Method of screening prion disease infection factor

Details Method of screening prion disease infection factor Method of screening prion disease infection factor

2002-01-31

2008-11-18

Chen, Stacy B (Department: 1648)

Chemistry: molecular biology and microbiology

Virus or bacteriophage, except for viral vector or...

C800S021000

Reexamination Certificate

active

07452709

ABSTRACT:
Early detection of infectious agents of human prion diseases such as CJD by using an animal model, etc. is needed in order to rapidly determine prion infections in pharmaceuticals such as blood products, foods, or cosmetics. This invention provides a screening method for infectious agents of human or non-human prion diseases in samples, which employs, as an indication, the deposition of the aberrant prion protein in the follicular dendritic cell (FDC) of a non-human animal.

REFERENCES:
patent: WO 97/04814 (1997-02-01), None
patent: WO 00/71575 (2000-11-01), None
Wall et al., Transgenic livestock: Progress and prospects for the future. 1996, Theriogenology vol. 45, p. 57-68.
Mullins et al., Molecular Medicine in Genetically Engineered Animals. 1996, Journal of Clinical Investigation vol. 97, p. 1557-1560.
Houdebine Production of pharmaceutical proteins from transgenic animals. 1994, Journal of Biotechnology. vol. 34, p. 269-287.
Ebert et al., A Moloney MLV-Rat Somatotropin fusion gene produces biologically active somatotropin in a transgenic pig. 1988, Molecular Endocrinology, p. 277-283.
Kappel et al., Regulating gene expression in transgenic animals. 1992. Current Opinion in Biotechnology, vol. 3, p. 548-553.
Hammer et al., Genetic engineering of mammalian embryos. 1986. J. Animal Science. vol. 63, p. 269-278.
Strojek and Wagner. The use of transgenic animal techniques for livestock improvement. 1988. Genetic Engineering: Principles and Methods vol. 10, Plenum Press, p. 221-246.
Kitamoto et al., Abnormal isoform of prion protein accumulates in follicular dendritic cells in mice with Creutzfeldt-Jacob disease. 1991, Journal of Virology, vol. 65, p. 6292-6295.
Race et al., Journal of Virology, Jan. 2000, vol. 74, p. 828-833.
T. Muramoto et al., “Accumulation of Abnormal Prion Protein in Mice Infected with Creutzfeldt-Jakob Disease via Intraperitoneal Route: A Sequential Study,”Am. J. Pathology, 143(5): 1470-79 (1993).
M.E. Bruce et al., “Follicular Dendritic Cells in TSE Pathogenesis,”Immunology Today, 21(9): 442-446 (2000).
T. Muramoto et al., “Species Barrier Prevents an Abnormal Isoform of Prion Protein from Accumulating in Follicular Dendritic Cells of Mice with Creutzfeldt-Jakob Disease,”J. Virology, 67(11): 6808-10 (1993).
T. Kitamoto et al., “Humanized Prion Protein Knock-in by Cre-Induced Site-Specific Recombination in the Mouse,”Biomed. Biophys. Res. Comm., 222: 742-7 (1996).
T. Muramoto et al., “Species Barrier Prevents an Abnormal Isoform of Prion Protein from Accumulating in Follicular Dendritic Cells of Mice with Creutzfeldt-Jakob Disease,”Journal of Virology, 67(11): 6808-6810 (1993).
G.C. Telling et al., “Transmission of Creutzfeldt-Jakob Disease from Humans to Transgenic Mice Expressing Chimeric Human-Mouse Prion Protein,”Proc. Natl. Acad. Sci. USA, 91:9936-9940 (1994).
G.C. Telling et al., “Prion Propagation in Mice Expressing Human and Chimeric PrP Transgenes Implicates the Interaction of Cellular PrP with Another Protein,”Cell, 83:79-90 (1995).
J. Collinge et al., “Unaltered Susceptibility to BSE in Transgenic Mice Expressing Human Prion Protein,”Nature, 378:779-783 (1995).
A.F. Hill et al., “The Same Prion Strain Causes vCJD and BSE,”Nature, 389:448-450 (1997).
E.A. Asante et al., BSE Prions Propagate as Either Variant CJD-like or Sporadic CJD-like Prion Strains in Transgenic Mice Expressing Human Prion Protein,The EMBO Journal, 21(23):6358-6366 (2002).
C.I. Lasmézas et al., “Transmission of the BSE Agent to Mice in the Absence of Detectable Abnormal Prion Protein,”Science, 275:402-404 (1997).
K. Nakamura, “Studies Regarding Technical Developments for Clarification of Mechanism of Abnormal Expression of Brain Functions due to Exogenous Factors (Phase II: years 1995 to 1997), Reports on the Study Results,” pp. 221-228 (Mar. 1999). English-language translation attached.
Mohri, S. et al., “Detection of Prion Accumulation in FDCs of NZW/Sea and I/LnJ Mice”, Annual Report of the Slow Virus Infection Research Committee; The Ministry of Health and Welfare of Japan 1997, Koseisho Tokutei Shikkan Chihatsusei Virus Kansen Chosa Kenkyuhan Heisei 8 nendo (1996) Kenyku Hokokusho Heisei 9 nen, pp. 37-42, (1997).
Nakamura, K. et al., “Humanized Gene Expression in Mice by Using Universal Gene Replacement”, Department of DNA Biology and Embryo Engineering, The Institute of Medical Science, The University of Tokyo, and Department of Neurological Science, Tohoku University School of Medicine, Koseisho Tokutei Shikkan Chihatsusei Virus Kansen Chosa Kenkyuhan Heisei 8 nendo (1996) Kenyku Hokokusho Heisei 9 nen, pp. 25-28 (1997).
Extended European Search Report mailed Jun. 3, 2008, for European Patent Application No. 08000541.6 (4 pages).
Telling, “Prion protein genes and prion diseases: studies in transgenic mice,” Neuropathology and Applied Neurobiology, 26: 209-220 (2000).

Affiliated with

Also associated with

Rating

Method of screening prion disease infection factor does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Method of screening prion disease infection factor, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method of screening prion disease infection factor will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4038415