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Natural anti-GBM antibodies from normal human sera recognize alpha 3(IV)NC1 restrictively and recognize the same epitopes as anti-GBM antibodies from patients with anti-GBM disease

Yang, Rui; Cui, Zhao; Hellmark, Thomas LU ; Segelmark, Marten; Zhao, Ming-hui and Wang, Hai-yan (2007) In Clinical Immunology 124(2). p.207-212
Abstract
Anti-GBM disease is a rare autoimmune condition characterized by autoantibodies targeting the alpha 3 chain non-collagen 1 domain of type IV collagen (alpha 3(IV)NC1). Recently, we isolated IgG reacting with alpha 3(IV)NC1 from normal healthy human sera. The current study examined the antigen and epitope specificity of these natural autoantibodies (NAA) using recombinant human alpha 1, 3, 5(IV)NC1 and three constructs expressing, previously defined epitope regions designated E-A, E-B and S2, in the alpha 1(IV)NC1 background. The NAA preparations reacted with recombinant human alpha 3(IV) NC1 to the same extent as with purified bovine alpha(IV)NC1, but not with recombinant human alpha 1 and alpha 5 (IV)NC1. NAA preparations recognized the... (More)
Anti-GBM disease is a rare autoimmune condition characterized by autoantibodies targeting the alpha 3 chain non-collagen 1 domain of type IV collagen (alpha 3(IV)NC1). Recently, we isolated IgG reacting with alpha 3(IV)NC1 from normal healthy human sera. The current study examined the antigen and epitope specificity of these natural autoantibodies (NAA) using recombinant human alpha 1, 3, 5(IV)NC1 and three constructs expressing, previously defined epitope regions designated E-A, E-B and S2, in the alpha 1(IV)NC1 background. The NAA preparations reacted with recombinant human alpha 3(IV) NC1 to the same extent as with purified bovine alpha(IV)NC1, but not with recombinant human alpha 1 and alpha 5 (IV)NC1. NAA preparations recognized the three chimeric proteins (E-A, E-B and S2) yielding similar absorbance values. We conclude that anti-GBM NAA recognize the same major epitopes as anti-GBM antibodies from patients with Goodpasture's disease. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
natural anti-GBM antibody, antigen specificity, epitope mapping
in
Clinical Immunology
volume
124
issue
2
pages
207 - 212
publisher
Elsevier
external identifiers
  • wos:000248371100012
  • scopus:34447544275
ISSN
1521-6616
DOI
10.1016/j.clim.2007.05.001
language
English
LU publication?
yes
id
16eced75-427e-4ab0-95ec-da08a8354f9e (old id 647830)
date added to LUP
2007-12-19 09:39:18
date last changed
2017-09-03 03:43:36
@article{16eced75-427e-4ab0-95ec-da08a8354f9e,
  abstract     = {Anti-GBM disease is a rare autoimmune condition characterized by autoantibodies targeting the alpha 3 chain non-collagen 1 domain of type IV collagen (alpha 3(IV)NC1). Recently, we isolated IgG reacting with alpha 3(IV)NC1 from normal healthy human sera. The current study examined the antigen and epitope specificity of these natural autoantibodies (NAA) using recombinant human alpha 1, 3, 5(IV)NC1 and three constructs expressing, previously defined epitope regions designated E-A, E-B and S2, in the alpha 1(IV)NC1 background. The NAA preparations reacted with recombinant human alpha 3(IV) NC1 to the same extent as with purified bovine alpha(IV)NC1, but not with recombinant human alpha 1 and alpha 5 (IV)NC1. NAA preparations recognized the three chimeric proteins (E-A, E-B and S2) yielding similar absorbance values. We conclude that anti-GBM NAA recognize the same major epitopes as anti-GBM antibodies from patients with Goodpasture's disease.},
  author       = {Yang, Rui and Cui, Zhao and Hellmark, Thomas and Segelmark, Marten and Zhao, Ming-hui and Wang, Hai-yan},
  issn         = {1521-6616},
  keyword      = {natural anti-GBM antibody,antigen specificity,epitope mapping},
  language     = {eng},
  number       = {2},
  pages        = {207--212},
  publisher    = {Elsevier},
  series       = {Clinical Immunology},
  title        = {Natural anti-GBM antibodies from normal human sera recognize alpha 3(IV)NC1 restrictively and recognize the same epitopes as anti-GBM antibodies from patients with anti-GBM disease},
  url          = {http://dx.doi.org/10.1016/j.clim.2007.05.001},
  volume       = {124},
  year         = {2007},
}