Amyloids, prions and the inherent infectious nature of misfolded protein aggregates.

Misfolded aggregates present in amyloid fibrils are associated with various diseases known as "protein misfolding" disorders. Among them, prion diseases are unique in that the pathology can be transmitted by an infectious process involving an unprecedented agent known as a "prion". Prions are infectious proteins that can transmit biological information by propagating protein misfolding and aggregation. The molecular mechanism of prion conversion has a striking resemblance to the process of amyloid formation, suggesting that misfolded aggregates have an inherent ability to be transmissible. Intriguing recent data suggest that other protein misfolding disorders might also be transmitted by a prion-like infectious process.

[1]  L. Hood,et al.  Purification and structural studies of a major scrapie prion protein , 1984, Cell.

[2]  H. Colten,et al.  Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA. , 1985, Biochemistry.

[3]  T. Chiba,et al.  Fibrilization in mouse senile amyloidosis is fibril conformation-dependent. , 1998, Laboratory investigation; a journal of technical methods and pathology.

[4]  C. Röcken,et al.  Pathology, diagnosis and pathogenesis of AA amyloidosis , 2002, Virchows Archiv.

[5]  TIKVAH ALPER,et al.  Does the Agent of Scrapie Replicate without Nucleic Acid ? , 1967, Nature.

[6]  Peter Bross,et al.  Protein misfolding and disease : principles and protocols , 2003 .

[7]  S. Prusiner,et al.  Immunoaffinity purification and neutralization of scrapie prion infectivity. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[8]  H. Wiśniewski,et al.  Senile dementia of the Alzheimer type: Possibility of infectious etiology in genetically susceptible individuals , 1984, Acta neurologica Scandinavica. Supplementum.

[9]  P. Fraser,et al.  New clothes for amyloid enhancing factor (AEF): silk as AEF. , 1999, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.

[10]  A. Roher,et al.  Exogenous induction of cerebral β-amyloidosis in βAPP-transgenic mice , 2002, Peptides.

[11]  B. Permanne,et al.  Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding , 2001, Nature.

[12]  R. Diaz-Avalos,et al.  Protein-only transmission of three yeast prion strains , 2004, Nature.

[13]  T. Chiba,et al.  Transmission of Mouse Senile Amyloidosis , 2001, Laboratory Investigation.

[14]  John Collinge,et al.  Variant Creutzfeldt-Jakob disease , 1999, The Lancet.

[15]  B. Caughey,et al.  Prion protein conversions: insight into mechanisms, TSE transmission barriers and strains. , 2003, British medical bulletin.

[16]  P. Lansbury,et al.  Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. , 1997, Annual review of biochemistry.

[17]  M. Pepys,et al.  SERUM AMYLOID-A PROTEIN CONCENTRATION IN INFLAMMATORY DISEASES AND ITS RELATIONSHIP TO THE INCIDENCE OF REACTIVE SYSTEMIC AMYLOIDOSIS , 1982, The Lancet.

[18]  D. Gajdusek,et al.  Nucleation of Amyloidogenesis in Infectious and Noninfectious Amyloidoses of Brain , 1994, Annals of the New York Academy of Sciences.

[19]  C. Soto,et al.  Prions: disease propagation and disease therapy by conformational transmission. , 2001, Trends in molecular medicine.

[20]  S. Bansil,et al.  Correlation between sex hormones and magnetic resonance imaging lesions in multiple sclerosis , 1999, Acta neurologica Scandinavica.

[21]  James E. Cleaver,et al.  Search for a Prion-Specific Nucleic Acid , 2005, Journal of Virology.

[22]  Sofia Nyström,et al.  Transmissibility of systemic amyloidosis by a prion-like mechanism , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[23]  C. Soto,et al.  Cyclic amplification of protein misfolding: application to prion-related disorders and beyond , 2002, Trends in Neurosciences.

[24]  A. Salazar,et al.  Alzheimer's Disease and Transmissible Virus Dementia (Creutzfeldt‐Jakob Disease) , 1982, Annals of the New York Academy of Sciences.

[25]  T. Alper,et al.  The exceptionally small size of the scrapie agent. , 1966, Biochemical and biophysical research communications.

[26]  T. Crow,et al.  Experimental Induction of β‐Amyloid Plaques and Cerebral Angiopathy in Primates a , 1993 .

[27]  R. Wickner,et al.  [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. , 1994, Science.

[28]  F. Cohen,et al.  Synthetic Mammalian Prions , 2004, Science.

[29]  S. Duvezin-Caubet,et al.  Amyloid aggregates of the HET-s prion protein are infectious , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[30]  A. Aguzzi,et al.  Mice devoid of PrP are resistant to scrapie , 1993, Cell.

[31]  P. Brown,et al.  Human spongiform encephalopathy: The national institutes of health series of 300 cases of experimentally transmitted disease , 1994, Annals of neurology.

[32]  D. Kryndushkin,et al.  Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104* , 2003, Journal of Biological Chemistry.

[33]  C. Masters,et al.  Evidence for and against the transmissibility of Alzheimer disease , 1980, Neurology.

[34]  B. Ghetti,et al.  Neurological Illness in Transgenic Mice Expressing a Prion Protein with an Insertional Mutation , 1998, Neuron.

