Prion proteins as memory molecules: An hypothesis

P. Tompa, P. Friedrich

Research output: Contribution to journalComment/debate

38 Citations (Scopus)


Prions are infectious agents widely implicated in a variety of mammalian neurodegenerative diseases generally referred to as transmissible spongiform encephalopathies. Their infectivity is primarily associated with an aberrant conformation of a host-encoded protein, the priori protein, induced by the prion itself in an autocatalytic reaction. The physiological function of this protein is not known. In this paper we suggest that alternative conformations of the prion protein, other than its pathological scrapie state, exist and that the self-sustaining autocatalytic propagation of these states underlies its normal cellular function. In kinetic model calculations we show that the prion protein may constitute a bi-stable molecular switch that can structurally encode and stably store information. A number of cases of priori involvement in normal cellular function and ample molecular detail of pathological prion propagation are cited and correlated to substantiate the implications of this tenet. Our contention is that the prion hypothesis should be extended to a wide variety of physiological processes. We propose that prion proteins are stable determinants of phenotype, operating in diverse functions possibly including memory.

Original languageEnglish
Pages (from-to)1037-1043
Number of pages7
Issue number4
Publication statusPublished - Jan 1 1998


  • Conformational switch
  • Kinetic simulation
  • Memory molecule
  • Phenotypic determinant
  • Physiological function
  • Prion protein

ASJC Scopus subject areas

  • Neuroscience(all)

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