
The major protein, PrP 27-30, in purified preparations of hamster scrapie prions is encoded within the genome of the experimental host. DNA sequences related to a PrP cDNA clone can be detected in a wide variety of organisms under relatively stringent conditions where the only signal generated by hamster or mouse DNA corresponds to the PrP gene. Three hosts for scrapie, goat, sheep and rat gave strong hybridization signals. In addition, three invertebrate DNAs reacted with the PrP probe, in the order nematode-Drosophila much greater than yeast. Thus, the sequences detected in goat, sheep, rat, nematode, Drosophila and possibly yeast DNA may arise from authentic PrP genes. This evolutionary conservation is consistent with the notion that PrP proteins participate in essential cellular processes.
Prions, Nucleic Acid Hybridization, DNA, PrP 27-30 Protein, Mice, Viral Proteins, Genes, Cricetinae, Sequence Homology, Nucleic Acid, Animals, Cloning, Molecular
Prions, Nucleic Acid Hybridization, DNA, PrP 27-30 Protein, Mice, Viral Proteins, Genes, Cricetinae, Sequence Homology, Nucleic Acid, Animals, Cloning, Molecular
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