from Keiji Uchiyama and Suehiro Sakaguchi writing in Prions: Current Progress in Advanced Research:

Prion diseases, which include Creutzfeldt-Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE) in animals, are a group of incurable neurodegenerative disorders caused by proteinaceous infectious agents, the so-called prions. No preventative vaccines and therapeutics of prion diseases have been developed. Recent lines of evidence suggest that antibodies against prion protein might be beneficial for both preventing and treating prion disease. In this chapter, we first discuss the possibility that there might be many individuals who are latently infected with vCJD prions in human populations, and then introduce the so far reported immunological approaches for development of prion vaccines and immunotherapy against prion disease, including our recent work.

Further reading: Prions: Current Progress in Advanced Research

from Hideharu Shintani and Gerald McDonnell writing in Prions: Current Progress in Advanced Research:

Several inactivation procedures to prion and endotoxins are reported so far. Most of these methods are not applicable to re-usable medical devices due to failure of achievement of material and functional compatibility. Gas plasma inactivation procedure for prion and endotoxin was studied and attain both sterility assurance level (SAL) of 10^-6 and material and functional compatibility in ease.

Further reading: Prions: Current Progress in Advanced Research

from Hermann C. Altmeppen, Berta Puig, Susanne Krasemann, Clemens Falker, Frank Dohler and Markus Glatzel writing in Prions: Current Progress in Advanced Research:

Prion diseases or transmissible spongiform encephalopathies are fatal neurodegenerative conditions occurring in humans and animals that may be transmitted. Experimental data and neuropathological examinations show that prions (here defined as the agent responsible for transmissible spongiform encephalopathies) consist of a self-propagating isoform of the cellular prion protein. Nucleic acids are not required for propagation of prions. In the last years a number of questions regarding the mechanism of prion propagation and neurotoxicity as well as the spread of prions to and within the brain have been answered, yet essential pieces of information regarding the execution of cell death and cell-to-cell spread of prions remain to be elucidated.

Further reading: Prions: Current Progress in Advanced Research

from Takashi Onodera and Akikazu Sakud writing in Prions: Current Progress in Advanced Research:

Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal neurological diseases that include Creutzfeldt-Jakob Disease (CJD) in humans, scrapie in sheep and goats, bovine spongiform encephalopathy (BSE) in cattle, and chronic wasting disease (CWD) in cervids. A key event in prion diseases is the conversion of the cellular, host-encoded prion protein (PrP^C) to its abnormal isoform (PrP^Sc) predominantly in the central nervous system of the infected host (Aguzzi et al. 2004).The diseases are transmissible under some circumstances, but unlike other transmissible disorders, prion diseases can also be caused by mutations in the host gene. The mechanism of prion spread among sheep and goats that develop natural scrapie is unknown. CWD, transmissible mink encephalopathy (TME), BSE, feline spongiform encephalopathy (FSE), and exotic ungulate encephalopathy (EUE) are all thought to occur after the consumption of prion-infected material. Most cases of human prion disease occur from unknown reasons, and >20 mutation in the prion gene may lead to inherited prion disease. In other instances, prion diseases are contracted by exposure to prion infectivity. This raises the question of how a mere protein aggregate can trespass mucosal barriers, circumvent innate and adoptive immunity, and travel across the blood-brain barrier to eventually provoke brain disease. To start the chapters of this book we will introduce a few topics in current prion studies.

Further reading: Prions: Current Progress in Advanced Research

from Akikazu Sakudo writing in Prions: Current Progress in Advanced Research:

Prion diseases are devastating neurodegenerative disorders caused by infectious proteinaceous agents known as prions. Prion protein (PrP) gene (Prnp)-deficient mice do not infect with prion agent, indicating essential role of PrP for prion diseases. An abnormal isoform of prion protein (PrP), known as PrP^Sc, which is converted from cellular PrP (PrP^C), is thought to constitute the prion agent. Recently, proteins homologous to PrP have been found, suggesting the existence of other PrP family members, which so far include PrP, Doppel (Dpl) and Shadoo (Sho). In this chapter, the author introduces recent research on the physiological function of PrP and PrP-related proteins together with our own studies.

Further reading: Prions: Current Progress in Advanced Research