Modeling of main characteristics of bullous pemphigoid antigen-2 (BPAG2) peptide structure in serological recognition by autoantibodies

Pathology & Oncology Research

Péter Németh³  Gabor K. Tóth¹  János Molnár¹  Ilona Marczinovits¹  Ferenc Hudecz²  Gábor Mezó²  József Pál³ 

[1] University of Szeged$$;Hungarian Academy of Sciences, Eötvös Loránd University$$;University of Pécs$$

关键词: cross-reaction;   

DOI  :  10.1007/BF02893410

学科分类：生理学与病理学

来源: Springer

【 摘 要 】

The serum level of autoantibodies against autoantigens of the bullous pemphigoid peptides 1 and 2 (BPAG1 and BPAG2) is a relevant diagnostic marker. Twelve representative sera of BP were tested against the RSILPYGDSMDRIEKDRLQMAP amino acid sequence that is an epitope fragment of the NC16A domain of BPAG2 (AC Q02802; 507�?528) to find the most suitable antigenic form for specific detection of autoantibodies of BP patients�? sera by quantitative ELISA system. The antigenic epitope sequence was presented as an antigen in a carrier free form of dimeric peptide (BP22), dimeric peptide fused to glutathione S-transf erase (GST-BP22) or dimeric peptide chemically conjugated to polyLys(Ser-DL-Ala_m) (SAK-BP22). The intensity of ELISA reaction was highest against the recombinant fusion antigen GST-BP22; the chemically conjugated SAK-BP22 performed less well than the free dimeric form of the peptide. In the case of the GST-BP22 antigen, the (GST-BP22)-(GST)_492nm optical density values were determined. There was no significant difference between the mean ODs of the GST-BP22 and the SAK-BP22 (0.888 vs. 0.892, p= 0.9726). Conjugating the epitope peptide with the synthetic carrier SAK was advantageous, as it abrogated cross-reactivity with GST carrier protein. Consequently, the SAK-BP22 conjugate appears to be the most reliable assay component, avoiding cross-reactivity with GST and simplifying the detection and evaluation of BP autoantibodies in routine ELISA diagnostic system.

【 授权许可】

Unknown