Heterogeneity of Abnormal Prion Protein (PrP[Sc]) in Murine Scrapie Prions Determined by PrP[Sc]-Specific Monoclonal Antibodies

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  • USHIKI-KAKU Yuko
    Nippi Research Institute of Biomatrix, 520–11 Kuwabara, Toride, Ibaraki 302–0017, Japan
  • SHIMIZU Yoshihisa
    National Institute of Animal Health, 3–1–5 Kannondai, Tsukuba, Ibaraki 305–0856, Japan
  • TABETA Naoko
    National Institute of Animal Health, 3–1–5 Kannondai, Tsukuba, Ibaraki 305–0856, Japan
  • IWAMARU Yoshifumi
    National Institute of Animal Health, 3–1–5 Kannondai, Tsukuba, Ibaraki 305–0856, Japan
  • OGAWA-GOTO Kiyoko
    Nippi Research Institute of Biomatrix, 520–11 Kuwabara, Toride, Ibaraki 302–0017, Japan
  • HATTORI Shunji
    Nippi Research Institute of Biomatrix, 520–11 Kuwabara, Toride, Ibaraki 302–0017, Japan
  • YOKOYAMA Takashi
    National Institute of Animal Health, 3–1–5 Kannondai, Tsukuba, Ibaraki 305–0856, Japan

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  • Heterogeneity of Abnormal Prion Protein (PrP<sup>Sc</sup>) in Murine Scrapie Prions Determined by PrP<sup>Sc</sup>-Specific Monoclonal Antibodies

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In prion diseases, abnormal prion protein (PrPSc) is considered as the main component of the infectious agent. Delineation of PrPSc conformation is expected to be a critical factor in understanding properties of prions. However, practical methods to differentiate between conformers of PrPSc are inadequate. Here, we used two PrPSc-specific monoclonal antibodies (mAbs), 3B7 and 3H6, and found that mAb 3H6 detected a limited portion of PrPSc in five mice-adapted prion strains. The quantity of mAb 3H6-precipitated PrPSc was significantly lesser in 22L compared to other strains. This result provides a direct evidence of the conformational heterogeneity of PrPSc within the prion strains. Conformation-specific probes, like these mAbs, have the potential to be powerful tools for investigating conformational variations in PrPSc.

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