Literature DB >> 11214932

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

I Vorberg1, E Pfaff, M H Groschup.   

Abstract

The key event in the pathogenesis of spongiform encephalopathies 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.

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Year:  2000        PMID: 11214932     DOI: 10.1007/978-3-7091-6308-5_27

Source DB:  PubMed          Journal:  Arch Virol Suppl        ISSN: 0939-1983


  1 in total

1.  Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform.

Authors:  Ina Vorberg; Martin H Groschup; Eberhard Pfaff; Suzette A Priola
Journal:  J Virol       Date:  2003-02       Impact factor: 5.103

  1 in total

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