Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein

Journal of Molecular Biology

Volumn 289, Issue 5, 1999, Pages 1163-1178

  Wopfner, Franziska ^a   Weidenhöfer, Georg ^a   Schneider, Ralf ^b   Von Brunn, Albrecht ^a   Gilch, Sabine ^a   Schwarz, Tino F ^c   Werner, Thomas ^b   Schätzl, Hermann M ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b INSTITUTE OF EPIDEMIOLOGY   (Germany)

^c UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

Non mammalian prion proteins; Prion disease; Prion protein genes; Species barrier; Structure function relationships

Indexed keywords

PRION PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARNIVORE; DEGENERATIVE DISEASE; FOWL; GENETIC CONSERVATION; MAMMAL; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN TERTIARY STRUCTURE; RODENT; SEQUENCE HOMOLOGY; UNGULATE;

ANIMALIA; AVES; GALLIFORMES; MAMMALIA; RODENTIA; UNGULATA; VERTEBRATA;

EID: 0344326239     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2831     Document Type: Article

References (61)

1. Bartz L. C., McKenzie D. I., Bessen R. A., Marsh R. F., Aiken J. M. Transmissible mink encephalopathy species barrier effects between ferret and mink: PrP gene and protein analysis. J. Gen. Virol. 75:1994;2947-2953.
2. Billeter M., Riek R., Wider G., Hornemann S., Glockshuber R., Wüthrich K. Prion protein NMR structure and species barrier for prion diseases. Proc. Natl Acad. Sci. USA. 94:1997;7281-7285.
3. Borchelt D. R., Scott M., Taraboulos A., Stahl N., Prusiner S. B. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J. Cell Biol. 110:1990;743-752.
4. Borchelt D. R., Taraboulos A., Prusiner S. B. Evidence of synthesis of scrapie prions proteins in the endocytic pathway. J. Biol. Chem. 267:1992;16188-16199.
5. Brown D., Qin K., Herms J. W., Madlung A., Manson J., Strome R., Fraser P. E., Kruck T., von Bohlen A., Schulz-Schaeffer W., Giese A., Westaway D., Kretzschmar H. The cellular prion protein binds copper in vivo. Nature. 390:1997;684-697.
6. Bruce M. E., Will R. G., Ironside J. W., McConnell I., Drummond D., Suttie A., McCardle L., Chree A., Hope J., Birkett C., Cousens S., Fraser H., Bostock C. J. Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature. 389:1997;498-501.
7. Bueler H., Fischer M., Lang Y., Bluethmann H., Lipp H. P., DeArmond S. J., Prusiner S. B., Aguet M., Weissmann C. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature. 356:1992;577-582.
8. Cohen F. E., Pan K.-M., Huang Z., Baldwin M., Fletterick R. J., Prusiner S. B. Structural clues to prion replication. Science. 264:1994;530-531.
9. Donne D. G., Viles J. H., Groth D., Mehlhorn I., James T. L., Cohen F. E., Prusiner S. B., Wright P. E., Dyson H. J. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N-terminus is highly flexible. Proc. Natl Acad. Sci. USA. 94:1997;13452-13456.
10. Estibeiro J. P. Multiple roles for PrP in the prion diseases. Trends Neurosci. Sci. 19:1996;257-259.
11. Faddis B. T., McGinn M. D. Glial populations in the juvenile and adult Mongolian gerbil: relationship to spongiform degeneration of the ventral cochlear nucleus. Exp. Neurol. 120:1993;160-169.
12. Fischer M., Rulicke T., Raeber A., Sailer A., Moser M., Oesch B., Brandner S., Aguzzi A., Weissmann C. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 15:1996;1255-1264.
13. Gabriel J.-M., Oesch B., Kretzschmar H., Scott M., Prusiner S. B. Molecular cloning of a candidate chicken prion protein. Proc. Natl Acad. Sci. USA. 89:1992;9097-9101.
14. Gasset M., Baldwin M. A., Lloyd D., Gabriel J.-M., Holtzman D. M., Cohen F., Fletterick R., Prusiner S. B. Predicted α-helical regions of the prion protein when synthesized as peptides form amyloid. Proc. Natl Acad. Sci. USA. 89:1992;10940-10944.
15. Gibbs C. J., Bolis C. L. Normal isoform of amyloid protein (PrP) in brains of spawning salmon. Mol. Psychiat. 2:1997;146-147.
16. Guiroy D. C., Williams E. S., Yanagihara R., Gajdusek D. C. Immunolocalization of scrapie amyloid (PrP27-30) in chronic wasting disease of Rocky Mountain elk and hybrids of captive mule deer and white-tailed deer. Neurosci. Letters. 126:1991;195-198.
