I know chaperone proteins help fold proteins that have become denatured, but is it possible for these chaperones to be a cause of misfolding?

I was reading an article posted on here about the prion-like spreading of amyloid-b in Alzheimer's disease and I remember talking about chaperone proteins in my biochem class and how they help refold proteins that have denatured or changed conformation in some way. I was just wondering if there are "defective" chaperones or maybe chaperones that try to fold the wrong proteins or something and if this could lead to the misfolded proteins associated with prion diseases.