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Molecular architecture of the Goodpasture autoantigen in anti-GBM nephritis

  • Vadim Pedchenko
  • , Olga Bondar
  • , Agnes Fogo
  • , Roberto Vanacore
  • , Paul Voziyan
  • , Arthur Richard Kitching
  • , Jorgen Wieslander
  • , Clifford Kashtan
  • , Dorin-Bogdan Borza
  • , Eric Neilson
  • , Curtis B Wilson
  • , Billy G Hudson

Research output: Contribution to journalArticleResearchpeer-review

Abstract

In Goodpasture s disease, circulating autoantibodies bind to the noncollagenous-1 (NC1) domain of type IV collagen in the glomerular basement membrane (GBM). The specificity and molecular architecture of epitopes of tissue-bound autoantibodies are unknown. Alport s post-transplantation nephritis, which is mediated by alloantibodies against the GBM, occurs after kidney transplantation in some patients with Alport s syndrome. We compared the conformations of the antibody epitopes in Goodpasture s disease and Alport s post-transplantation nephritis with the intention of finding clues to the pathogenesis of anti-GBM glomerulonephritis.
Original languageEnglish
Pages (from-to)343 - 354
Number of pages12
JournalThe New England Journal of Medicine
Volume363
Issue number4
DOIs
Publication statusPublished - 2010

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