conformational change.
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