Microbiology and Immunology
© The Societies and John Wiley & Sons Australia, Ltd
Edited By: Shigetada Kawabata, Takaji Wakita and Yasunobu Yoshikai
Impact Factor: 1.428
ISI Journal Citation Reports © Ranking: 2015: 100/123 (Microbiology); 137/151 (Immunology)
Online ISSN: 1348-0421
Virtual Special Issue on Prion
Impact of prions
Takashi Onodera (1)* and Akikazu Sakudo (2)
1 Research Center for Food Safety, School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku Yayoi 1-1-1, Tokyo 113-8657, Japan 2 Laboratory of Biometabolic Chemistry, School of Health Sciences, Faculty of Medicine, University of the Ryukyus, 207 Uehara, Nishihara, Okinawa 903-0215, Japan
*To whom correspondence should be addressed: Research Center for Food Safety, School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku Yayoi 1-1-1, Tokyo 113-8657, Japan Tel and Fax:+81-3-5841-5196 E-mail: firstname.lastname@example.org
Prion diseases are a unique category of illness, the pathogenesis of which is related to conformational changes in the normal protein, PrPC (cellular prion protein), to a form with a high β-sheet content, PrPSc (abnormal prion protein), that is protease resistant and infectious. These diseases include bovine spongiform encephalopathy (BSE) in cattle, scrapie in sheep, and Creutzfeldt-Jakob disease (CJD) in humans (1). The appearance of variant CJD (vCJD) has raised public health concerns that BSE might be transmissible to humans across species through dietary exposure to BSE-contaminated foodstuffs. In addition, human cases of vCJD have recently emerged in the UK, many years after the eradication of BSE from the country, due to the very long incubation times of prion diseases, which range from months to decades.
Since 1996, increasing incidence of BSE and vCJD have been noted and accumulating evidence has confirmed a link between BSE and vCJD. The extent of BSE epidemic was probably amplified by introducing the infected cattle to the rendering process. However, BSE is not readily transmitted either horizontally or vertically, and the epidemic has been self limiting with feed ban imposed in the year of 2001 (2). It is still not clear whether or not maternal-offspring transmission of BSE will occur in affected animals. Mouse transmission and strain-typing from Japanese BSE and scrapie agents are the important subjects in the transmission perspective.
Experimental transmission of prion disease was achieved using non-human primates, but can now be done effectively using rodents in Japanese studies by Tateishi J. et al (1). There are several key points in transmission experiments as follows; Selection of susceptible mouse strains such as NZW, CF#1, C57BL, and BALB/C; strict inactivation of the pathogen to avoid cross-contamination by boiling contaminated instruments in 3% sodium dodecyl sulfate (SDS) solution for 10 min; and correct evaluation of clinico- pathological findings including immunohistochemical analysis of every mouse brain section. Immunostaining of anti-PrP antibodies can exclude physiological vacuolation due to aging and autolytic vacuoles as well as possible contamination of mouse-adapted PrPSc in the primary transmission experiments.
Prion diseases belong to a new disease group having the characteristics of both transmissible and heredodegenerative disease. Transmission from sporadic CJD patients with wild-type PrP gene is highly positive and incubation periods are relatively uniform. Inocula from 44 of 51 human patients transmitted the disease, with mean incubation periods of between 573 and 865 days after inoculation according to Tateishi J. group’s study (1). Hereditary patients with E200K and M232R mutations have clinicopathological features and transmission frequencies similar to those of sporadic CJD patients with 129M/M. Transmission to mice from patients with fatal familial insomnia (FFI) and FFI-like symptoms with localized thalamic lesions with or without PrP gene mutations D178N and 129M on the same allele has been successful. Inocula from 5 of 15 patients with P105L transmitted the disease to mice. From patients with A117V, Y145stop, and insertion mutations, transmissions were negative even after repeated inoculation. Therefore these mutations result in a low infectious nature (1).
Since the outbreak Japanese BSE in 2001 (2), so many manuscripts were submitted to Microbiology and Immunology from young scientists in this field. Most of them are basically high quality in their result. In this virtual issue of Microbiology and Immunology (Prion) we could enjoy the enthusiasms and discussion preformed by young scientists in prion biology.
