The measured level of prion infectivity varies in a predictable way according to the aggregation state of the infectious agent

Joanna Masel, Vincent A.A. Jansen

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

Transmissible spongiform encephalopathies are believed to be caused by an infectious form of the prion protein, designated PrPSc. The concentration of PrPSc is often poorly correlated to the level of infectivity. Infectivity can be measured in two ways, namely endpoint titration and the incubation time assay, but patterns of infectivity vary depending on which method is used. These discrepancies can be explained by variation in the aggregation state of PrPSc. Both methods of measuring infectivity are modelled mathematically, and the theoretical results are in agreement with published data. It was found to be theoretically impossible to characterise prion infectivity by a multiple of a single quantity representing 'one prion', no matter how it is measured. Infectivity is instead characterised by both the number and sizes of the PrPSc aggregates. Apparent discrepancies arise when these complexities are reduced to a single number.

Original languageEnglish (US)
Pages (from-to)164-173
Number of pages10
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Volume1535
Issue number2
DOIs
StatePublished - Feb 14 2001
Externally publishedYes

Keywords

  • Amyloid
  • Incubation time assay
  • Mathematical model
  • One-hit model
  • Prion disease
  • Protein aggregation

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology

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