[The gene of human prion: reassessment of its features and pathogenic role]

After a detailed examination of some features of the human prion gene, we propose a reassessment of its role in the pathogenicity of the derived neurodegenerative diseases e.g. Creutzfeldt-Jakob's disease. The particular resistance of this gene towards physico-chemical agents is related to the relative abundance of the guanine and cytosine bases. Other features such as the paucity of CpG sequences, GC box, polyadenylic tail, direct and inverted repeats, all evoke those of retroviral LTRs. Finally, the presence of polypurinic and polyadenylic sequences, as well as that of a functional AP2 element coding a superantigen are all reminiscent of a parenthood of this gene with that of the murine virus MMTV, whose pathogenicity is based on the interaction between either endogenous or exogenous mutated viral forms. A similar biological behavior between, respectively the MMTV virus and the endogenous plus exogenous infectious forms of the prion is therefore suggested. All these clues are in agreement with the prominent data of the natural history of prion diseases, but il would be necessary that the prion protein should be associated with a nucleic acid belonging to its own gene and which would play a role in the animal or human illness, together with the endogenous prion gene. Thus, some exogenous forms originating from animals, e.g. bovine or perhaps ovine ones, could recombine with the human prion gene and would be responsible for the human illnesses.