Methods for the in vivo and in vitro analysis of [Het-s] prion infectivity

L. Benkemoun, R. Sabate, L. Malato, S. Dos Reis, H.J.P. Dalstra, S.J. Saupe, M.L. Maddelein

Research output: Contribution to journalArticleAcademicpeer-review

17 Citations (Scopus)


Prions have been described in mammals and fungi. The [Het-s] infectious genetic element of the filamentous fungus Podospora anserina is the prion form of the HET-s protein. This protein is involved in the control of a cell death reaction termed heterokaryon incompatibility. The infectious form of HET-s corresponds to a self-perpetuating amyloid. The purpose of the present paper is to describe the techniques that can be used to analyse [Het-s] prion propagation in vivo and HET-s amyloid aggregation in vitro. In addition, we report several methods that can be used to infect Podospora with recombinant HET-s amyloid.
Original languageEnglish
Pages (from-to)61-67
JournalMethods : a companion to Methods in enzymology
Issue number1
Publication statusPublished - 2006


  • fungus podospora-anserina
  • hydrogen/deuterium exchange
  • mass-spectrometry
  • protein
  • transmission
  • yeast
  • incompatibility
  • organization
  • aggregation
  • generation

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