Structure prion diseases associated with

Prion diseases may be genetic or infectious. Nineteen mutations of the PrP gene are associated with inherited human prion disease, all distinguishable by their phenotypes, e.g. patients with Val-129 on the mutant allele develop familial CJD, whereas those with Met-129 develop FFI. The ability of prion diseases to cross species barriers depends, at least in part, on the structural similarity between the respective PrP amino acid sequences. 

Rappley I, Myers DS, Milne SB, et al. Lipidomic profiling in mouse brain reveals differences between ages and genders, with smaller changes associated with alpha-synuclein genotype. /Neumchem. 2009 lll(l) 15-25. Fantini J, Garmy N, Mahfoud RS, Yahi N. Lipid rafts structure, function and role in HIV, Alzheimer s and prion diseases. Exp Rev Mol Med. 2002 4(27) l-22. 

A notorious example of continuous self-association occurs in the prion proteins, which are responsible for neurodegenerative diseases such as BSE (mad cow disease). An isolated prion protein, a normal constituent of nerve cells, undergoes, for unknown reasons, a switch from its normal to an aberrant structure. This has a high affinity for like molecules, which are accordingly dragged into the aberrant structural state by the rogue subunit, to which they bind. This initiates a wholesale process of filament formation with catastrophic effects on the cell. Or so... 

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