PrP<sup>Sc</sup>-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains
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- Eri Saijo
- Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA
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- Andrew G. Hughson
- Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA
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- Gregory J. Raymond
- Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA
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- Akio Suzuki
- Laboratory of Veterinary Hygiene, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Japan
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- Motohiro Horiuchi
- Laboratory of Veterinary Hygiene, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Japan
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- Byron Caughey
- Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA
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- K. L. Beemon
- editor
説明
<jats:title>ABSTRACT</jats:title><jats:p>Understanding the structure of PrP<jats:sup>Sc</jats:sup>and its strain variation has been one of the major challenges in prion disease biology. To study the strain-dependent conformations of PrP<jats:sup>Sc</jats:sup>, we purified proteinase-resistant PrP<jats:sup>Sc</jats:sup>(PrP<jats:sup>RES</jats:sup>) from mouse brains with three different murine-adapted scrapie strains (Chandler, 22L, and Me7) and systematically tested the accessibility of epitopes of a wide range of anti-PrP and anti-PrP<jats:sup>Sc</jats:sup>specific antibodies by indirect enzyme-linked immunosorbent assay (ELISA). We found that epitopes of most anti-PrP antibodies were hidden in the folded structure of PrP<jats:sup>RES</jats:sup>, even though these epitopes are revealed with guanidine denaturation. However, reactivities to a PrP<jats:sup>Sc</jats:sup>-specific conformational C-terminal antibody showed significant differences among the three different prion strains. Our results provide evidence for strain-dependent conformational variation near the C termini of molecules within PrP<jats:sup>Sc</jats:sup>multimers.</jats:p><jats:p><jats:bold>IMPORTANCE</jats:bold>It has long been apparent that prion strains can have different conformations near the N terminus of the PrP<jats:sup>Sc</jats:sup>protease-resistant core. Here, we show that a C-terminal conformational PrP<jats:sup>Sc</jats:sup>-specific antibody reacts differently to three murine-adapted scrapie strains. These results suggest, in turn, that conformational differences in the C terminus of PrP<jats:sup>Sc</jats:sup>also contribute to the phenotypic distinction between prion strains.</jats:p>
収録刊行物
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- Journal of Virology
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Journal of Virology 90 (10), 4905-4913, 2016-05-15
American Society for Microbiology