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Accumulation of misfolded protein aggregates is a hallmark event in diverse diseases. These structures are able to seed their own polymerization by acting as aggregation nuclei both in vitro and in vivo. Recent studies in animal models suggest that misfolded proteins associated with different diseases can synergize in a heterologous fashion, potentiating pathological mechanisms and accelerating disease progression. The coexistence of misfolded protein aggregates has been described in patients affected by several protein misfolding disorders, suggesting a possible molecular cross-talk between pathological processes associated with different diseases. One putative mechanism for this cross-talk is a direct interaction between misfolded proteins, leading to cross-seeding of protein aggregation. This article summarizes the evidence for the cross-seeding phenomenon recently obtained in studies performed in vitro, in animal models, and in human patients, as well as the potential contribution of this mechanism to our understanding of the still elusive etiology and progression of maladies such as Alzheimer's disease, where no effective diagnostic or therapeutic strategies exist.

Cross-Seeding of Misfolded Proteins: Implications for Etiology and Pathogenesis of Protein Misfolding Diseases