Abstract:
:Prion diseases are a group of fatal neurodegenerative disorders that affect humans and animals. They are characterized by the accumulation in the central nervous system of a pathological form of the host-encoded prion protein (PrP(C)). The prion protein is a membrane glycoprotein that consists of two domains: a globular, structured C-terminus and an unstructured N-terminus. The N-terminal part of the protein is involved in different functions in both health and disease. In the present work we discuss the production and biochemical characterization of a panel of four monoclonal antibodies (mAbs) against the distal N-terminus of PrP(C) using a well-established methodology based on the immunization of Prnp (0/0) mice. Additionally, we show their ability to block prion (PrP(Sc)) replication at nanomolar concentrations in a cell culture model of prion infection. These mAbs represent a promising tool for prion diagnostics and for studying the physiological role of the N-terminal domain of PrP(C).
journal_name
PeerJjournal_title
PeerJauthors
Didonna A,Venturini AC,Hartman K,Vranac T,Čurin Šerbec V,Legname Gdoi
10.7717/peerj.811subject
Has Abstractpub_date
2015-03-19 00:00:00pages
e811issn
2167-8359pii
811journal_volume
3pub_type
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