Next Article in Journal
Mutation of the Highly Conserved Ser-40 of the HIV-1 p6 Gag Protein to Phe Causes the Formation of a Hydrophobic Patch, Enhances Membrane Association, and Polyubiquitination of Gag
Next Article in Special Issue
Molecular Modeling of Prion Transmission to Humans
Previous Article in Journal
A Call to Action to Enhance Filovirus Disease Outbreak Preparedness and Response
Previous Article in Special Issue
Low Copper and High Manganese Levels in Prion Protein Plaques
Open AccessReview

Prion Protein-Specific Antibodies-Development, Modes of Action and Therapeutics Application

Prion Biology Laboratory, Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), Trieste 34100, Italy
*
Author to whom correspondence should be addressed.
Viruses 2014, 6(10), 3719-3737; https://doi.org/10.3390/v6103719
Received: 31 July 2014 / Revised: 22 September 2014 / Accepted: 23 September 2014 / Published: 1 October 2014
(This article belongs to the Special Issue Recent Developments in the Prion Field)
Prion diseases or Transmissible Spongiform Encephalopathies (TSEs) are lethal neurodegenerative disorders involving the misfolding of the host encoded cellular prion protein, PrPC. This physiological form of the protein is expressed throughout the body, and it reaches the highest levels in the central nervous system where the pathology occurs. The conversion into the pathogenic isoform denoted as prion or PrPSc is the key event in prion disorders. Prominent candidates for the treatment of prion diseases are antibodies and their derivatives. Anti-PrPC antibodies are able to clear PrPSc from cell culture of infected cells. Furthermore, application of anti-PrPC antibodies suppresses prion replication in experimental animal models. Major drawbacks of immunotherapy are immune tolerance, the risks of neurotoxic side effects, limited ability of compounds to cross the blood-brain barrier and their unfavorable pharmacokinetic. The focus of this review is to recapitulate the current understanding of the molecular mechanisms for antibody mediated anti-prion activity. Although relevant for designing immunotherapeutic tools, the characterization of key antibody parameters shaping the molecular mechanism of the PrPC to PrPSc conversion remains elusive. Moreover, this review illustrates the various attempts towards the development of anti-PrP antibody compounds and discusses therapeutic candidates that modulate PrP expression. View Full-Text
Keywords: prion; PrP; antibody; recombinant antibody; immunotherapy; molecular mechanism prion; PrP; antibody; recombinant antibody; immunotherapy; molecular mechanism
Show Figures

Figure 1

MDPI and ACS Style

Rovis, T.L.; Legname, G. Prion Protein-Specific Antibodies-Development, Modes of Action and Therapeutics Application. Viruses 2014, 6, 3719-3737.

Show more citation formats Show less citations formats

Article Access Map by Country/Region

1
Only visits after 24 November 2015 are recorded.
Search more from Scilit
 
Search
Back to TopTop