Koch’s postulates and infectious proteins - Acta Neuropathologica
- ️Jucker, Mathias
- ️Tue May 16 2006
Aguzzi A, Polymenidou M (2004) Mammalian prion biology: one century of evolving concepts. Cell 116:313–327
Brock TD (1999) Robert Koch: a life in medicine and bacteriology. American Society of Microbiology Press, Washington
Carrell RW, Lomas DA (2002) Alpha1-antitrypsin deficiency—a model for conformational diseases. N Engl J Med 346:45–53
Castilla J, Saa P, Hetz C, Soto C (2005) In vitro generation of infectious scrapie prions. Cell 121:195–206
Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26:267–298
Chesebro B (2003) Introduction to the transmissible spongiform encephalopathies or prion diseases. Br Med Bull 66:1–20
Chesebro B, Trifilo M, Race R, Meade-White K, Teng C, LaCasse R, Raymond L, Favara C, Baron G, Priola S, Caughey B, Masliah E, Oldstone M (2005) Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308:1420–1421
Chien P, Weissman JS, DePace AH (2004) Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 73:617–656
Dobson CM (2002) Getting out of shape. Nature 418:729–730
Dobson CM (2005) Structural biology: prying into prions. Nature 435:747–749
Dzwolak W, Grudzielanek S, Smirnovas V, Ravindra R, Nicolini C, Jansen R, Loksztejn A, Porowski S, Winter R (2005) Ethanol-perturbed amyloidogenic self-assembly of insulin: looking for origins of amyloid strains. Biochemistry 44:8948–8958
Evans AS (1991) Causation and disease: effect of technology on postulates of causation. Yale J Biol Med 64:513–528
Evans AS (1976) Causation and disease: the Henle-Koch postulates revisited. Yale J Biol Med 49:175–195
Falkow S (2004) Molecular Koch’s postulates applied to bacterial pathogenicity—a personal recollection 15 years later. Nat Rev Microbiol 2:67–72
Fu X, Korenaga T, Fu L, Xing Y, Guo Z, Matsushita T, Hosokawa M, Naiki H, Baba S, Kawata Y, Ikeda S, Ishihara T, Mori M, Higuchi K (2004) Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils. FEBS Lett 563:179–184
Gajdusek DC (1994) Spontaneous generation of infectious nucleating amyloids in the transmissible and nontransmissible cerebral amyloidoses. Mol Neurobiol 8:1–13
Hardy J (2005) Expression of normal sequence pathogenic proteins for neurodegeneration contributes to disease risk: “Permissive templating” as a general disease mechanism of neurodegeneration. Biochem Soc Trans 33:578–581
Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science 297:353–356
Heikenwalder M, Zeller N, Seeger H, Prinz M, Klohn PC, Schwarz P, Ruddle NH, Weissmann C, Aguzzi A (2005) Chronic lymphocytic inflammation specifies the organ tropism of prions. Science 307:1107–1110
Jones EM, Surewicz WK (2005) Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell 121:63–72
Jones EM, Surewicz K, Surewicz WK (2006) Role of N-terminal familial mutations in prion protein fibrillization and prion amyloid propagation in vitro. J Biol Chem 281:8190–8196
Kakizuka A (1998) Protein precipitation: a common etiology in neurodegenerative disorders? Trends Genet 14:396–402
Krishnan R, Lindquist SL (2005) Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435:765–772
Legname G, Baskakov IV, Nguyen HO, Riesner D, Cohen FE, DeArmond SJ, Prusiner SB (2004) Synthetic mammalian prions. Science 305:673–676
Legname G, Nguyen HO, Baskakov IV, Cohen FE, DeArmond SJ, Prusiner SB (2005) Strain-specified characteristics of mouse synthetic prions. Proc Natl Acad Sci USA 102:2168–2173
Loeffler F (1884) Untersuchungen über die Bedeutung der Mikroorganismen für die Entstehung der Diptherie beim Menschen, bei der Taube und beim Kalbe. Mitth. a.d. kaiserl. Gesundheitsampte Ii, pp 421–499
Lundmark K, Westermark GT, Olsen A, Westermark P (2005) Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: cross-seeding as a disease mechanism. Proc Natl Acad Sci USA 102:6098–6102
Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D (2005) Structure of the cross-beta spine of amyloid-like fibrils. Nature 435:773–778
O’Nuallain B, Williams AD, Westermark P, Wetzel R (2004) Seeding specificity in amyloid growth induced by heterologous fibrils. J Biol Chem 279:17490–17490
Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R (2005) Self-propagating, molecular-level polymorphism in Alzheimer’s beta-amyloid fibrils. Science 307:262–265
Prusiner SB (1995) The prion diseases. Sci Am 272:48–51
Prusiner SB (2001) Shattuck lecture—neurodegenerative diseases and prions. N Engl J Med 344:1516–1526
Prusiner SB, Safar J, Cohen FE, DeArmond SJ (1999) The prion diseases. In: Terry RD, Katzman R, Bick KL, Sisodia SS (eds) Alzheimer disease. Lippincott Williams and Wilkins, Philadelphia, pp 161–179
Ritter C, Maddelein ML, Siemer AB, Luhrs T, Ernst M, Meier BH, Saupe SJ, Riek R (2005) Correlation of structural elements and infectivity of the HET-s prion. Nature 435:844–848
Sigurdsson EM, Wisniewski T, Frangione B (2002) Infectivity of amyloid diseases. Trends Mol Med 8:411–413
Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, Hayes SF, Caughey B (2005) The most infectious prion protein particles. Nature 437:257–261
Tanaka M, Chien P, Yonekura K, Weissman JS (2005) Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins. Cell 121:49–62
Unterberger U, Voigtlander T, Budka H (2005) Pathogenesis of prion diseases. Acta Neuropath 109:32–48
Van Everbroeck B, Pals P, Martin JJ, Cras P (2002) Transmissible spongiform encephalopathies: the story of a pathogenic protein. Peptides 23:1351–1359
Walker LC, LeVine H (2000) The cerebral proteopathies: neurodegenerative disorders of protein conformation and assembly. Mol Neurobiol 21:83–95
Walker LC, LeVine H III (2002) Proteopathy: the next therapeutic frontier? Curr Opin Investig Drugs 3:782–787
Walker LC, LeVine H, Mattson MP, Jucker M (2006) Inducible proteopathies. TINS (in press)
Weissman C (2004) The state of the prion. Nat Rev Microbiol 2:861–871
Weissmann C (2005) Birth of a prion: spontaneous generation revisited. Cell 122:165–168
Xing Y, Nakamura A, Korenaga T, Guo Z, Yao J, Fu X, Matsushita T, Kogishi K, Hosokawa M, Kametani F, Mori M, Higuchi K (2002) Induction of protein conformational change in mouse senile amyloidosis. J Biol Chem 277:164–169
Yamaguchi K, Takahashi S, Kawai T, Naiki H, Goto Y (2005) Seeding-dependent propagation and maturation of amyloid fibril conformation. J Mol Biol 352:952–960
Zou WQ, Gambetti P (2005) From microbes to prions: the final proof of the prion hypothesis. Cell 121:155–157