A single prion protein peptide can elicit a panel of isoform specific monoclonal antibodies

Peptides ◽  
2006 ◽  
Vol 27 (11) ◽  
pp. 2695-2705 ◽  
Author(s):  
Tanja Vranac ◽  
Katrina Pretnar Hartman ◽  
Mara Popović ◽  
Anja Venturini ◽  
Eva Žerovnik ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Prion Protein ◽  
Prion Protein Peptide

scholarly journals Chicken Monoclonal Antibodies against Synthetic Bovine Prion Protein Peptide.

1998 ◽  
Vol 60 (6) ◽  
pp. 777-779 ◽  
Author(s):  
Kaori MATSUSHITA ◽  
Hiroyuki HORIUCHI ◽  
Shuichi FURUSAWA ◽  
Motohiro HORIUCHI ◽  
Morikazu SHINAGAWA ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Prion Protein ◽  
Prion Protein Peptide

scholarly journals Altered toxicity of the prion protein peptide PrP106–126 carrying the Ala117→Val mutation

2000 ◽  
Vol 346 (3) ◽  
pp. 785-791 ◽  
Author(s):  
David R. BROWN
Keyword(s):  
Point Mutation ◽  
Prion Protein ◽  
Prion Diseases ◽  
Point Mutations ◽  
Human Sequence ◽  
Gene Coding ◽  
Normal Human ◽  
Microtubule Formation ◽  
Β Sheet ◽  
Prion Protein Peptide

The inherited prion diseases such as Gerstmann-Sträussler-Scheinker syndrome (GSS) are linked to point mutations in the gene coding for the cellular isoform of the prion protein (PrPC). One particular point mutation A117V (Ala117 → Val) is linked to a variable pathology that usually includes deposition of neurofibrillary tangles. A prion protein peptide carrying this point mutation [PrP106-126(117V)] was generated and compared with a peptide based on the normal human sequence [PrP106-126(117A)]. The inclusion of this point mutation increased the toxicity of PrP106-126 which could be linked to an increased β-sheet content. An assay of microtubule formation in the presence of tau indicated that PrP106-126 decreased the rate of microtubule formation that could be related to the displacement of tau. PrP106-126 carrying the 117 mutation was more efficient at inhibiting microtubule formation. These results suggest a possible mechanism of toxicity for protein carrying this mutation via destabilization of the cytoskeleton and deposition of tau in filaments, as observed in GSS.

scholarly journals Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc

2014 ◽  
Author(s):  
Alessandro Didonna ◽  
Anja Colja Venturini ◽  
Katrina Hartman ◽  
Tanja Vranac ◽  
Vladka Curin Serbec ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Prion Protein ◽  
Biochemical Characterization ◽  
Prion Diseases ◽  
Physiological Role ◽  
Prion Infection ◽  
Promising Tool ◽  
C Terminus ◽  
N Terminus

Prion diseases are a group of fatal neurodegenerative disorders that affect humans and animals. They are characterized by the accumulation in the central nervous system of a pathological form of the host-encoded prion protein (PrPC). The prion protein is a membrane glycoprotein that consists of two domains: a globular, structured C-terminus and an unstructured N-terminus. The N-terminal part of the protein is involved in different functions in both health and disease. In the present work we discuss the production and biochemical characterization of a panel of four monoclonal antibodies (mAbs) against the distal N-terminus of PrPC using a well-established methodology based on the immunization of Prnp0/0 mice. Additionally, we show their ability to block prion (PrPSc) replication at nanomolar concentrations in a cell culture model of prion infection. These mAbs represent a promising tool for prion diagnostics and for studying the physiological role of the N-terminal domain of PrPC.

scholarly journals A human prion protein peptide (PrP59–91) protects against copper neurotoxicity

2003 ◽  
Vol 8 (10) ◽  
pp. 835-835 ◽  
Author(s):  
M A Chacón ◽  
M I Barría ◽  
R Lorca ◽  
J P Huidobro-Toro ◽  
N C Inestrosa
Keyword(s):  
Prion Protein ◽  
Human Prion Protein ◽  
Prion Protein Peptide

scholarly journals 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

2004 ◽  
Vol 279 (29) ◽  
pp. 30143-30149 ◽  
Author(s):  
Nathalie Morel ◽  
Stéphanie Simon ◽  
Yveline Frobert ◽  
Hervé Volland ◽  
Chantal Mourton-Gilles ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Prion Protein ◽  
Nonspecific Interactions

Cellular effects of a neurotoxic prion protein peptide are related to its ?-sheet content

1998 ◽  
Vol 23 (2) ◽  
pp. 119-128 ◽  
Author(s):  
David R. Brown ◽  
Martin Pitschke ◽  
Detlev Riesner ◽  
Hans A. Kretzschmar
Keyword(s):  
Prion Protein ◽  
Cellular Effects ◽  
Prion Protein Peptide

scholarly journals Mapping the Prion Protein Using Recombinant Antibodies

1998 ◽  
Vol 72 (11) ◽  
pp. 9413-9418 ◽  
Author(s):  
R. Anthony Williamson ◽  
David Peretz ◽  
Clemencia Pinilla ◽  
Hadyn Ball ◽  
Raiza B. Bastidas ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Prion Protein ◽  
Disease Process ◽  
Cellular Prion Protein ◽  
Epitope Region ◽  
Molecular Events ◽  
C Terminus ◽  
Phage Display Libraries ◽  
Recombinant Molecule

ABSTRACT The fundamental event in prion disease is thought to be the posttranslational conversion of the cellular prion protein (PrPC) into a pathogenic isoform (PrPSc). The occurrence of PrPC on the cell surface and PrPSc in amyloid plaques in situ or in aggregates following purification complicates the study of the molecular events that underlie the disease process. Monoclonal antibodies are highly sensitive probes of protein conformation which can be used under these conditions. Here, we report the rescue of a diverse panel of 19 PrP-specific recombinant monoclonal antibodies from phage display libraries prepared from PrP deficient (Prnp0/0) mice immunized with infectious prions either in the form of rods or PrP 27-30 dispersed into liposomes. The antibodies recognize a number of distinct linear and discontinuous epitopes that are presented to a varying degree on different PrP preparations. The epitope reactivity of the recombinant PrP(90-231) molecule was almost indistinguishable from that of PrPC on the cell surface, validating the importance of detailed structural studies on the recombinant molecule. Only one epitope region at the C terminus of PrP was well presented on both PrPC and PrPSc, while epitopes associated with most of the antibodies in the panel were present on PrPCbut absent from PrPSc.

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