Molecular basis of barriers for interspecies transmissibility of mammalian prions

Molecular Cell

Volumn 14, Issue 1, 2004, Pages 139-145

  Vanik, David L ^a   Surewicz, Krystyna A ^a   Surewicz, Witold K ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; RECOMBINANT PROTEIN; VIRUS PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BRAIN SPONGIOSIS; GENETIC VARIABILITY; IN VITRO STUDY; INTERSPECIFIC RELATIONSHIP; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN VARIANT; SPECIES DIFFERENCE; STRAIN DIFFERENCE; VIRUS INHIBITION; VIRUS RECOMBINANT; VIRUS TRANSMISSION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMYLOID; ANIMALS; ANIMALS, GENETICALLY MODIFIED; CATTLE; DISEASE TRANSMISSION; FLUORESCENT DYES; HUMANS; MOLECULAR SEQUENCE DATA; PRION DISEASES; PRIONS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SPECIES SPECIFICITY; THIAZOLES;

ANIMALIA; MAMMALIA; MAMMALIAN PRIONS;

EID: 1842766124     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00155-8     Document Type: Article

References (35)

1. Baskakov I.V. Autocatalytic conversion of recombinant prion protein displays a species barrier. J. Biol. Chem. 279:2003;7671-7677.
2. Bessen R.A., Marsh R.F. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68:1994;7859-7868.
3. Bessen R.A., Kocisko D.A., Raymond G.J., Nandan S., Lansbury P.T., Caughey B. Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature. 375:1995;698-700.
4. Bruce M.E., Fraser H. Scrapie strain variation and its implications. Curr. Top. Microbiol. Immunol. 172:1991;125-138.
5. Bruce M.E., Will R.G., Ironside J.W., McConnell I., Drummond D., Suttie A., McCardie L., Chree A., Hope J., Birkett C.et al. Transmissions to mice indicate that "new variant" CJD is caused by the BSE agent. Nature. 389:1997;498-501.
6. Caughey B. Interactions between prion protein isoforms. the kiss of death Trends Biochem. Sci. 26:2001;235-242.
7. Caughey B., Chesebro B. Transmissible spongiform encephalopathies and prion protein interconversions. Adv. Virus Res. 56:2001;277-311.
8. Chien P., Weissman J.S. Conformational diversity in a yeast prion dictates its seeding specificity. Nature. 410:2001;223-227.
9. Chien P., DePace A.H., Collins S.R., Weissman J.S. Generation of prion transmission barriers by mutational control of amyloid conformations. Nature. 424:2003;948-951.
10. Collinge J. Prion diseases of humans and animals. their causes and molecular basis Annu. Rev. Neurosci. 24:2001;519-550.
11. Come J.H., Fraser P.E., Lansbury P.T. Jr. A kinetic model for amyloid formation in the prion disease. importance of seeding Proc. Natl. Acad. Sci. USA. 90:1993;5959-5963.
12. Derkatch I.L., Chernoff Y.O., Kushnirov V.V., Inge-Vechtomov S.G., Liebman S.W. Genetics. 144:1996;1375-1386.
13. Goldmann W., Martin T., Foster J., Hughes S., Smith G., Hughes K., Dawson M., Hunter N. Novel polymorphisms in the caprine PrP gene. a codon 142 mutation associated with scrapie incubation period J. Gen. Virol. 77:1996;2885-2891.
14. Hill A.F., Desbruslais M., Joiner S., Sidle K.C.L., Gowland I., Collinge J. The same prion strain causes vCJD and BSE. Nature. 389:1997;448-450.
15. Kimberlin R.H., Walker C.A. Evidence for the transmission of one source of scrapie agent to hamster involves separation of agent strains from a mixture. J. Gen. Virol. 39:1978;487-496.
16. Kocisko D.A., Priola S.A., Raymond G.J., Chesebro B., Lansbury P.T. Jr., Caughey B. Species specificity in the cell-free conversion of prion protein to protease-resistant forms. a model for the scrapie species barrier Proc. Natl. Acad. Sci. USA. 92:1995;3923-3927.
17. Kong Q., Surewicz W.K., Petersen R.B., Zou W., Chen S.G., Gambetti P., Parchi P., Capellari S., Goldfarb L., Montagna P.et al. Inherited prion diseases. Second Edition S.B., Prusiner Prion Biology and Diseases. 2004;673-775 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
18. Kundu B., Maiti N.R., Jones E.M., Surewicz K.A., Vanik D.L., Surewicz W.K. Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein. structural clues for prion propagation Proc. Natl. Acad. Sci. USA. 100:2003;12069-12074.
19. Lee S., Eisenberg D. Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process. Nat. Struct. Biol. 10:2003;725-730.
20. Lucassen R., Nishina K., Supattapone S. In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups. Biochemistry. 42:2003;4127-4135.
21. Morillas M., Swietnicki W., Gambetti P., Surewicz W.K. Membrane environment alters the conformational structure of the recombinant human prion protein. J. Biol. Chem. 274:1999;36859-36865.
22. Naiki H., Higuchi K., Hosokawa M., Takeda T. Fluorimetric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal. Biochem. 177:1989;244-249.
23. Parchi P., Zou W., Wang W., Brown P., Capellari S., Ghetti B., Kopp N., Schultz-Schaeffer W.J., Kretzschmar H.A., Head M.W.et al. Genetic influence on the structural variations of the abnormal prion protein. Proc. Natl. Acad. Sci. USA. 97:2000;10168-10172.
24. Peretz D., Williamson R.A., Lagname G., Matsunaga Y., Vergara J., Burton D.R., DeArmond S.J., Prusiner S.B., Scott M.R. A change in the conformation of prions accompanies the emergence of a new prion strain. Neuron. 34:2002;921-932.
25. Priola S.A., Chesebro B. A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells. J. Virol. 69:1995;7754-7758.
26. Priola S.A., Chabry J., Chan K. Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155. J. Virol. 75:2001;4673-4680.
27. Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science. 216:1982;136-144.
28. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA. 95:1998;13363-13383.
29. Raymond G.J., Hope J., Kocisko D.A., Priola S.A., Raymond L.D., Bossers A., Ironside J., Will R.G., Chen S.G., Petersen R.B.et al. Molecular assessment of the potential transmissibilities of BSE and scrapie to humans. Nature. 388:1997;285-288.
30. Sc molecules with different conformations. Nat. Med. 4:1998;1157-1165.
31. Scott M., Groth D., Foster D., Torchia M., Yang S.L., DeArmond S.J., Prusiner S.B. Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell. 73:1993;979-988.
32. Tateishi J., Kitamoto T., Hoque M.Z., Furukawa H. Experimental transmission of Creutzfeldt-Jakob disease and related diseases to rodents. Neurology. 46:1996;532-537.
33. Telling G.C., Parchi P., DeArmond S.J., Cortelli P., Montagna P., Gabizon R., Mastrianni J., Lugaresi E., Gambetti P., Prusiner S.B. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science. 274:1996;2079-2082.
34. Uptain S.M., Lindquist S. Prions as protein-based genetic elements. Annu. Rev. Microbiol. 56:2002;703-741.
35. Wickner R.B., Taylor K.L., Edskes H.K., Maddelein M.L., Moriyama H., Roberts B.T. Prions of yeast as heritable amyloidoses. J. Struct. Biol. 130:2000;310-322.