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Journal of Virology, February 2001, p. 1408-1413, Vol. 75, No. 3
Institute for Neurodegenerative
Diseases1 and Departments of
Neurology,2
Medicine,3 Pharmaceutical
Chemistry,4 Biochemistry and
Biophysics,5 and
Pathology,6 University of California,
San Francisco, California 94143
Received 8 August 2000/Accepted 23 October 2000
A series of prion transmission experiments was performed in
transgenic (Tg) mice expressing either wild-type, chimeric, or truncated prion protein (PrP) molecules. Following inoculation with
Rocky Mountain Laboratory (RML) murine prions, scrapie incubation times
for Tg(MoPrP)4053, Tg(MHM2)294/Prnp0/0, and
Tg(MoPrP,
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.3.1408-1413.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Identification of Two Prion Protein Regions That
Modify Scrapie Incubation Time


23-88)9949/Prnp0/0 mice were ~50, 120, and
160 days, respectively. Similar scrapie incubation times were obtained
after inoculation of these lines of Tg mice with either MHM2(MHM2(RML))
or MoPrP(
23-88)(RML) prions, excluding the possibility that
sequence-dependent transmission barriers could account for the observed
differences. Tg(MHM2)294/Prnp0/0 mice displayed prolonged
scrapie incubation times with four different strains of murine prions.
These data provide evidence that the N terminus of MoPrP and the
chimeric region of MHM2 PrP (residues 108 through 111) both influence
the inherent efficiency of prion propagation.
*
Corresponding author. Mailing address: Institute for
Neurodegenerative Diseases, Box 0518, University of California, San
Francisco, CA 94143-0518. Phone: (415) 476-4482. Fax: (415) 476-8386.
Present address: Department of Neurological Science, Tohoku
University School of Medicine, Aoba-ku, Sendai, Japan 980-8575.
Present address: Montclair Group, Tal Biosciences, Alameda, CA 94501.
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