The Anti-Prion Antibody 15B3 Detects Toxic Amyloid-β Oligomers

Matteo Stravalaci, Laura Tapella, Marten Beeg, Alessandro Rossi, Pooja Joshi, Erika Pizzi, Michele Mazzanti, Claudia Balducci, Gianluigi Forloni, Emiliano Biasini, Mario Salmona, Luisa DIomede, Roberto Chiesa, Marco Gobbi

Research output: Contribution to journalArticle

Abstract

15B3 is a monoclonal IgM antibody that selectively detects pathological aggregates of the prion protein (PrP). We report the unexpected finding that 15B3 also recognizes oligomeric but not monomeric forms of amyloid-β (Aβ)42, an aggregating peptide implicated in the pathogenesis of Alzheimer's disease (AD). The 15B3 antibody: i) inhibits the binding of synthetic Aβ42 oligomers to recombinant PrP and neuronal membranes; ii) prevents oligomer-induced membrane depolarization; iii) antagonizes the inhibitory effects of oligomers on the physiological pharyngeal contractions of the nematode Caenorhabditis elegans; and iv) counteracts the memory deficits induced by intracerebroventricular injection of Aβ42 oligomers in mice. Thus this antibody binds to pathologically relevant forms of Aβ, and offers a potential research, diagnostic, and therapeutic tool for AD.

Original languageEnglish
Pages (from-to)1485-1497
Number of pages13
JournalJournal of Alzheimer's Disease
Volume53
Issue number4
DOIs
Publication statusPublished - 2016

    Fingerprint

Keywords

  • 15B3 antibody
  • Alzheimer's disease
  • Amyloid beta-protein (1-42)
  • Oligomers
  • Prion protein
  • Prions

ASJC Scopus subject areas

  • Clinical Psychology
  • Geriatrics and Gerontology
  • Psychiatry and Mental health

Cite this