Anti-PrP antibodies block PrP(Sc) replication in prion-infected cell cultures by accelerating PrP(C) degradation

The usage of anti-PrP antibodies represent one of the most promising strategy for the treatment of prion diseases. In the present study, we screened various anti-PrP antibodies, with the aim to identify those that will block PrP(Sc) replication in prion infected cell culture. Two antibodies, SAF34 r...

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Main Authors: Perrier, Véronique, Solassol, Jérôme, Crozet, Carole, Frobert, Yveline, Mourton-Gilles, Chantal, Grassi, Jacques, Lehmann, Sylvain
Formato: Artigo
Idioma:English
Publicado em: Blackwell Science 2004
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2063508/
https://ncbi.nlm.nih.gov/pubmed/15056288
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1111/j.1471-4159.2004.02356.x
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spelling pubmed-20635082007-11-15 Anti-PrP antibodies block PrP(Sc) replication in prion-infected cell cultures by accelerating PrP(C) degradation Perrier, Véronique Solassol, Jérôme Crozet, Carole Frobert, Yveline Mourton-Gilles, Chantal Grassi, Jacques Lehmann, Sylvain J Neurochem Article The usage of anti-PrP antibodies represent one of the most promising strategy for the treatment of prion diseases. In the present study, we screened various anti-PrP antibodies, with the aim to identify those that will block PrP(Sc) replication in prion infected cell culture. Two antibodies, SAF34 recognizing the flexible octarepeats region on HuPrP protein and SAF61 directed against PrP amino acid residues (144–152), not only inhibited PrP(Sc) formation in prion-infected neuroblastoma cells but also decreased the PrP(C) levels in non infected N2a cells. In addition, treatment with both SAF34 and SAF61 antibodies decreased the PrP(C) and the PrP(Sc) levels in the cells, synergistically. In presence of both antibodies, our results showed that the mode of action which leads to the disappearance of the PrP(Sc) in cells is directly coupled to PrP(C) degradation by reducing the half-life of the PrP(C) protein. Blackwell Science 2004-04 /pmc/articles/PMC2063508/ /pubmed/15056288 http://dx.doi.org/10.1111/j.1471-4159.2004.02356.x Text en
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Article
spellingShingle Article
Perrier, Véronique
Solassol, Jérôme
Crozet, Carole
Frobert, Yveline
Mourton-Gilles, Chantal
Grassi, Jacques
Lehmann, Sylvain
Anti-PrP antibodies block PrP(Sc) replication in prion-infected cell cultures by accelerating PrP(C) degradation
description The usage of anti-PrP antibodies represent one of the most promising strategy for the treatment of prion diseases. In the present study, we screened various anti-PrP antibodies, with the aim to identify those that will block PrP(Sc) replication in prion infected cell culture. Two antibodies, SAF34 recognizing the flexible octarepeats region on HuPrP protein and SAF61 directed against PrP amino acid residues (144–152), not only inhibited PrP(Sc) formation in prion-infected neuroblastoma cells but also decreased the PrP(C) levels in non infected N2a cells. In addition, treatment with both SAF34 and SAF61 antibodies decreased the PrP(C) and the PrP(Sc) levels in the cells, synergistically. In presence of both antibodies, our results showed that the mode of action which leads to the disappearance of the PrP(Sc) in cells is directly coupled to PrP(C) degradation by reducing the half-life of the PrP(C) protein.
author Perrier, Véronique
Solassol, Jérôme
Crozet, Carole
Frobert, Yveline
Mourton-Gilles, Chantal
Grassi, Jacques
Lehmann, Sylvain
author_facet Perrier, Véronique
Solassol, Jérôme
Crozet, Carole
Frobert, Yveline
Mourton-Gilles, Chantal
Grassi, Jacques
Lehmann, Sylvain
author_sort Perrier, Véronique
title Anti-PrP antibodies block PrP(Sc) replication in prion-infected cell cultures by accelerating PrP(C) degradation
title_short Anti-PrP antibodies block PrP(Sc) replication in prion-infected cell cultures by accelerating PrP(C) degradation
title_full Anti-PrP antibodies block PrP(Sc) replication in prion-infected cell cultures by accelerating PrP(C) degradation
title_fullStr Anti-PrP antibodies block PrP(Sc) replication in prion-infected cell cultures by accelerating PrP(C) degradation
title_full_unstemmed Anti-PrP antibodies block PrP(Sc) replication in prion-infected cell cultures by accelerating PrP(C) degradation
title_sort anti-prp antibodies block prp(sc) replication in prion-infected cell cultures by accelerating prp(c) degradation
publisher Blackwell Science
publisher_facet Blackwell Science
publishDate 2004
url https://ncbi.nlm.nih.gov/pmc/articles/PMC2063508/
https://ncbi.nlm.nih.gov/pubmed/15056288
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1111/j.1471-4159.2004.02356.x
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