Tracking protein aggregate interactions

Amyloid fibrils share a structural motif consisting of highly ordered β-sheets aligned perpendicular to the fibril axis. ^1,2 At each fibril end, β-sheets provide a template for recruiting and converting monomers. ³ Different amyloid fibrils often co-occur in the same individual, yet whether a protein aggregate aids or inhibits the assembly of a heterologous protein is unclear. In prion disease, diverse prion aggregate structures, known as strains, are thought to be the basis of disparate disease phenotypes in the same species expressing identical prion protein sequences. ^4-7 Here we explore the interactions reported to occur when two distinct prion strains occur together in the central nervous system.