PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

The development of antibodies with binding capacity towards soluble oligomeric forms of PrPSc recognised in the aggregation process in early stage of the disease would be of paramount importance in diagnosing prion diseases before extensive neuropathology has ensued. As blood transfusion appears to...

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Autores principales:	Mourad Tayebi, Daryl Rhys Jones, William Alexander Taylor, Benjamin Frederick Stileman, Charlotte Chapman, Deming Zhao, Monique David
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/76552ae6d7ab4a238b2c18aeea91cb1a
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spelling	oai:doaj.org-article:76552ae6d7ab4a238b2c18aeea91cb1a2021-11-18T06:53:41ZPrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.1932-620310.1371/journal.pone.0019998https://doaj.org/article/76552ae6d7ab4a238b2c18aeea91cb1a2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21625515/?tool=EBIhttps://doaj.org/toc/1932-6203The development of antibodies with binding capacity towards soluble oligomeric forms of PrPSc recognised in the aggregation process in early stage of the disease would be of paramount importance in diagnosing prion diseases before extensive neuropathology has ensued. As blood transfusion appears to be efficient in the transmission of the infectious prion agent, there is an urgent need to develop reagents that would specifically recognize oligomeric forms of the abnormally folded prion protein, PrPSc.To that end, we show that anti-PrP monoclonal antibodies (called PRIOC mAbs) derived from mice immunised with native PrP-coated microbeads are able to immunodetect oligomers/multimers of PrPSc. Oligomer-specific immunoreactivity displayed by these PRIOC mAbs was demonstrated as large aggregates of immunoreactive deposits in prion-permissive neuroblastoma cell lines but not in equivalent non-infected or prn-p(0/0) cell lines. In contrast, an anti-monomer PrP antibody displayed diffuse immunoreactivity restricted to the cell membrane. Furthermore, our PRIOC mAbs did not display any binding with monomeric recombinant and cellular prion proteins but strongly detected PrPSc oligomers as shown by a newly developed sensitive and specific ELISA. Finally, PrioC antibodies were also able to bind soluble oligomers formed of Aβ and α-synuclein. These findings demonstrate the potential use of anti-prion antibodies that bind PrPSc oligomers, recognised in early stage of the disease, for the diagnosis of prion diseases in blood and other body fluids.Mourad TayebiDaryl Rhys JonesWilliam Alexander TaylorBenjamin Frederick StilemanCharlotte ChapmanDeming ZhaoMonique DavidPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 5, p e19998 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mourad Tayebi Daryl Rhys Jones William Alexander Taylor Benjamin Frederick Stileman Charlotte Chapman Deming Zhao Monique David PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.
description	The development of antibodies with binding capacity towards soluble oligomeric forms of PrPSc recognised in the aggregation process in early stage of the disease would be of paramount importance in diagnosing prion diseases before extensive neuropathology has ensued. As blood transfusion appears to be efficient in the transmission of the infectious prion agent, there is an urgent need to develop reagents that would specifically recognize oligomeric forms of the abnormally folded prion protein, PrPSc.To that end, we show that anti-PrP monoclonal antibodies (called PRIOC mAbs) derived from mice immunised with native PrP-coated microbeads are able to immunodetect oligomers/multimers of PrPSc. Oligomer-specific immunoreactivity displayed by these PRIOC mAbs was demonstrated as large aggregates of immunoreactive deposits in prion-permissive neuroblastoma cell lines but not in equivalent non-infected or prn-p(0/0) cell lines. In contrast, an anti-monomer PrP antibody displayed diffuse immunoreactivity restricted to the cell membrane. Furthermore, our PRIOC mAbs did not display any binding with monomeric recombinant and cellular prion proteins but strongly detected PrPSc oligomers as shown by a newly developed sensitive and specific ELISA. Finally, PrioC antibodies were also able to bind soluble oligomers formed of Aβ and α-synuclein. These findings demonstrate the potential use of anti-prion antibodies that bind PrPSc oligomers, recognised in early stage of the disease, for the diagnosis of prion diseases in blood and other body fluids.
format	article
author	Mourad Tayebi Daryl Rhys Jones William Alexander Taylor Benjamin Frederick Stileman Charlotte Chapman Deming Zhao Monique David
author_facet	Mourad Tayebi Daryl Rhys Jones William Alexander Taylor Benjamin Frederick Stileman Charlotte Chapman Deming Zhao Monique David
author_sort	Mourad Tayebi
title	PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.
title_short	PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.
title_full	PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.
title_fullStr	PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.
title_full_unstemmed	PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.
title_sort	prp(sc)-specific antibodies with the ability to immunodetect prion oligomers.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/76552ae6d7ab4a238b2c18aeea91cb1a
work_keys_str_mv	AT mouradtayebi prpscspecificantibodieswiththeabilitytoimmunodetectprionoligomers AT darylrhysjones prpscspecificantibodieswiththeabilitytoimmunodetectprionoligomers AT williamalexandertaylor prpscspecificantibodieswiththeabilitytoimmunodetectprionoligomers AT benjaminfrederickstileman prpscspecificantibodieswiththeabilitytoimmunodetectprionoligomers AT charlottechapman prpscspecificantibodieswiththeabilitytoimmunodetectprionoligomers AT demingzhao prpscspecificantibodieswiththeabilitytoimmunodetectprionoligomers AT moniquedavid prpscspecificantibodieswiththeabilitytoimmunodetectprionoligomers
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PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

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