Uptake dynamics of scrapie agent in the intestinal villous epithelium of suckling and weanling Syrian hamsters
Kono J, Toyoshima R, Iseki T, Sato Y, Umematu A, Okano M, Tashiro A, Ano Y, Sata T, Yokoyama T, Onodera T, Yukawa M.
Strain-specific effects of reducing agents on the cell-free conversion of recombinant prion protein into protease-resistant form
Imamura M, Kato N, Okada H, Iwamaru Y, Shimizu Y, Mohri S, Yokoyama T.
Deduction of the evaluation limit and termination timing of multi-round protein misfolding cyclic amplification from a titration curve
Atsuko Takeuchi, Mayumi Komiya, Tetsuyuki Kitamoto, Masanori Morita
Sc237 hamster PrPSc and Sc237-derived mouse PrPSc generated by interspecies in vitro amplification exhibit distinct pathological and biochemical properties in tga20 transgenic mice
Miyako Yoshioka, Morikazu Imamura, Hiroyuki Okada, Noriko Shimozaki, Yuichi Murayama, Takashi Yokoyama and Shirou Mohri
The effects of lysosomal and proteasomal inhibitors on abnormal forms of prion protein degradation in murine macrophages
Yukiko Sassa, Takeshi Yamasaki, Motohiro Horiuchi, Yasuo Inoshima and Naotaka Ishiguro
A novel anti-prion protein monoclonal antibody and its single-chain fragment variable derivative with ability to inhibit abnormal prion protein accumulation in cultured cells
Yoshihisa Shimizu, Yuko Kaku-Ushiki, Yoshifumi Iwamaru, Tamaki Muramoto, Tetsuyuki Kitamoto, Takashi Yokoyama, Shirou Mohri and Yuichi Tagawa
Intraspecies transmission of L-type-like bovine spongiform encephalopathy detected in Japan
Shigeo Fukuda, Yoshifumi Iwamaru, Morikazu Imamura, Kentarou Masujin, Yoshihisa Shimizu, Yuichi Matsuura, Yujing Shu, Megumi Kurachi, Kazuo Kasai, Yuichi Murayama, Sadao Onoe, Ken’ichi Hagiwara, Tetsutaro Sata, Shirou Mohri, Takashi Yokoyama and Hiroyuki Okada
Incorporation of β-amyloid protein through the bovine ileal epithelium before and after weaning: Model for orally transmitted amyloidoses
Yasuhisa Ano, Hiroyuki Nakayama, Yusuke Sakai, Akikazu Sakudo, Maiko Endo, Shogo Ebisu, JunYou Li, Koji Uetsuka, Noboru Manabe and Takashi Onodera
Synthetic fibril peptide promotes clearance of scrapie prion protein by lysosomal degradation
Yuko Okemoto-Nakamura, Yoshio Yamakawa, Kentaro Hanada, Keiko Tanaka, Masami Miura, Isei Tanida, Masahiro Nishijima and Ken'ichi Hagiwara
Distinct immunohistochemical localization in Kuru plaques using novel anti-prion protein antibodies
Tomoko Hosokawa, Fumiko Ono, Kotaro Tsuchiya, Ichiro Sato, Natsumi Takeyama, Susumu Ueda, Gianluigi Zanusso, Hidehiro Takahashi, Tetsutaro Sata, Akikazu Sakudo, Katsuaki Suguira, Andreina Baj, Antonio Toniolo, Yasuhiro Yoshikawa and Takashi Onodera
Isolation of Scrapie Agent from the Placenta of Sheep with Natural Scrapie in Japan
Takashi Onodera,Toshio Ikeda,Yasukazu Muramatsu and Morikazu Shinagawa
Practical Methods for Chemical Inactivation of Creutzfeldt-Jakob Disease Pathogen
Jun Tateishi,Takatoshi Tashima and Tetsuyuki Kitamoto
Characterization of Scrapie Agent Isolated from Sheep in Japan
Morikazu Shinagawa,Kaname Takahashi,Satoshi Sasaki,Satoshi Doi,Hitoshi Goto and Gihei Sato
1. Tateishi J. (1995) Prion diseases. Microbiol. Immunol. 39: 923-8.
2. Onodera T., Sakudo A., Wu G.Y., Saeki K. (2006) Bovine spongiform encephalopathy in Japan: History and recent studies on oxidative stress in prion diseases. Microbiol. Immunol. 50: 565-78.