title: A route for prion neuroinvasion.
abstract: The astonishing recognition that self-propagating changes in protein structure may be at the basis of spongiform encephalopathies is changing our views of transmissible diseases. Infectious agents consisting of abnormally folded proteins (i.e., the prion) can propagate in host organisms using previously unrecognized routes and invade the brain after a dangerous liaison with the immune system. The identification of the nodal points of neuroinvasion and new techniques to amplify minute amounts of misfolded proteins may open the possibility for post exposure prophylaxis.
authors.affiliation: MRC Toxicology Unit, Hodgkin Building, University of Leicester, Lancaster Road, LE1 9HN, Leicester, United Kingdom. pn10@le.ac.uk
authors.forename: P
authors.initials: P
authors.lastname: Nicotera
mesh_terms: D000818:Animals; D001812:Blood-Brain Barrier; D001921:Brain / Q000473:pathology / Q000502:physiology* / Q000503:physiopathology; D006801:Humans; D017096:Prion Diseases / Q000473:pathology / Q000503:physiopathology*; D011328:Prions / Q000472:pathogenicity* / Q000502:physiology; D017510:Protein Folding
chemical_list: D011328:Prions