Are prions misfolded molecular chaperones?
A theory has been developed that could explain prion infection. Prions could be molecular chaperones that are required for their own assembly. The theory has been deduced from an analysis of protein folding and consequences explored by computer simulations. Thermo-kinetic analysis of protein folding shows that a misfolded chaperone gives rise to new misfolded chaperones. Consequently such a protein could behave as a new kind of informative molecule and replicate misfolding according to a process similar to infection. A quantitative model has been derived from this hypothesis that displays the characteristics of prion infections. This hypothesis satisfactorily explains the three manifestations - infection, familial and sporadic - that are the characteristic features of all prion diseases.
Liautard
J P
JP
INSERM U-65, Laboratoire de Biologie Cellulaire, Université de Montpellier II, France.
D000818:Animals; D003198:Computer Simulation; D007562:Creutzfeldt-Jakob Syndrome / Q000209:etiology* / Q000235:genetics; D006801:Humans; D008954:Models, Biological; D011328:Prions / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D012608:Scrapie / Q000209:etiology* / Q000235:genetics; D013816:Thermodynamics
D011328:Prions