Detection of PrP(Sc) in peripheral tissues of clinically affected cattle after oral challenge with bovine spongiform encephalopathy.
Bovine spongiform encephalopathy (BSE) is a fatal neurodegenerative prion disease that mainly affects cattle. Transmission of BSE to humans caused a variant form of Creutzfeldt-Jakob disease. Following infection, the protease-resistant, disease-associated isoform of prion protein (PrP(Sc)) accumulates in the central nervous system and in other tissues. Many countries have defined bovine tissues that may contain prions as specified risk materials, which must not enter the human or animal food chains and therefore must be discarded. Ultrasensitive techniques such as protein misfolding cyclic amplification (PMCA) have been developed to detect PrP(Sc) when present in minuscule amounts that are not readily detected by other diagnostic methods such as immunohistochemistry or Western blotting. This study was conducted to determine when and where PrP(Sc) can be found by PMCA in cattle orally challenged with BSE. A total of 48 different tissue samples from four cattle infected orally with BSE at various clinical stages of disease were examined using a standardized PMCA protocol. The protocol used brain homogenate from bovine PrP transgenic mice (Tgbov XV) as substrate and three consecutive rounds of PMCA. Using this protocol, PrP(Sc) was found in the brain, spinal cord, nerve ganglia, optic nerve and Peyer's patches. The presence of PrP(Sc) was confirmed in adrenal glands, as well as in mesenteric lymph nodes - a finding that was reported recently by another group. Interestingly, additional positive results were obtained for the first time in the oesophagus, abomasum, rumen and rectum of clinically affected cattle.
Institute for Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, Südufer 10, 17493 Greifswald-Insel Riems, Germany.
Martin
M
Franz
Institute for Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, Südufer 10, 17493 Greifswald-Insel Riems, Germany.
Martin
M
Eiden
Institute for Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, Südufer 10, 17493 Greifswald-Insel Riems, Germany.
Anne
A
Balkema-Buschmann
Virus and Prion Research Unit, National Animal Disease Center, ARS, USDA, PO BOX 70 Ames, IA 50010, USA.
Justin
J
Greenlee
Department of Veterinary Sciences and Molecular Biology, University of Wyoming, MICRO/Molecular Biology, 1000 E. University Avenue Laramie, Wyoming, WY 82071, USA.
Hermann
H
Schatzl
Institute for Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, Südufer 10, 17493 Greifswald-Insel Riems, Germany.
Christine
C
Fast
Kansas State University, College of Veterinary Medicine, K224B Mosier Hall, Manhattan, KS 66506, USA.
Jürgen
J
Richt
Ernst-Moritz-Arndt University, Zoological Institute, Animal Physiology and Biochemistry, Biotechnikum, Walther-Rathenau-Strasse 49a, 17489 Greifswald, Germany.
Jan-Peter
JP
Hildebrandt
Institute for Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, Südufer 10, 17493 Greifswald-Insel Riems, Germany.
Martin H
MH
Groschup
D000284:Administration, Oral; D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D016643:Encephalopathy, Bovine Spongiform / Q000175:diagnosis / Q000635:transmission*; D020387:Food Chain; D005506:Food Contamination; D006801:Humans; D051379:Mice; D008822:Mice, Transgenic; D018620:PrPSc Proteins / Q000302:isolation & purification* / Q000472:pathogenicity; D013116:Spinal Cord / Q000737:chemistry; D014018:Tissue Distribution
D018620:PrPSc Proteins