The reaction of antibodies with the native and deglycosylated thyrotropin receptor obtained from transfected insect cells.

The role of glycan moieties in thyrotropin receptor molecule in binding of antibodies is a subject of intense debate. To approach the function of sugars in recognition by antibody of the extracellular part of the receptor (ETSHR) we studied the reaction of the HPLC purified ETSHR from insect cells in the reaction with autoantibodies and antibodies of animal origin. None of the autoantibodies from Graves' patients sera bound to ETSHR. In contrast, each of the animal antibodies: three monoclonal, five polyclonal antireceptor and two polyclonal anti peptide corresponding to the amino acid sequence present in the receptor, became bound to the native receptor from insect cells as well as to its deglycosylated form. The shape of the dilution curves of particular antibodies in the reaction with either form of the receptor was almost the same. The coefficients of correlation was about 0.9. It seems that the correct receptor glycosylation is not crucial for binding of animal origin antibodies.