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ABSTRACT: It has been reported that macrophages degrade infectious forms of prion protein (PrP(Sc) ). In order to investigate the mechanisms underlying PrP(Sc) degradation in macrophages, the effects of lysosomal and proteasomal inhibitors on macrophage cell lines which were incubated with scrapie-affected brain homogenate were studied. PrP(Sc) degradation was inhibited in the presence of both proteasomal and lysosomal inhibitors. Indirect fluorescence assays to determine the cellular localization of PrP(Sc) were undertaken. PrP(Sc) colocalized with the lysosomal membrane protein Lamp-1 and ubiquitin, a protein that is related to the proteasome. The present data indicate that macrophages might degrade PrP(Sc) via the lysosomal and proteasomal pathways.
Microbiology and Immunology 12/2010; 54(12):763-8. · 1.30 Impact Factor
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ABSTRACT: Feline parvoviruses were isolated from frozen samples of intestines taken from a snow leopard (Uncia uncia) and a serval (Leptailurus serval) that died successively at Sapporo Maruyama Zoo in Hokkaido, Japan. Isolates possessed an antigenic epitope for both the feline panleukopenia virus (FPLV) and mink enteritis virus, identified with a hemagglutination inhibition test. Sequencing analyses of the VP2 region of the isolates revealed that the two isolates were identical and of the FPLV-type. These results suggested that FPLV was introduced from a feral cat which entered the zoo and transmitted the virus inside the zoo.
Journal of Veterinary Medical Science 11/2010; 73(4):491-4. · 0.85 Impact Factor
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ABSTRACT: The causative agent of prion diseases is the pathological isoform (PrPSc) of the host-encoded cellular prion protein (PrPC). PrPSc has an identical amino acid sequence to PrPC; thus, it has been assumed that an immune response against PrPSc could not be found in prion-affected animals. In this study, we found the anti-prion protein (PrP) antibody at the terminal stage of mouse scrapie. Several sera from mice in the terminal stage of scrapie reacted to the recombinant mouse PrP (rMPrP) molecules and brain homogenates of mouse prion diseases. These results indicate that mouse could recognize PrPC or PrPSc as antigens by the host immune system. Furthermore, immunization with rMPrP generates high titers of anti-PrP antibodies in wild-type mice. Some anti-PrP antibodies immunized with rMPrP prevent PrPSc replication in vitro. The mouse sera from terminal prion disease have several wide epitopes, although mouse sera immunized with rMPrP possess narrow epitopes.
Cellular Immunology 04/2010; 263(2):212-8. · 1.97 Impact Factor
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ABSTRACT: Transmissible spongiform encephalopathies (TSEs), such as bovine spongiform encephalopathy (BSE) and scrapie, display long incubation periods before PrP(Sc) accumulates in the central neuronal system (CNS). The precise role that phagocytic cells, such as macrophages, play in prion pathogenesis is uncertain. In this study, the involvement of bovine macrophages at the early stage of prion infection was studied. Brain homogenates of mouse scrapie and BSE were degraded sequentially in the bovine macrophage cell line, Bo120, and freshly prepared in monocyte-derived macrophages from peripheral blood. Mouse scrapie brain homogenates degraded in Bo120 cells were inoculated intraperitoneally to C57BL mice, showing that the degree of cellular degradation (2h, 10, 28, and 36d) correlated with survival periods (288, 303, 324, and 340d, respectively). Partial colocalizations of PrP and lysosomes were observed in Bo120 cells by confocal microscopy. These results suggest that bovine macrophages have the ability to take up and degrade PrP(Sc), resulting in decreased TSE infectivity in mice.
Veterinary Immunology and Immunopathology 08/2009; 133(1):33-9. · 2.08 Impact Factor
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ABSTRACT: We obtained seven monoclonal antibodies (mAbs) against chicken cellular prion protein (ChPrP(C)) by immunizing BALB/c mice with recombinant prion protein (rChPrP). Of the seven mAbs, two mAbs (6 and 26) could recognize rChPrP, but not ChPrP(C), in chicken brain lysate via Western blot (WB) analysis. Three C-terminal linear epitopes (AAANQTEVEM, RWWS and SPVPQD) were identified in ChPrP amino acids by pepspot analysis with five mAbs. The mAbs recognizing the C-terminal epitopes in ChPrP(C) predominantly reacted with the N-terminal truncated ChPrP(C) in WB analysis, which differed from the reaction with N-terminal proline/glycine-rich repeats recognizing rabbit polyclonal antibody. These mAbs will soon be available as a useful tool to characterize the biology of ChPrP(C) in birds.
Veterinary Immunology and Immunopathology 12/2008; 128(4):402-6. · 2.08 Impact Factor
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ABSTRACT: The virus neutralization (VN) antibody titers of serum samples from 18 individuals representing 8 carnivore species vaccinated with commercial polyvalent vaccines optimized for domestic cats containing inactivated feline panleukopenia virus (FPLV) were evaluated against canine parvovirus type 2 (CPV2). In addition, the titers among 5 individuals from 4 carnivore were evaluated against antigenic variants of feline parvoviruses; FPLV, CPV2, CPV2a, CPV2b, CPV2c, mink enteritis virus type 1 (MEV1) and MEV2. The polyvalent vaccines induced cross-reactive VN titers against antigenic variants of feline parvoviruses in nondomestic felids. However, we observed very low cross-reactive VN antibody in lions and Siberian tigers, therefore we should pay attention to CPV infections in these animals even if they were vaccinated with inactivated FPLV vaccines.
Journal of Veterinary Medical Science 12/2006; 68(11):1195-8. · 0.85 Impact Factor