17. Harris D. A., Falls D. L., Johnson F. A., Fischbach G. D. A prion-like protein from chicken brain copurifies with an acetylcholine receptor- inducing activity. Proc. Natl Acad. Sci. USA. 88:1991;7664-7668.
18. Herrmann G., Schön A., Brack-Werner R., Werner T. CONRAD: a method for identification of variable and conserved regions within proteins by scale-space filtering. CABIOS. 12:1996;197-203.
19. Hill A. F., Desbruslais M., Joiner S., Sidle K. C. L., Gowland I., Collinge J., Doey L. J., Lantos P. The same prion strain causes vCJD and BSE. Nature. 289:1997;448-450.
20. Hornshaw M. P., McDermott J. R., Candy J. M. Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem. Biophys. Res. Commun. 207:1995;621-629.
21. Huang Z., Gabriel J.-M., Baldwin M. A., Fletterick R. J., Prusiner S. B., Cohen F. E. Proposed three-dimensional structure for the cellular prion protein. Proc. Natl Acad. Sci. USA. 91:1994;7139-7143.
22. Huang Z., Prusiner S. B., Cohen F. E. Scrapie prions: a three-dimensional model of an infectious fragment. Fold. Des. 1:1995;13-19.
23. James T. L., Liu H., Ulyanov N. B., Farr-Lones S., Zhang H., Donne D. G., Kaneko K., Groth D., Mehlhorn I., Prusiner S. B., Cohen F. E. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl Acad. Sci. USA. 94:1997;10086-10091.
24. Kaneko K., Zulianello L., Scott M., Cooper C. M., Wallace A. C., James T. L., Cohen F. E., Prusiner S. B. Evidence for protein X binding to a discontinous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl Acad. Sci. USA. 94:1997;10069-10074.
25. Kirkwood J. K., Cunningham A. A. Epidemiological observations on spongiform encephalopathies in captive wild animals in the British Isles. Vet. Records. 135:1994;296-303.
26. Kitamoto T., Tateishi J. Human prion diseases with variant prion protein. Phil. Trans. Roy. Soc. ser. B. 343:1994;391-398.
27. Krakauer D. C., Pagel M., Southwood T. R. E., Zanotto de P. M. A. Phylogenesis of prion protein. Nature. 380:1996;675.
28. Krakauer D. C., Zanotto de P. M. A., Pagel M. Prion's progress: patterns and rates of molecular evolution in relation to spongiform disease. J. Mol. Evol. 47:1998;133-145.
29. Kretzschmar H. A., Neumann M., Riethmüller G., Prusiner S. B. Molecular cloning of a mink prion protein gene. J. Gen. Virol. 73:1992;2757-2761.
30. Lowenstein D. H., Butler D. A., Westaway D., McKinley M. P., DeArmond S. J., Prusiner S. B. Three hamster species with different scrapie incubation times and neuropathological features encode distinct prion proteins. Mol. Cell. Biol. 10:1990;1153-1163.
31. Lück R., Steger G., Riesner D. Thermodynamic prediction of conserved secondary structure: application to the RRE element of HIV, the tRNA element of CMV and the mRNA of prion protein. J. Mol. Biol. 258:1996;813-826.
32. Mastrianni J. A., Iannicola C., Myers R. M., DeArmond S., Prusiner S. B. Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease. Neurology. 47:1996;1305-1312.
33. Miura T., Hori-i A., Takeuchi H. Metal-dependent α-helix formation promoted by the glycine-rich octapeptide region of the prion protein. FEBS Letters. 396:1996;248-252.
34. Oesch B., Westaway D., Walchli M., McKinley M. P., Kent S. B., Aebersold R., Barry R. A., Rempst P., Teplow D. B., Hood L. E., Prusiner S. B., Weissmann C. A cellular gene encodes scrapie PrP 27-30 protein. Cell. 40:1985;735-746.
35. Owen F., Poulter M., Lofthouse R., Collinge J., Crow T. J., Risby D., Baker H. F., Ridley R. M., Hsiao K., Prusiner S. B. Insertion in prion protein gene in familial Creutzfeldt-Jakob disease. Lancet. i:1989;51-52.
36. Palmer M. S., Collinge J. Mutations and polymorphisms in the prion protein gene. Hum. Mutat. 2:1993;168-173.
37. Pan K.-M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D., Mehlhorn I., Huang Z., Fletterick R. J., Cohen F. E., Prusiner S. B. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA. 90:1993;10962-10966.
38. Pattison I. H. Experiments with scrapie with special reference to the nature of the agent and the pathology of the disease. Gajdusek D. C., Gibbs C. J. Jr, Alpers M. P. Slow, Latent and Temperate Virus Infections, NINDB Monograph 2. 1965;249-257 US Government Printing, Washington.
