Molecular Cloning of a Candidate Chicken Prion Protein

• Published in: Proceedings of the National Academy of Sciences - PNAS 1992-10, Vol.89 (19), p.9097-9101
• Main Authors: Gabriel, Jean-Marc, Oesch, Bruno, Kretzschmar, Hans, Scott, Michael, Prusiner, Stanley B.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Animals; Base Sequence; Biological and medical sciences; Blotting, Southern; brain; cDNA; Chickens; Cloning, Molecular - methods; degeneration; DNA; DNA - genetics; DNA - isolation & purification; DNA probes; Fundamental and applied biological sciences. Psychology; genes; Genes. Genome; Genetics; Genomic Library; Genomics; Humans; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Molecules; nucleotide sequence; Nucleotides; Oligonucleotide Probes; Open Reading Frames; Phylogeny; Poultry; predictions; prion protein; Prions - genetics; Proteins; Sequence Homology, Amino Acid; Ungulates
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.89.19.9097

Fractions enriched for acetylcholine receptor-inducing activity from chicken brain were found to contain a protein that was ≈30% homologous with mammalian prion proteins [Harris, D. A., Falls, D. L., Johnson, F. A. \& Fischbach, G. D. (1991) Proc. Natl. Acad. Sci. USA 88, 7664-7668]. To extend these observations, we recovered genomic clones encoding a putative chicken prion protein (PrP). Like mammalian PrP molecules, the candidate chicken PrP is encoded by a single-copy gene and the entire open reading frame is found within a single exon. All of the structural features of mammalian PrP were found in the chicken protein. When the N-terminal repeats of PrP were not considered, the chicken and mammalian proteins were ≈55% homologous, allowing for conservative substitutions. Screening of a chicken genomic DNA library failed to identify a more closely related chicken PrP homologue. These findings argue that the protein which purifies with acetylcholine receptor-inducing activity is chicken PrP.