Cytoplasmic expression of mouse prion protein causes severe toxicity in Caenorhabditis elegans

Kyung Won Park, Liming Li*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


To test if Caenorhabditis elegans could be established as a model organism for prion study, we created transgenic C. elegans expressing the cytosolic form of the mouse prion protein, MoPrP(23-231), which lacks the N-terminal signal sequence and the C-terminal glycosylphosphatidylinisotol (GPI) anchor site. We report here that transgenic worms expressing MoPrP(23-231)-CFP exhibited a wide range of distinct phenotypes: from normal growth and development, reduced mobility and development delay, complete paralysis and development arrest, to embryonic lethality. Similar levels of MoPrP(23-231)-CFP were produced in animals exhibiting these distinct phenotypes, suggesting that MoPrP(23-231)-CFP might have misfolded into distinct toxic species. In combining with the observation that mutations in PrP that affect prion pathogenesis also affect the toxic phenotypes in C. elegans, we conclude that the prion protein-folding mechanism is similar in mammals and C. elegans. Thus, C. elegans can be a useful model organism for prion research.

Original languageEnglish (US)
Pages (from-to)697-702
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Aug 8 2008


  • Aggregation
  • C. elegans
  • Neurodegeneration
  • Prion
  • Protein misfolding
  • Toxicity

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Cytoplasmic expression of mouse prion protein causes severe toxicity in Caenorhabditis elegans'. Together they form a unique fingerprint.

Cite this