Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapie-associated fibrils.

Title:

Dataset

identifier:	1274623
description:	epitope description:YEDRYYRE antigen name:Major prion protein host organism:Mus musculus PrP null antibody name:SHA-31
aggregation:	instance of dataset
availability:	available
primaryPublications:	15140886

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1001492
landingPage:	http://www.iedb.org/assay/1274623

Publication

type:	Literature
publicationVenue:	J Biol Chem
dates:	2004

Dimension

study type:	b cell assays
subject species:	Homo sapiens

Person

fullName:	Nathalie Morel Sté phanie Simon Yveline Frobert Hervé Volland Chantal Mourton-Gilles Alessandro Negro Maria Catia Sorgato Christophe Cré minon Jacques Grassi

Data Type

method:	immunoprecipitation

Study

name:	Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapie-associated fibrils.
description:	The human, sheep, and bovine sequences are identical in this redgion. MAb SHA31 immunoprecipitates PrP from brain homogenates of normal or Creutzfeldt-Jakob disease-infected humans and normal or scrapie-infected sheep. The antibody also recognizes PrPsc from protease K-treated human CJD or scrapie-infected sheep brain homogenates, but not from PK-treated normal brain homogenates. Immunoprecipitation of PrP from normal human or CJD untreated brain homogenates is inihibited by preincubation of MAb SHA31 with Pri-4 peptide (residues 126-164 of human PrP which includes the epitope), whereas binding to PrPsc from PK-treated CJD brain homogenates is only partially inhibited. Fab' fragments of SHA31 fail to immunoprecipitate PrPsc but still recognize normal PrP indicating the antibody binding site is not involved in PrPsc binding.

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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