Prion protein gene variation among primates

Schätzl, Hermann; Costa, Maria da Conceição Nascimento; Taylor, Leslie; Cohen, Fred E.; Prusiner, Stanley B.

doi:10.1006/jmbi.1996.0791

Cited by 68 publications

(90 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In mammals, DNA sequences of the ORFs encoding PrP generally exhibit ∼90% similarity. As expected, the degree of similarity at the amino acid level increases to >95% when PrPs of different primates are compared (Schätzl et al 1995) but is much lower when human PrP is compared with that of a marsupial (∼70%) (Windl et al 1995). An even lower degree of homology is found when human PrP is compared with that of the chicken (∼30%) (Harris et al 1989;Gabriel et al 1992).…”

supporting

confidence: 73%

Complete Genomic Sequence and Analysis of the Prion Protein Gene Region from Three Mammalian Species

Lee

Westaway²,

Smit³

et al. 1998

Genome Res.

152

124

View full text Add to dashboard Cite

The prion protein (PrP), first identified in scrapie-infected rodents, is encoded by a single exon of a single-copy chromosomal gene. In addition to the protein-coding exon, PrP genes in mammals contain one or two 5′-noncoding exons. To learn more about the genomic organization of regions surrounding the PrP exons, we sequenced 105 bp of DNA from clones containing human, sheep, and mouse PrP genes isolated in cosmids or λ phage. Our findings are as follows: (1) Although the human PrP transcript does not include the untranslated exon 2 found in its mouse and sheep counterparts, the large intron of the human PrP gene contains an exon 2-like sequence flanked by consensus splice acceptor and donor sites. (2) The mouse Prnpa but not thePrnpb allele found in 44 inbred lines contains a 6593 nucleotide retroviral genome inserted into the anticoding strand of intron 2. This intracisternal A-particle element is flanked by duplications of an AAGGCT nucleotide motif. (3) We found that thePrP gene regions contain from 40% to 57% genome-wide repetitive elements that independently increased the size of the locus in all three species by numerous mutations. The unusually long sheepPrP 3′-untranslated region contains a “fossil” 1.2-kb mariner transposable element. (4) We identified sequences in noncoding DNA that are conserved between the three species and may represent biologically functional sites.[The nucleotide sequence data reported in this paper have been submitted to the GenBank sequence database and have been assigned the accession numbers U29185(human), U29186 (mouse), and U67922 (sheep).]

show abstract

supporting

confidence: 73%

Complete Genomic Sequence and Analysis of the Prion Protein Gene Region from Three Mammalian Species

Lee

Westaway²,

Smit³

et al. 1998

Genome Res.

152

124

View full text Add to dashboard Cite

show abstract

“…Intracerebral inoculation of squirrel monkeys (Saimiri sciureus) demonstrated a positive CWD transmission [49]. Among nonhuman primates, however, the Prnp sequence of the new world monkeys are the most distant from humans [72], and therefore may not indicate that human prion protein conversion would be induced by CWD PrP Sc .…”

Section: Human Susceptibility To Cwdmentioning

confidence: 99%

A prion disease of cervids: Chronic wasting disease

2008

View full text Add to dashboard Cite

-Chronic wasting disease (CWD) is a prion disease of deer, elk, and moose, initially recognized in Colorado mule deer. The discovery of CWD beyond the borders of Colorado and Wyoming, in Canada and as far east as New York, has led to its emergence as a prion disease of international importance. Epidemiological studies indicate that CWD is horizontally transmitted among free-ranging animals, potentially indirectly by prion-containing secreta or excreta contaminating the environment. Experimental CWD transmission attempts to other wild and domestic mammals and to transgenic mice expressing the prion protein of cattle, sheep, and humans have shed light on CWD species barriers. Transgenic mice expressing the cervid prion protein have proven useful for assessing the genetic influences of Prnp polymorphisms on CWD susceptibility. Accumulating evidence of CWD pathogenesis indicates that the misfolded prion protein or prion infectivity seems to be widely disseminated in many nonneural organs and in blood. This review highlights contemporary research findings in this prion disease of free-ranging wildlife.

show abstract

“…However, alignments of human and mammalian PRNP sequences indicate that codons located between residues 90 and 130 influence the transmissibility of prions in mammals, including humans (Schatzl et al, 1995). In addition, some paralogue genes have been described in chicken, amphibians, reptiles and fish (Gabriel et al, 1992;Simonic et al, 2000;Strumbo et al, 2001;Suzuki et al, 2002) 2.…”

Section: Introductionmentioning

confidence: 99%