IgG Autoantibodies from Bullous Pemphigoid Patients Recognize Multiple Antigenic Reactive Sites Located Predominantly Within the B and C Subdomains of.

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IgG Autoantibodies from Bullous Pemphigoid Patients Recognize Multiple Antigenic Reactive Sites Located Predominantly Within the B and C Subdomains of the COOH- Terminus of BP230 Mouna Skaria, Fabienne Jaunin, Sara Riou, Jean-Hilaire Saurat, Bertrand Favre, Luca Borradori Journal of Investigative Dermatology Volume 114, Issue 5, Pages 998-1004 (May 2000) DOI: 10.1046/j.1523-1747.2000.00893.x Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 1 Schematic representation of wild-type and mutant forms of BP230. For wild-type BP230, the various subdomains represented in white for the NH2-terminus, in gray for the coiled-coil domain, and in dotted boxes for the COOH-terminus are based on the predicted secondary structure (Green et al. 1992). The clones for recombinants A to E have been tagged at their 5′ end with c-myc, whereas recombinants F and G are fused to the COOH-terminus of the green fluorescent protein (GFP). The amino acid range of the segment of BP230 that is covered by the recombinant is indicated. The protein sequence of BP230 is numbered according toSawamura et al. (1991). Journal of Investigative Dermatology 2000 114, 998-1004DOI: (10.1046/j.1523-1747.2000.00893.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 2 BP sera react with multiple antigenic epitopes throughout BP230. Reactivity of 25 BP sera was assessed by immunoblotting as described in Materials and Methods against BP230 recombinants (listed in Figure 1) that were expressed by an in vitro translation system. Reactivity against recombinants A (A), B (B), C (C), D (D), and E (E). Lanes 1–8 correspond to MoAb 9E10 anti-c-myc-epitope, and sera from BP patients BP3, BP7, BP10, BP13, BP17, and two normal volunteers, respectively. The apparent molecular weights of the recombinants (arrow), each epitope tagged with c-myc at their 5′ end, were slightly smaller than the sizes predicted on the basis of the corresponding sequences, i.e., 63 kDa, 75 kDa, 35 kDa, 79 kDa, and 50 kDa for recombinant A, B, C, D, and E, consistent with the abnormal electrophoretic migration of BP230 and other plakins (Wiche et al. 1993). Each of the 5 BP sera exhibits a different pattern of immunoreactivity and is representative of the reactivity patterns observed with other BP sera. Note that some additional reactive bands were occasionally found with both experimental and control sera and most probably represented either unspecific background or reactivity against proteins in the lysate translation system. Samples were separated by 7.5% SDS-PAGE under nonreducing conditions. Journal of Investigative Dermatology 2000 114, 998-1004DOI: (10.1046/j.1523-1747.2000.00893.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 3 Immunodominant sequences are located within the B domain, the linker, and the C domain of BP230. Reactivity of the 21 BP sera binding to the COOH-terminal domain (recombinant D) were assayed by immunoblotting as described in Materials and Methods against recombinants F and G (Figure 1) that were expressed by transfected COS-7 cells. Reactivity against recombinants F (F) and G (G). Lanes 1–8 correspond to rabbit anti-GFP, and sera from BP patients BP3, BP7, BP12, BP17, BP21, and two normal volunteers, respectively. Proteins close to their predicted mass of 61 kDa and 45 kDa, respectively, are recognized by the rabbit antiserum against GFP. The 5 BP sera are representative of the reactivity patterns observed with other BP sera. Note that some additional reactive bands were occasionally found with both experimental and control sera and most probably represented either unspecific background or reactivity against proteins in COS-7 extracts. Samples were separated by 7.5% SDS-PAGE under nonreducing conditions. Journal of Investigative Dermatology 2000 114, 998-1004DOI: (10.1046/j.1523-1747.2000.00893.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 4 IgG autoantibodies binding to the BP230 tail belong predominantly to the IgG4 and IgG1 subclasses. The subclass distribution of the IgG autoantibody response to recombinant D was assessed by immunoblotting as described in Materials and Methods for 20 BP sera. Reactivity with MoAb 9E10, lane 1; with BP7 serum, lanes 2–6; and with BP18 serum, lanes 5–8. The sera were probed for IgG1 (lanes 2 and 5), for IgG2 (lanes 3 and 7), for IgG3 (lanes 4 and 8), and for IgG4 (lanes 5 and 9). Samples were separated by 7.5% SDS-PAGE under nonreducing conditions. Journal of Investigative Dermatology 2000 114, 998-1004DOI: (10.1046/j.1523-1747.2000.00893.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions