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International Immunology, Vol. 12, No. 8, 1135-1143, August 2000
© 2000 Japanese Society for Immunology

Properties of HLA class II molecules divergently associated with Goodpasture's disease

Richard G. Phelps, Victoria Jones1, A. Neil Turner and Andrew J. Rees1

Department of Clinical and Surgical Sciences (Internal Medicine), University of Edinburgh, Royal Infirmary, Edinburgh EH3 9YW, UK
1 Department of Medicine and Therapeutics, University of Aberdeen, Aberdeen AB25 2ZD, UK

Correspondence to: R. G .Phelps

Goodpasture's disease provides an opportunity to analyse molecular mechanisms that may underlie MHC class II associations with autoimmune disease because it is caused by autoimmunity to a defined antigen [the 230 amino acid NC1 domain of the {alpha}3 chain of type IV collagen ({alpha}3(IV)NC1)] and has strong HLA class II associations. We compared the {alpha}3(IV)NC1 peptide binding of class II molecules with strong positive (DR15) and dominant negative (DR7/1) associations using an inhibition binding assay and short synthetic peptides spanning the sequence of {alpha}3(IV)NC1. DR15 in general bound the peptides with low affinity (three of 23 < 100 nM) compared to DR1 and DR7 (12 and 10 < 100 nM respectively), and no peptide bound DR15 with much higher affinity (>10-fold) than both DR1 and DR7. Thus DR15 molecules are unlikely to increase susceptibility to Goodpasture's disease by presenting a particular {alpha}3(IV)NC1-derived peptide uniquely well and DR1/7 are unlikely to protect by their inability to present particular peptides. However DR1/7 could protect by capturing {alpha}3(IV)NC1 peptides and preventing their display bound to DR15; the binding data suggest that all the major (biochemically detectable) {alpha}3(IV)NC1 peptides presented bound to DR15 by DR15 homozygous antigen-presenting cells (APC) would bind preferentially to DR1/7 in DR15, 1/7 heterozygote APC.

Keywords: autoimmunity, Goodpasture's disease, HLA class II molecules, HLA complex

Transmitting editor: L. Simpson


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