Wild-type human γd-crystallin promotes aggregation of its oxidation-mimicking misfolding-prone W42Q mutant

Abstract

Background: Oxidative damage and destabilizing mutations in γ-crystallins lead to cataract disease. Results: Addition of wild-type γD-crystallin promotes aggregation of the oxidation-mimicking W42Q mutant, yet the wild-type protein escapes coaggregation. Conclusion Wild-type human γD-crystallin can serve as a catalyst for aggregation of its misfolding-prone point mutant. Significance: This finding provides a model of pathology caused by wild-type/mutant or undamaged/damaged protein interactions.