Prion Diseases pp 285-290 | Cite as

The use of monoclonal antibody epitopes for tagging PrP in conversion experiments

  • I. Vorberg
  • E. Pfaff
  • M. H. Groschup
Part of the Archives of Virology. Supplementa book series (ARCHIVES SUPPL, volume 16)


The key event in the pathogenesis of spongiform encephalo-pathies is a conformational transition of a normal cellular protein, PrPsen, to its pathological isoform, PrPres. The mechanism of PrPres formation is unknown but is likely to involve a direct interaction between PrPsen and PrPres. The molecular basis of PrPres formation has been studied extensively using transgenic mice and scrapie-infected tissue cultures that express heterologous PrP molecules. However, these experiments are dependant on the discrimination of endogenous host PrP and exogenous PrP molecules. Here we give a short review on the PrP-specific epitopes that have been used for tagging exogenous PrP molecules and present a novel PrP-specific epitope that is well suitable for in vivo and in vitro conversion experiments.


Prion Protein Conversion Experiment Scrapie Prion Protein Monoclonal Antibody Epitope Syrian Hamster Prion Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer-Verlag Wien 2000

Authors and Affiliations

  • I. Vorberg
    • 1
    • 2
  • E. Pfaff
    • 1
  • M. H. Groschup
    • 1
  1. 1.Federal Research Center for Virus Diseases of AnimalsTüebingenGermany
  2. 2.Laboratory of Persistent Viral Diseases, NIAID, National Institutes of HealthRocky Mountain LaboratoriesHamiltonUSA

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