Mammalian prion amyloid formation in bacteria

REFERENCES

• Prusiner SB, Prusiner SB, Scott MR, Scott MR, DeArmond SJ, DeArmond SJ, Cohen FE, Cohen FE. Prion protein biology-review. Cell 1998; 93:337-48; PMID:9590169; http://dx.doi.org/10.1016/S0092-8674(00)81163-0.
   PubMed Web of Science ®Google Scholar
• Caughey B, Baron GS, Chesebro B, Jeffrey M. Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions. Annu Rev Biochem 2009; 78:177-204; PMID:19231987; http://dx.doi.org/10.1146/annurev.biochem.78.082907.145410.
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136-44; PMID:6801762; http://dx.doi.org/10.1126/science.6801762.
   PubMed Web of Science ®Google Scholar
• Alper T, Cramp WA, Haig DA, Clarke MC. Does the agent of scrapie replicate without nucleic acid? Nature 1967; 214:764-6; PMID:4963878; http://dx.doi.org/10.1038/214764a0
   Google Scholar
• Griffith JS. Nature of the scrapie agent: self-replication and scrapie. Nature 1967; 215:1043-4; PMID:4964084; http://dx.doi.org/10.1038/2151043a0
   Google Scholar
• Brettschneider J, Tredici K Del, LeeVM-Y, Trojanowski JQ. Spreading of pathology in neurodegenerative diseases: a focus on human studies. Nat Rev Neurosci 2015; 16:109-20; PMID:25588378; http://dx.doi.org/10.1038/nrn3887.
   PubMed Web of Science ®Google Scholar
• Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006; 75:333-66; PMID:16756495; http://dx.doi.org/10.1146/annurev.biochem.75.101304.123901.
   PubMed Web of Science ®Google Scholar
• Guo JL, Lee VMY. Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat Med 2014; 20:130-8; PMID:24504409; http://dx.doi.org/10.1038/nm.3457.
   PubMed Web of Science ®Google Scholar
• Baskakov IV. Switching in amyloid structure within individual fibrils: Implication for strain adaptation, species barrier and strain classification. FEBS Lett 2009; 583:2618-22; PMID:19482025; http://dx.doi.org/10.1016/j.febslet.2009.05.044.
   PubMed Web of Science ®Google Scholar
• Bruce ME, McConnell I, Fraser H, Dickinson AG. The disease characteristics of different strains of scrapie in Sinc congenic mouse lines: implications for the nature of the agent and host control of pathogenesis. J Gen Virol 1991; 72:595-603.
   PubMed Web of Science ®Google Scholar
• Hecker R, Taraboulos A, Scott M, Pan KM, Yang SL, Torchia M, Jendroska K, DeArmond SJ, Prusiner SB. Replication of distinct scrapie prion isolates is region specific in brains of transgenic mice and hamsters. Genes Dev 1992 6:1213-28; PMID:1628828; http://dx.doi.org/10.1101/gad.6.7.1213.
   PubMed Web of Science ®Google Scholar
• Legname G, Baskakov IV, Nguyen H-OB, Riesner D, Cohen FE, DeArmond SJ, Prusiner SB. Synthetic mammalian prions. Science 2004; 305:673-6; PMID:15286374; http://dx.doi.org/10.1126/science.1100195.
   PubMed Web of Science ®Google Scholar
• Makarava N, Kovacs GG, Savtchenko R, Alexeeva I, Budka H, Rohwer RG, Baskakov I V. Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease. PLoS Pathog 2011 7:e1002419; PMID:22144901; http://dx.doi.org/10.1371/journal.ppat.1002419.
   PubMed Web of Science ®Google Scholar
• Makarava N, Kovacs GG, Savtchenko R, Alexeeva I, Ostapchenko VG, Budka H, Rohwer RG, Baskakov I V. A new mechanism for transmissible prion diseases. J Neurosci 2012; 32:7345-55; PMID:22623680; http://dx.doi.org/10.1523/JNEUROSCI.6351-11.2012.
   PubMed Web of Science ®Google Scholar
• Cordeiro Y, Machado F, Juliano L, Juliano MA, Brentani RR, Foguel D, Silva JL. DNA converts cellular prion protein into the β-Sheet conformation and inhibits prion peptide aggregation. J Biol Chem 2001; 276:49400-9; PMID:11604397; http://dx.doi.org/10.1074/jbc.M106707200.
   PubMed Web of Science ®Google Scholar
• Macedo B, Millen TA, Braga CACA, Gomes MPB, Ferreira PS, Kraineva J, Winter R, Silva JL, Cordeiro Y. Nonspecific prion protein-nucleic acid interactions lead to different aggregates and cytotoxic species. Biochemistry 2012; 51:5402-13; PMID:22691027; http://dx.doi.org/10.1021/bi300440e.
   PubMed Web of Science ®Google Scholar
• Critchley P, Kazlauskaite J, Eason R, Pinheiro TJT. Binding of prion proteins to lipid membranes. Biochem Biophys Res Commun 2004; 313:559-67; PMID:14697227; http://dx.doi.org/10.1016/j.bbrc.2003.12.004.
   PubMed Web of Science ®Google Scholar
• Vieira TCRG, Reynaldo DP, Gomes MPB, Almeida MS, Cordeiro Y, Silva JL. Heparin binding by murine recombinant prion protein leads to transient aggregation and formation of rna-resistant species. J Am Chem Soc 2011; 133:334-44; PMID:21142149; http://dx.doi.org/10.1021/ja106725p.
   PubMed Web of Science ®Google Scholar
• Yuan AH, Garrity SJ, Nako E, Hochschild A. Prion propagation can occur in a prokaryote and requires the ClpB chaperone. Elife 2014; 3:e0294910.7554:eLife.02949; PMID:25122461.
