The use of monoclonal antibody epitopes for tagging PrP in conversion experiments.
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.
Vorberg
I
I
Federal Research Center for Virus Diseases of Animals, Tüebingen, Germany.
Pfaff
E
E
Groschup
M H
MH
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D006224:Cricetinae; D000939:Epitopes / Q000276:immunology; D051379:Mice; D018621:PrPC Proteins / Q000737:chemistry* / Q000276:immunology* / Q000378:metabolism; D018620:PrPSc Proteins / Q000737:chemistry* / Q000276:immunology* / Q000378:metabolism; D011487:Protein Conformation; D012608:Scrapie / Q000209:etiology / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D000911:Antibodies, Monoclonal; D000939:Epitopes; D018621:PrPC Proteins; D018620:PrPSc Proteins