Publication Date

2026

Presentation Length

Poster/Gallery presentation

College

College of Sciences & Mathematics

Department

Biology, Department of

Student Level

Undergraduate

Faculty Mentor

Andrea Florian

Presentation Type

Poster

Summary

Goodpasture’s syndrome (GP) is an autoimmune disorder that primarily affects kidneys and lungs. The main issue for patients with Goodpasture's syndrome is the binding of autoantibodies to the glomerular basement membrane (GBM), which hinders the filtration of blood. A key characteristic of Goodpasture's syndrome is the presence of autoantibodies that target the NC1 domain of the α345 isoform of type IV collagen, a crucial component of the GBM that provides structural support and is critical for filtration function. Sulfilimine bonds crosslink the collagen IV NC1 hexamers, contributing to the stabilization of these structures. A recent clinical case of recurring Goodpasture's disease suggests that environmental triggers may play a role in its pathway, although the exact mechanisms are still unclear. We hypothesize that these environmental triggers lead to the rearrangement of the epitope and that the removal of sulfilimine crosslinks could amplify the effects of these triggers. In this study, NC1 hexamers of collagen IV were purified from bovine glomeruli and subject them to chemical reduction to eliminate the sulfilimine crosslinks. ELISA assays were then performed to assess the binding of human autoantibodies from Goodpasture’s syndrome to both crosslinked and non-crosslinked NC1 hexamers in the presence of various environmental triggers. The group of potential triggers that will be investigated consists of pesticides that are commonly used in farming. SDS page electrophoresis and mass photometry were also used as an alternative methods to detect auto-antibodies binding.

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