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

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22 Scopus citations


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 (US)
Pages (from-to)717-724
Number of pages8
JournalNeurobiology of Disease
Issue number3
StatePublished - Sep 1 2006


ASJC Scopus subject areas

  • Neurology

Cite this

Moroncini, G., Mangieri, M., Morbin, M., Mazzoleni, G., Ghetti, B., Gabrielli, A., Williamson, R. A., Giaccone, G., & Tagliavini, F. (2006). Pathologic prion protein is specifically recognized in situ by a novel PrP conformational antibody. Neurobiology of Disease, 23(3), 717-724.