Preferential Reactivity of Dipeptidyl Peptidase-IV Inhibitor-Associated Bullous Pemphigoid Autoantibodies to the Processed Extracellular Domains of BP180

Front Immunol. 2019 May 29:10:1224. doi: 10.3389/fimmu.2019.01224. eCollection 2019.

Abstract

Bullous pemphigoid (BP) is a common autoimmune blistering disease in which autoantibodies target the hemidesmosomal components BP180 and/or BP230 in basal keratinocytes. In BP, 80 to 90% of autoantibodies target the juxtamembranous extracellular non-collagenous 16th A (NC16A) domain of BP180. Recently, the administration of dipeptidyl peptidase-IV inhibitors (DPP4i), which are widely used as antihyperglycemic drugs, has been recognized to be a causative factor for BP. DPP4i-associated BP (DPP4i-BP) autoantibodies tend to target epitopes on non-NC16A regions of BP180, and the pathomechanism for the development of the unique autoantibodies remains unknown. To address the characteristics of DPP4i-BP autoantibodies in detail, we performed epitope analysis of 18 DPP4i-BP autoantibodies targeting the non-NC16A domains of BP180 using various domain-specific as well as plasmin-digested polypeptides derived from recombinant BP180. Firstly, Western blotting showed that only one DPP4i-BP serum reacted with the epitopes on the intracellular domain of BP180, and no sera reacted with the C-terminal domain of the molecule. In addition, only 2 DPP4i-BP sera reacted with BP230 as determined by enzyme-linked immunosorbent assay. Thus, DPP4i-BP autoantibodies were found to mainly target the non-NC16A mid-portion of the extracellular domain of BP. Interestingly, Western blotting using plasmin-digested BP180 as a substrate revealed that all of the DPP4i-BP sera reacted more intensively with the 97-kDa processed extracellular domain of BP180, which is known as the LABD97 autoantigen, than full-length BP180 did. All of the DPP4i-BP autoantibodies targeting the LABD97 autoantigen were IgG1, and IgG4 was observed to react with the molecule in only 7 cases (38.9%). In summary, the present study suggests that IgG1-class autoantibodies targeting epitopes on the processed extracellular domain of BP180, i.e., LABD97, are the major autoantibodies in DPP4i-BP.

Keywords: BP180; BP230; IgG subclass; autoantibodies; autoimmune disease; bullous pemphigoid; dipeptidyl peptidase-IV inhibitor; dipeptidyl peptidase-IV inhibitor-associated bullous pemphigoid.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Aged, 80 and over
  • Antibody Specificity
  • Autoantibodies / immunology*
  • Autoantigens / chemistry
  • Autoantigens / drug effects
  • Autoantigens / immunology*
  • Blotting, Western
  • Collagen Type XVII
  • Dipeptidyl Peptidase 4 / immunology
  • Dipeptidyl-Peptidase IV Inhibitors / adverse effects*
  • Dipeptidyl-Peptidase IV Inhibitors / immunology
  • Dystonin / chemistry
  • Dystonin / immunology
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes / chemistry
  • Epitopes / immunology*
  • Female
  • Fibrinolysin / pharmacology
  • Humans
  • Immunoglobulin G / immunology
  • Male
  • Middle Aged
  • Non-Fibrillar Collagens / chemistry
  • Non-Fibrillar Collagens / drug effects
  • Non-Fibrillar Collagens / immunology*
  • Pemphigoid, Bullous / chemically induced*
  • Pemphigoid, Bullous / immunology
  • Peptide Fragments / chemistry
  • Peptide Fragments / immunology
  • Protein Domains / immunology
  • Recombinant Proteins / drug effects
  • Recombinant Proteins / immunology

Substances

  • Autoantibodies
  • Autoantigens
  • Dipeptidyl-Peptidase IV Inhibitors
  • Dystonin
  • Epitopes
  • Immunoglobulin G
  • Non-Fibrillar Collagens
  • Peptide Fragments
  • Recombinant Proteins
  • DPP4 protein, human
  • Dipeptidyl Peptidase 4
  • Fibrinolysin