Switching in amyloid structure within individual fibrils: Implication for strain adaptation, species barrier and strain classification

FEBS Letters

Volumn 583, Issue 16, 2009, Pages 2618-2622

  Baskakov, Ilia V ^a,b  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

^b UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

Amyloid fibril; Conformational switch; Prion protein; Strain adaptation

Indexed keywords

AMYLOID; PRION PROTEIN;

BETA SHEET; CATALYSIS; CONFORMATIONAL TRANSITION; CROSS REACTION; CRYSTAL STRUCTURE; EVOLUTIONARY ADAPTATION; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SHORT SURVEY; SPECIES DIFFERENCE;

AMYLOID; ANIMALS; MODELS, CHEMICAL; PRIONS; PROTEIN CONFORMATION;

EID: 68649104202     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.05.044     Document Type: Short Survey

References (43)

1. Diaz-Avalos R., Long C., Fontano E., Balbirnie M., Grothe R., Eisenberg D., and Caspar D.L.D. Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide. J. Mol. Biol. 330 (2003) 1165-1175
2. Nelson R., Sawaya M.R., Balbirnie M., Madsen A.O., Riekel C., Grothe R., and Eisenberg D. Structure of the cross-b spine of amyloid-like fibrils. Nature 435 (2005) 773-778
3. Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24 (2002) 329-332
4. Anderson M., Bocharova O.V., Makarava N., Breydo L., Salnikov V.V., and Baskakov I.V. Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy. J. Mol. Biol. 358 (2006) 580-596
5. Tycko R. Molecular structure of amyloid fibrils: insights from solid-state NMR. Quart. Rev. Biophys. (2006) 1-55
6. Petkova A.T., Leapman R.D., Gua Z., Yau W.-M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's b-amyloid fibrils. Science 307 (2005) 262-265
7. Makarava N., and Baskakov I.V. The same primary structure of the prion protein yields two distinct self-propagating states. J. Biol. Chem. 283 (2008) 15988-15996
8. Chien P., Weissman J.S., and DePace A.H. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 73 (2004) 617-656
9. Si K., Lindquist S., and Kandel E.R. A nauronal isoform of the aplysia CPEB has prion-like properties. Cell 115 (2003) 879-891
10. Wickner R.B., Taylor K.L., Edskes H.K., Maddelein M.L., Moriyama H., and Roberts B.T. Yeast prions act as genes composed of self-propagating protein amyloids. Adv. Protein Chem. 57 (2001) 313-314
11. Makarava N., Ostapchenko V.G., Savtchenko R., and Baskakov I.V. Conformational switching within individual amyloid fibrils. J. Biol. Chem. 284 (2009) 14386-14395
12. Baskakov I.V., and Bocharova O.V. In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features. Biochemistry 44 (2005) 2339-2348
13. Eisenberg D., Nelson R., Sawaya M.R., Balbirnie M., Sambashivan S., Ivanova M.I., Madsen A.O., and Riekel C. The structural biology of protein aggregation diseases: fundamental questions and some answers. Acc. Chem. Res. 39 (2006) 568-575
14. Makarava N., Lee C.I., Ostapchenko V.G., and Baskakov I.V. Highly promiscuous nature of prion polymerization. J. Biol. Chem. 282 (2007) 36704-36713
15. Shashilov, V., Xu, M., Makarava, N., Savtchenko, R., Baskakov, I.V. and Lednev, I.K. (submitted for publication) Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy.
16. Colby D.W., Zhang Q., Wang S., Groth D., Legname G., Riesner D., and Prusiner S.B. Prion detection by an amyloid seeding assay. Proc. Acad. Natl. Sci. USA 104 (2007) 20914-20919
17. Atarashi R., Moore R.A., Sim V.L., Hughson A.G., Dorward D.W., Onwubiko H.A., Priola S.A., and Caughey B. Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat. Method 4 (2007) 645-650
18. Sc Prot. Science 14 (2005) 1222-1232
19. Wille, H., McDonald, M., Bian, W., Kendall, A., Borovinskiy, A., Cohen, F., Prusiner, S. and Stubbs, G. (2008) X-ray fiber diffraction reveals major structural differences between brain-derived prions and recombinant prion protein amyloid. In: Abstracts, International Conference "Prion-2008", Madrid, Spain, p. 39 (Ref Type: Abstract).
20. Peretz D., Scott M., Groth D., Williamson A., Burton D., Cohen F.E., and Prusiner S.B. Strain-specified relative conformational stability of the scrapie prion protein. Protein Sci. 10 (2001) 854-863
21. Sun Y., Breydo L., Makarava N., Yang Q., Bocharova O.V., and Baskakov I.V. Site-specific conformational studies of PrP amyloid fibrils revealed two cooperative folding domain within amyloid structure. J. Biol. Chem. 282 (2007) 9090-9097
