IgG autoantibodies in patients with anti-epiligrin cicatricial pemphigoid recognize the G domain of the laminin 5 alpha-subunit. Clin Immunol 2001 Oct;101(1):100-5
Date
10/03/2001Pubmed ID
11580232DOI
10.1006/clim.2001.5091Scopus ID
2-s2.0-0034797368 (requires institutional sign-in at Scopus site) 36 CitationsAbstract
Anti-epiligrin cicatricial pemphigoid (AECP) is a mucosal-predominant, subepithelial blistering disease characterized by IgG anti-basement membrane autoantibodies to laminin 5 (alpha3beta3gamma2). This and prior studies found that autoantibodies from most patients recognize the alpha-subunit of this laminin isoform. Accordingly, sera from 10 representative patients were tested against prokaryotic recombinants of this polypeptide in epitope mapping studies. cDNAs spanning the full length of the alpha-subunit were generated by PCR, directionally cloned into the pGEX-4T-3 vector, and expressed as glutathione-S-transferase fusion proteins of appropriate size and immunoreactivity. Sera from 9 of 10 AECP patients immunoblotted fusion proteins corresponding to subdomains G2, G3, G4, and G5 at the carboxyl terminus of the laminin 5 alpha-subunit. Serum from 1 patient (and that from normal volunteers) showed no reactivity to any fusion proteins; no sera bound recombinant glutathione-S-transferase alone. Immunoadsorption of patient sera with fusion proteins corresponding to the G domain substantially reduced basement membrane autoantibody titers. IgG from patients with this form of cicatricial pemphigoid recognize the portion of laminin 5 thought to play a key role in promoting keratinocyte adhesion to epidermal basement membrane.
Author List
Lazarova Z, Yee C, Lazar J, Yancey KBMESH terms used to index this publication - Major topics in bold
AutoantibodiesAutoantigens
Autoimmune Diseases
Cell Adhesion Molecules
Humans
Immunoblotting
Immunoglobulin G
Laminin
Pemphigoid, Benign Mucous Membrane
Protein Structure, Tertiary
Recombinant Fusion Proteins