[35]  Claudio Soto,et al.  Unfolding the role of protein misfolding in neurodegenerative diseases , 2003, Nature Reviews Neuroscience.

[36]  J. Buxbaum,et al.  The genetics of the amyloidoses. , 2000, Annual review of medicine.

[37]  G. J. Raymond,et al.  The most infectious prion protein particles , 2005, Nature.

[38]  G. Glenner.  Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts). , 1980, The New England journal of medicine.

[39]  K. Kitagawa,et al.  Apolipoprotein A-II gene and development of amyloidosis and senescence in a congenic strain of mice carrying amyloidogenic ApoA-II. , 1995, Laboratory investigation; a journal of technical methods and pathology.

[40]  T. Crow,et al.  Induction of beta (A4)-amyloid in primates by injection of Alzheimer's disease brain homogenate. Comparison with transmission of spongiform encephalopathy. , 1994, Molecular neurobiology.

[41]  J. Weissman,et al.  Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein. , 2000, Science.

[42]  J. Sipe,et al.  Review: history of the amyloid fibril. , 2000, Journal of structural biology.

[43]  S. Lindquist,et al.  Mad Cows Meet Psi-chotic Yeast: The Expansion of the Prion Hypothesis , 1997, Cell.

[44]  E. Sigurdsson,et al.  Infectivity of amyloid diseases. , 2002, Trends in molecular medicine.

[45]  J. Collinge.  Prion diseases of humans and animals: their causes and molecular basis. , 2001, Annual review of neuroscience.

[46]  Stanley B. Prusiner,et al.  Nobel Lecture: Prions , 1998 .

[47]  J. Castilla,et al.  The controversial protein-only hypothesis of prion propagation , 2004, Nature Medicine.

[48]  L. Serpell,et al.  A molecular model of the amyloid fibril. , 1996, Ciba Foundation symposium.

[49]  R. Kisilevsky,et al.  Kinetics of amyloid deposition. I. The effects of amyloid-enhancing factor and splenectomy. , 1983, Laboratory investigation; a journal of technical methods and pathology.

[50]  C. Soto,et al.  Protein misfolding and disease; protein refolding and therapy , 2001, FEBS letters.

[51]  S. Prusiner,et al.  Attempts to restore scrapie prion infectivity after exposure to protein denaturants. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[52]  J. Sánchez-Vizcaíno,et al.  Subclinical Bovine Spongiform Encephalopathy Infection in Transgenic Mice Expressing Porcine Prion Protein , 2004, The Journal of Neuroscience.

[53]  S. Prusiner,et al.  Transmission of Creutzfeldt-Jakob disease from humans to transgenic mice expressing chimeric human-mouse prion protein. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[54]  A. Roher,et al.  Evidence for Seeding of β-Amyloid by Intracerebral Infusion of Alzheimer Brain Extracts in β-Amyloid Precursor Protein-Transgenic Mice , 2000, The Journal of Neuroscience.

[55]  Kimberlin Rh.  Experimental scrapie in the mouse: a review of an important model disease. , 1976 .

[56]  P. Lansbury,et al.  Cell-free formation of protease-resistant prion protein , 1994, Nature.

[57]  C. Dobson,et al.  Observation of sequence specificity in the seeding of protein amyloid fibrils , 2004, Protein science : a publication of the Protein Society.

[58]  J. Kelly,et al.  Alternative conformations of amyloidogenic proteins govern their behavior. , 1996, Current opinion in structural biology.

[59]  S. Prusiner,et al.  Spontaneous neurodegeneration in transgenic mice with mutant prion protein , 1990, Science.

[60]  D. Borchelt,et al.  The Value of Transgenic Models for the Study of Neurodegenerative Diseases , 2000, Annals of the New York Academy of Sciences.

[61]  F. Kametani,et al.  Induction of Protein Conformational Change in Mouse Senile Amyloidosis* , 2002, The Journal of Biological Chemistry.

[62]  C. Dobson.  Protein misfolding, evolution and disease. , 1999, Trends in biochemical sciences.

[63]  P. Westermark,et al.  Fibrils from synthetic amyloid-related peptides enhance development of experimental AA-amyloidosis in mice. , 1994, Biochemical and biophysical research communications.

[64]  A. Fink.  Chaperone-mediated protein folding. , 1999, Physiological reviews.

[65]  P. Lansbury,et al.  Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? , 1993, Cell.

[66]  C. Dobson,et al.  Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases , 2002, Nature.

[67]  Roger Cooke,et al.  Conformational variations in an infectious protein determine prion strain differences , 2004, Nature.

[68]  S. Prusiner,et al.  Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins , 1994, Cell.

[69]  D. Kirschner,et al.  On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[70]  M. Skinner,et al.  Murine amyloid protein AA in casein-induced experimental amyloidosis. , 1977, Laboratory investigation; a journal of technical methods and pathology.

[71]  P. Westermark,et al.  Acceleration of amyloid protein A amyloidosis by amyloid-like synthetic fibrils. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[72]  J. Castilla,et al.  In Vitro Generation of Infectious Scrapie Prions , 2005, Cell.