Heterogeneity of Abnormal Prion Protein (PrPSc) in Murine Scrapie Prions Determined by PrPSc-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 strain. Conformation-specific probes, like these mAbs, have the potential to be powerful tools for investigating conformational variations in PrPSc.
公益社団法人日本獣医学会の論文