%0 Journal Article %J J Alzheimers Dis %D 2016 %T The Anti-Prion Antibody 15B3 Detects Toxic Amyloid-β Oligomers. %A Stravalaci, Matteo %A Tapella, Laura %A Beeg, Marten %A Rossi, Alessandro %A Joshi, Pooja %A Pizzi, Erika %A Mazzanti, Michele %A Balducci, Claudia %A Forloni, Gianluigi %A Biasini, Emiliano %A Salmona, Mario %A Diomede, Luisa %A Chiesa, Roberto %A Gobbi, Marco %X

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.

%B J Alzheimers Dis %V 53 %P 1485-97 %8 2016 Jul 06 %G eng %N 4 %1 http://www.ncbi.nlm.nih.gov/pubmed/27392850?dopt=Abstract %R 10.3233/JAD-150882