Article citationsMore>>

T. Kitamoto, K. Doh-ura, T. Muramoto, M. Miyazono and J. Tateishi, “The Primary Structure of the Prion Protein Influences the Distribution of Abnormal Prion Protein in the Central Nervous System,” American Journal of Pathology, Vol. 141, No. 2, 1992, pp. 271-277.

has been cited by the following article:

• TITLE: A Rapid Bioassay for Classical and L-Type Bovine Spongiform Encephalopathies

  AUTHORS: Yuichi Matsuura, Yukiko Ishikawa, Robert A. Somerville, Takashi Yokoyama, Ken’ichi Hagiwara, Yoshio Yamakawa, Tetsutaro Sata, Tetsuyuki Kitamoto, Shirou Mohri

  KEYWORDS: Bovine Spongiform Encephalopathy; Follicular Dendritic Cell; Transgenic Mice

  JOURNAL NAME: Open Journal of Veterinary Medicine, Vol.3 No.1, March 27, 2013

  ABSTRACT: The rapid detection of infectivity of several agents that cause Creutzfeldt-Jakob disease has previously been achieved by assaying for deposits of abnormal prion protein (PrPSc) in follicular dendritic cells in the spleens of transgenic mice carrying the human prion protein gene. In this study, transgenic mice expressing the bovine prion protein were inoculated intraperitoneally with classical (C-type) or atypical L-type bovine spongiform encephalopathies (BSE). Proteinase-resistant PrPSc were detected in the spleens of all transgenic mice at 75 days after inoculation with both types of BSE. Infectivity in PrPSc-positive spleens of the transgenic mice revealed that prions of C- and L-type BSE replicated. These results suggest that bioassay system by the transgenic mice could be useful for the rapid detection of BSE infectivity with discriminating between C- and L-type BSEs.