22. Legname G., Nguyen H.-O.B., Baskakov I.V., Cohen F.E., DeArmond S.J., and Prusiner S.B. Strain-specified characteristics of mouse synthetic prions. Proc. Natl. Acad. Sci. USA 102 (2005) 2168-2173
23. Caughey B., Raymond G.J., and Bessen R.A. Strain-dependent differences in b-sheet conformations of abnormal prion protein. J. Biol. Chem. 273 (1998) 32230-32235
24. Thomzig A., Spassov S., Friedrich M., Naumann D., and Beekes M. Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein. J. Biol. Chem. 279 (2004) 33854
25. Legname G., Nguyen H.-O.B., Peretz D., Cohen F.E., DeArmond S.J., and Prusiner S.B. Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc. Acad. Natl. Sci. USA 103 (2006) 19105-19110
26. Baskakov I.V., and Breydo L. Converting the prion protein: what makes the protein infectious. Biochim. Biophys. Acta (Molecular Basis of Disease) 1772 (2007) 692-703
27. Chesebro B., Trifilo M., Race M., Meade-White K., Teng C., LaCasse R., Raymond L., Favara C., Baron G., Priola S., Caughey B., Masliah E., and Oldstone M. Anchorless prion protein result in infectious amyloid disease without clinical scrapie. Science 308 (2005) 1435-1439
28. Tuzi N.L., Cancellotti E., Baybutt H., Blackford L., Bradford B., Plinston C., Coghill A., Hart P., Piccardo P., Barron R.M., and Manson J.C. Host PrP glycosylation: a major factor determining the outcome of prion infection. PLOS Biol. 6 (2008) e100
29. Lu K.P. Pinning down cell signaling, cancer and Alzheimer's disease. Trends Biochem. Sci. 29 (2004) 200-209
30. Cohen E., and Taraboulos A. Scrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells. EMBO J. 22 (2003) 404-417
31. Eakin C.M., Berman A.J., and Miranker A.D. A native to amyloidogenic transition regulated by a backbone trigger. Nat. Struct. Mol. Biol. 13 (2006) 202-208
32. Capobianco R., Casalone C., Suardi S., Mangieri M., Miccolo C., Limido L., Catania M., Rossi G., Di Fede G., Giaccone G., Bruzzone M.G., Minati L., Corona C., Acutis P., Gelmetti D., Lombardi G., Groschup M.H., Buschmann A., Zanusso G., Monaco S., Caramelli M., and Tagliavini F. Conversion of the BASE prion strain into BSE strain: the origin of BSE?. PLOS Pathog. 3 (2007) e31
33. Peretz D., Williamson R.A., Legname G., Matsunaga Y., Vergara J., Burton D., DeArmond S., Prusiner S., and Scott M.R. A change in the conformation of prions accompanies the emergence of a new prion strain. Neuron 34 (2002) 921-932
34. Castilla J., Gonzalez-Romero D., Saa P., Morales R., De Castro J., and Soto C. Crossing the species barrier by PrPSc replication in vitro generates unique infectious prions. Cell 134 (2008) 757-768
35. Green K.M., Castilla J., Seward T.S., Napier D.L., Jewell J.E., Soto C., and Telling G.C. Accelerated high fidelity prion amplification within and across prion species barriers. PLOS Pathog. 4 (2008) e1000139
36. Nilsson K.P.R., Aslund A., Berg I., Nystrom S., Konradsson P., Herland A., Inganas O., Stabo-Eeg F., Lindgren M., Westermark G.T., Lannfelt L., Nilsson L.N.G., and Hammarstrom P. Imaging distinct conformational states of amyloid-beta fibrils in Alzheimer's disease using novel luminescent probes. ACS Chem. Biol. 2 (2007) 553-560
37. Derkatch I.L., Bradley M.E., Hong J.Y., and Liebman S.W. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 106 (2001) 171-182
38. Derkatch I.L., Uptain S.M., Quteiro T.F., Krishnan R., Lindquist S.L., and Liebman S.W. Effects of Q/N-rich, polyQ, and non-polyQ, amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc. Acad. Natl. Sci. USA 101 (2004) 12934-12939
39. Lundmark K., Westermark G.T., Olsen A., and Westermark P. Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: cross-seeding as a disease mechanism. Proc. Acad. Natl. Sci. USA 102 (2005) 6098-6102
40. O'Nuallain B., Williams A.D., Westermark P., and Wetzel R. Seeding specificity in amyloid growth induced by heterologous fibrils. J. Biol. Chem. 279 (2004) 17490-17494
41. Yan J., Fu X., Ge F., Zhang B., Yao J., Zhang H., Qian J., Tomozawa H., Naiki H., Sawashita J., Mori M., and Higuchi K. Cross-seeding and cross-competition in mouse apolipoprotein A-II amyloid fibrils and protein A amyloid fibrils. Am. J. Pathol. 171 (2007) 172-180
42. Vitrenko Y.A., Gracheva E.O., Richmond J.E., and Liebman S.W. Visualisation of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM. J. Biol. Chem. 282 (2007) 1779-1787
43. Meriin A.B., Zhang X., Newnam G.P., Chernoff Y.O., and Sherman M.Y. Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J. Cell Biol. 157 (2002) 997-1004