Pathologic prion protein is specifically recognized in situ by a novel PrP conformational antibody

Gianluca Moroncini, Michela Mangieri, Michela Morbin, Giulia Mazzoleni, Bernardino Ghetti, Armando Gabrielli, Robert Anthony Williamson, Giorgio Giaccone, Fabrizio Tagliavini

Research output: Contribution to journalArticlepeer-review

Abstract

Prion diseases are characterized by the accumulation in the brain of abnormal conformers (PrPSc) of the cellular prion protein (PrPC). PrPSc immunohistochemistry, currently based on antibodies non-distinguishing between PrPC and PrPSc, requires pre-treatments of histological sections to eliminate PrPC and to denature PrPSc. We employed the PrPSc-specific antibody 89-112 PrP motif-grafted IgG on mildly fixed, untreated brain sections from several cases of human prion diseases. The results confirmed specific binding of IgG 89-112 to a structural determinant found exclusively on native disease-associated PrP conformations and lost following tissue denaturation or cross-linking fixation. Importantly, IgG 89-112 demonstrated no reactivity with normal brain tissue or with amyloid deposits in Alzheimer disease brain sections. Thus, immunohistochemical detection of native PrPSc deposits was obtained by means of a PrPSc-specific antibody. Such unique reagent may have many applications in the study of prion biology and in the diagnosis and prevention of prion diseases.

Original languageEnglish
Pages (from-to)717-724
Number of pages8
JournalNeurobiology of Disease
Volume23
Issue number3
DOIs
Publication statusPublished - Sep 2006

ASJC Scopus subject areas

  • Neurology

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