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The aggregation of the tau protein into intraneuronal fibrillar tangles is closely associated with the pathology of Alzheimer’s disease. The endogenous defense system against this process includes molecular chaperones, among which DNAJB6b has emerged as a key component. Using a tau model system comprising the tau fragment 304-380C322S, which spans the amyloidogenic core of ex vivo Alzheimer’s disease fibrils, we investigated the impact of DNAJB6b on tau fibril formation. Here, we show that DNAJB6b potently delays tau aggregation by co-assembling with small tau aggregates and by binding to mature fibrils, thereby reducing their ability to catalyze further fibril growth. This interplay between tau and the chaperone results in greatly reduced fibril formation rate and a lower final fibril mass, which we interpret as increased tau solubility. Moreover, solution-state NMR spectroscopy confirms that DNAJB6b does not interact with tau monomers. Human chaperone DNAJB6b has emerged as a key component involved in the endogeneous defense system against tau protein aggregation in the context of Alzheimer’s disease. Here, the authors study the impact of DNAJB6b on tau fibril formation, showing that it delays tau aggregation by co-assembling with small tau aggregates and by binding to mature fibrils, reducing their ability to catalyze further fibril growth.
