AII amyloid can be induced in mice by a variety of β-sheet rich amyloid fibrils, and cerebral tauopathy can be induced by brain extracts that are rich in aggregated Aβ. There is also experimental evidence for cross-seeding between prion protein and Aβ. In general, such heterologous seeding is less efficient than is seeding by a corrupted form of the same protein.
AII amyloid can be triggered in mice by various β-sheet-rich amyloid fibrils, and cerebral tauopathy can be initiated by brain extracts abundant in aggregated Aβ. There is also experimental evidence of cross-seeding between prion protein and Aβ. Generally, such mixed seeding is less effective than seeding with a corrupted form of the same protein.