39. Poidinger M., Kirkwood J., Almond W. Sequence analysis of the prion protein from two species of antelope susceptible to transmissible spongiform encephalopathy. Arch. Virol. 131:1993;193-199.
40. Prusiner S. B. Novel proteinaceous infectious particles cause scrapie. Science. 216:1982;136-144.
41. Prusiner S. B. Molecular biology of prion diseases. Science. 252:1991;1515-1522.
42. Prusiner S. B. Prion diseases and the BSE crisis. Science. 278:1997;245-251.
43. Prusiner S. B., Fuzi M., Scott M., Serban D., Serban H., Taraboulos A., Gabriel J.-M., Wells G., Wilesmith J., Bradley R., DeArmond S. J., Kristensson K. Immunologic and molecular biologic studies of the prion proteins in bovine spongiform encephalopathy. J. Infect. Dis. 167:1993;602-613.
44. Riek R., Hornemann S., Wider G., Billeter M., Glockshuber R., Wüthrich K. NMR structure of the mouse prion protein domain PrP(121-231). Nature. 382:1996;180-182.
45. Riek R., Hornemann S., Wider G., Glockshuber R., Wüthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Letters. 413:1997;282-288.
46. Rogers M., Yehiely F., Scott M., Prusiner S. B. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultered cells. Proc. Natl Acad. Sci. USA. 90:1993;3182-3186.
47. Rother K. I., Clay O. K., Bourquin J.-P., Silke J., Schaffner W. Long non-stop reading frames on the antisense strand of heat shock protein 70 genes and prion protein (PrP) genes are conserved between species. Biol. Chem. 378:1997;1521-1530.
48. Schätzl H., DaCosta M., Taylor L., Cohen F., Prusiner S. B. Prion protein gene variation among primates. J. Mol. Biol. 245:1995;362-374.
49. Schätzl H., Wopfner F., Gilch S., von Brunn A., Jäger G. Why is the codon 129 of PrP polymorphic in humans but not in animals? Lancet. 349:1997;1603-1604.
50. Scott M., Foster D., Mirenda C., Serban D., Coufal F., Wälchi M., Torchia M., Groth D., Carlson G., DeArmond S., Westaway D., Prusiner S. B. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell. 59:1989;847-857.
51. Scott M., Groth D., Foster D., Torchia M., Yang S.-L., DeArmond S. J., Prusiner S. B. Propagation of prion with artifical properties in transgenic mice expressing chimeric PrP genes. Cell. 73:1993;979-988.
52. Scott M. R., Safar J., Telling G., Ngugen O., Groth D., Torchia M., Koehler R., Tremblay P., Walther D., Cohen F. E., DeArmond S. J., Prusiner S. B. Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice. Proc. Natl Acad. Sci. USA. 94:1997;14279-14284.
53. Stahl N., Baldwin M. A., Teplow D. B., Hood L., Gibson B. W., Burlingame A. L., Prusiner S. B. Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry. 32:1993;1991-2002.
54. Taraboulos A., Serban D., Prusiner S. B. Scrapie prion proteins accumulate in the cytoplasm of persistently-infected cultured cells. J. Cell Biol. 110:1990;2117-2132.
55. Telling G. C., Scott M., Foster D., Yang S.-L., Torchia M., Sidle K. C. L., Collinge J., DeArmond S. J., Prusiner S. B. Transmission of CJD from humans to transgenic mice expressing chimeric human-mouse prion proteins. Proc. Natl Acad. Sci. USA. 91:1994;9936-9940.
56. Telling G. C., Scott M., Mastrianni J., Gabizon R., Torchia M., Cohen F. E., DeArmond S. J., Prusiner S. B. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another factor. Cell. 83:1995;79-90.
57. Westaway D., Zuliani V., Cooper C., Da Costa M., Neuman S., Jenny A. L., Detwiler L., Prusiner S. B. Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie. Genes Dev. 8:1994;959-969.
58. Wickner R. B. (URE3) as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science. 264:1994;566-569.
59. Will R. G., Ironside J. W., Zeidler M., Cousens S. N., Estibeiro K., Alperovitch A., Poser S., Pocchiari M., Hofman A., Smith P. G. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet. 347:1996;921-925.
60. Williams E. S., Young S. Chronic wasting disease of captive mule deer: a spongiform encephalopathy. J. Wildl. Dis. 16:1980;89-98.
61. Windl O., Dempster M., Estibeiro P., Lathe R. A candidate marsupial PrP gene reveals two domains conserved in mammalian PrP proteins. Gene. 159:1995;181-186.