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

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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; Segelmark, Marten; Zhao, Ming-hui; Wang, Hai-yan.

I: Clinical Immunology, Vol. 124, Nr. 2, 2007, s. 207-212.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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T1 - 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

AU - Yang, Rui

AU - Cui, Zhao

AU - Hellmark, Thomas

AU - Segelmark, Marten

AU - Zhao, Ming-hui

AU - Wang, Hai-yan

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

KW - natural anti-GBM antibody

KW - antigen specificity

KW - epitope mapping

U2 - 10.1016/j.clim.2007.05.001

DO - 10.1016/j.clim.2007.05.001

M3 - Article

VL - 124

SP - 207

EP - 212

JO - Clinical Immunology

T2 - Clinical Immunology

JF - Clinical Immunology

SN - 1521-6616

IS - 2

ER -