   PubMedGoogle Scholar
• Deleault NR, Harris BT, Rees JR, Supattapone S. Formation of native prions from minimal components in vitro. Proc Natl Acad Sci U S A 2007; 104:9741-6; PMID:17535913; http://dx.doi.org/10.1073/pnas.0702662104.
   PubMed Web of Science ®Google Scholar
• Wang F, Wang X, Yuan C-G, Ma J. Generating a prion with bacterially expressed recombinant prion protein. Science 2010; 327:1132-5; PMID:20110469; http://dx.doi.org/10.1126/science.1183748.
   PubMed Web of Science ®Google Scholar
• Miller MB, Wang DW, Wang F, Noble GP, Ma J, Woods VL, Li S, Supattapone S. Cofactor molecules induce structural transformation during infectious prion formation. Structure 2013; 21:2061-8; PMID:24120764; http://dx.doi.org/10.1016/j.str.2013.08.025.
   PubMed Web of Science ®Google Scholar
• Villar-Piqué A, Ventura S. Modeling amyloids in bacteria. Microb Cell Fact 2012; 11:166; http://dx.doi.org/10.1186/1475-2859-11-166.
   PubMed Web of Science ®Google Scholar
• Morell M, Bravo R, Espargaró A, Sisquella X, Avilés FX, Fernàndez-Busquets X, Ventura S. Inclusion bodies: Specificity in their aggregation process and amyloid-like structure. Biochim Biophys Acta - Mol Cell Res 2008; 1783:1815-25; http://dx.doi.org/10.1016/j.bbamcr.2008.06.007.
   PubMed Web of Science ®Google Scholar
• de Groot NS, Sabate R, Ventura S. Amyloids in bacterial inclusion bodies. Trends Biochem Sci 2009; 34:408-16.
   PubMed Web of Science ®Google Scholar
• Wasmer C, Benkemoun L, Sabaté R, Steinmetz MO, Coulary-Salin B, Wang L, Riek R, Saupe SJ, Meier BH. Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids. Angew Chem Int Ed Engl 2009; 48:4858-60; PMID:19472238; http://dx.doi.org/10.1002/anie.200806100.
   PubMed Web of Science ®Google Scholar
• Garrity SJ, Sivanathan V, Dong J, Lindquist S, Hochschild A. Conversion of a yeast prion protein to an infectious form in bacteria. Proc Natl Acad Sci U S A 2010; 107:10596-601; PMID:20484678; http://dx.doi.org/10.1073/pnas.0913280107.
   PubMed Web of Science ®Google Scholar
• Espargaró A, Sabate R, Ventura S. Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation. Mol. Biosyst 2012; 8:2839; http://dx.doi.org/10.1039/c2mb25214g.
   Web of Science ®Google Scholar
• Giraldo R. Defined DNA sequences promote the assembly of a bacterial protein into distinct amyloid nanostructures. Proc Natl Acad Sci U S A 2007 104:17388-93; PMID:17959784; http://dx.doi.org/10.1073/pnas.0702006104.
   PubMed Web of Science ®Google Scholar
• Giraldo R, Moreno-Díaz de la Espina S, Fernández-Tresguerres ME, Gasset-Rosa F. RepA-WH1 prionoid: a synthetic amyloid proteinopathy in a minimalist host. Prion 2011; 5:60-4; PMID:21293179; http://dx.doi.org/10.4161/pri.5.2.14913.
   PubMed Web of Science ®Google Scholar
• Molina-García L, Giraldo R. Aggregation interplay between variants of the RepA-WH1 prionoid in Escherichia coli. J Bacteriol 2014; 196:2536-42; http://dx.doi.org/10.1128/JB.01527-14.
   PubMed Web of Science ®Google Scholar
• Moreno-Del Álamo M, de la Espina SM-D, Fernández-Tresguerres ME, Giraldo R. Pre-amyloid oligomers of the proteotoxic RepA-WH1 prionoid assemble at the bacterial nucleoid. Sci Rep 2015; 5:14669; PMID:26423724; http://dx.doi.org/10.1038/srep14669.
   PubMed Web of Science ®Google Scholar
• Macedo B, Sant'Anna R, Navarro S, Cordeiro Y, Ventura S. Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria. Microb Cell Fact 2015; 14:174; PMID:26536866; http://dx.doi.org/10.1186/s12934-015-0361-y.
   PubMed Web of Science ®Google Scholar
• Govaerts C, Wille H, Prusiner SB, Cohen FE. Evidence for assembly of prions with left-handed β-helices into trimers. Proc Natl Acad Sci U S A 2004; 101:8342-7; PMID:15155909; http://dx.doi.org/10.1073/pnas.0402254101.
   PubMed Web of Science ®Google Scholar
• Diaz-Espinoza R, Soto C. High-resolution structure of infectious prion protein: the final frontier. Nat Struct Mol Biol 2012; 19:370-7; PMID:22472622; http://dx.doi.org/10.1038/nsmb.2266.
   PubMed Web of Science ®Google Scholar
• Groveman BR, Dolan MA, Taubner LM, Kraus A, Wickner RB, Caughey B. Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids. J Biol Chem 2014; 289:24129-42; PMID:25028516; http://dx.doi.org/10.1074/jbc.M114.578344.
   PubMed Web of Science ®Google Scholar
• Saborio GP, Permanne B, Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001; 411:810-3; PMID:11459061; http://dx.doi.org/10.1038/35081095.
   PubMed Web of Science ®Google Scholar
• Wilham JM, Orrú CD, Bessen RA, Atarashi R, Sano K, Race B, Meade-White KD, Taubner LM, Timmes A, Caughey B. Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays. PLoS Pathog 2010; 6(12):e1001217.
   PubMed Web of Science ®Google Scholar