New insights into structural determinants of prion protein folding and stability

REFERENCES

• 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
• Benetti F, Geschwind MD, Legname G. De novo prions. F1000 Biol Rep 2010; 2; PMID:20948787
   PubMedGoogle Scholar
• Prusiner SB. Prions. Proc Natl Acad Sci U S A 1998; 95:13363–83; PMID:9811807; http://dx.doi.org/10.1073/pnas.95.23.13363
   PubMed Web of Science ®Google Scholar
• Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, Mehlhorn I, Huang Z, Fletterick RJ, Cohen FE, et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci U S A 1993; 90:10962–6; PMID:7902575; http://dx.doi.org/10.1073/pnas.90.23.10962
   PubMed Web of Science ®Google Scholar
• Smirnovas V, Baron GS, Offerdahl DK, Raymond GJ, Caughey B, Surewicz WK. Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat Struct Mol Biol 2011; 18:504–6; PMID:21441913; http://dx.doi.org/10.1038/nsmb.2035
   PubMed Web of Science ®Google Scholar
• Amenitsch H, Benetti F, Ramos A, Legname G, Requena JR. SAXS structural study of PrP(Sc) reveals ˜11 nm diameter of basic double intertwined fibers. Prion 2013; 7:496–500; PMID:24247356; http://dx.doi.org/10.4161/pri.27190
   PubMed Web of Science ®Google Scholar
• Legname G, Giachin G, Benetti F. Structural studies of prion proteins and prions. In: Rahimi F, Bitan G, eds., Non-Fibrillar Amyloidogenic Protein Assemblies-Common Cytotoxins Underlying Degenerative Diseases. Taylor & Francis; 2012; 289–317
   Google Scholar
• Supattapone S. Prion protein conversion in vitro. J Mol Med (Berl) 2004; 82:348–56; PMID:15014886; http://dx.doi.org/10.1007/s00109-004-0534-3
   PubMed Web of Science ®Google Scholar
• Benetti F, Legname G. De novo mammalian prion synthesis. Prion 2009; 3:213–9; PMID:19887900; http://dx.doi.org/10.4161/pri.3.4.10181
   PubMed Web of Science ®Google Scholar
• Brown K, Mastrianni JA. The prion diseases. J Geriatr Psychiatry Neurol 2010; 23:277–98; PMID:20938044; http://dx.doi.org/10.1177/0891988-710383576
   PubMed Web of Science ®Google Scholar
• Premzl M, Delbridge M, Gready JE, Wilson P, Johnson M, Davis J, Kuczek E, Marshall Graves JA. The prion protein gene: identifying regulatory signals using marsupial sequence. Gene 2005; 349:121–34; PMID:15777726
   PubMed Web of Science ®Google Scholar
• Wopfner F, Weidenhofer G, Schneider R, von Brunn A, Gilch S, Schwarz TF, Werner T, Schatzl HM. Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein. J Mol Biol 1999; 289:1163–78; PMID:10373359; http://dx.doi.org/10.1006/jmbi.1999.2831
   PubMed Web of Science ®Google Scholar
• Damberger FF, Christen B, Perez DR, Hornemann S, Wuthrich K. Cellular prion protein conformation and function. Proc Natl Acad Sci U S A 2011; 108:17308–13; PMID:21987789; http://dx.doi.org/10.1073/pnas.1106325108
   PubMed Web of Science ®Google Scholar
• Hornshaw MP, McDermott JR, Candy JM. Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem Biophys Res Commun 1995; 207:621–9; PMID:7864852; http://dx.doi.org/10.1006/bbrc.1995.1233
   PubMed Web of Science ®Google Scholar
• Brown DR, Hafiz F, Glasssmith LL, Wong BS, Jones IM, Clive C, Haswell SJ. Consequences of manganese replacement of copper for prion protein function and proteinase resistance. EMBO J 2000; 19:1180–6; PMID:10716918; http://dx.doi.org/10.1093/emboj/19.6.1180
   PubMed Web of Science ®Google Scholar
• Jackson GS, Murray I, Hosszu LL, Gibbs N, Waltho JP, Clarke AR, Collinge J. Location and properties of metal-binding sites on the human prion protein. Proc Natl Acad Sci U S A 2001; 98:8531–5; PMID:11438695; http://dx.doi.org/10.1073/pnas.151038498
   PubMed Web of Science ®Google Scholar
• Jones CE, Klewpatinond M, Abdelraheim SR, Brown DR, Viles JH. Probing copper2+ binding to the prion protein using diamagnetic nickel2+ and 1H NMR: the unstructured N terminus facilitates the coordination of six copper2+ ions at physiological concentrations. J Mol Biol 2005; 346:1393–407; PMID:15713489; http://dx.doi.org/10.1016/j.jmb.2004.12.043
   PubMed Web of Science ®Google Scholar
• Singh N, Das D, Singh A, Mohan ML. Prion protein and metal interaction: physiological and pathological implications. Curr Issues Mol Biol 2010; 12:99–107; PMID:19767653
   PubMed Web of Science ®Google Scholar
• D'Angelo P, Della Longa S, Arcovito A, Mancini G, Zitolo A, Chillemi G, Giachin G, Legname G, Benetti F. Effects of the pathological Q212P mutation on human prion protein non-octarepeat copper-binding site. Biochemistry 2012; 51:6068–79; PMID:22788868; http://dx.doi.org/10.1021/bi300233n
   PubMed Web of Science ®Google Scholar
• Gasperini L, Meneghetti E, Pastore B, Benetti F, Legname G. Prion protein and copper cooperatively protect neurons by modulating NMDA receptor through S-nitrosylation. Antioxid Redox Signal 2014; [Epub ahead of print]; PMID:25490055
   PubMedGoogle Scholar
• Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wuthrich K. NMR structure of the mouse prion protein domain PrP(121-231). Nature 1996; 382:180–2; PMID:8700211; http://dx.doi.org/10.1038/382180a0
   PubMed Web of Science ®Google Scholar
• McDonald AJ, Millhauser GL. PrP overdrive: Does inhibition of alpha-cleavage contribute to PrP toxicity and prion disease? Prion 2014; 8(2);183–191 PMID:24721836; http://dx.doi.org/10.4161/pri.28796
   PubMedGoogle Scholar
• Liang J, Kong Q. alpha-Cleavage of cellular prion protein. Prion 2012; 6:453–60; PMID:23052041; http://dx.doi.org/10.4161/pri.22511
   PubMed Web of Science ®Google Scholar
• McDonald AJ, Dibble JP, Evans EG, Millhauser GL. A new paradigm for enzymatic control of alpha-cleavage and beta-cleavage of the prion protein. J Biol Chem 2014; 289:803–13; PMID:24247244; http://dx.doi.org/10.1074/jbc.M113.502351
   PubMed Web of Science ®Google Scholar
• Benetti F, Biarnes X, Attanasio F, Giachin G, Rizzarelli E, Legname G. Structural determinants in prion protein folding and stability. J Mol Biol 2014; 426:3796–810; PMID:25280897; http://dx.doi.org/10.1016/j.jmb.2014.09.017
   PubMed Web of Science ®Google Scholar
• Marijanovic Z, Caputo A, Campana V, Zurzolo C. Identification of an intracellular site of prion conversion. PLoS Pathog 2009; 5:e1000426; PMID:19424437; http://dx.doi.org/10.1371/journal.ppat.1000426
   PubMed Web of Science ®Google Scholar
• Govaerts C, Wille H, Prusiner SB, Cohen FE. Evidence for assembly of prions with left-handed beta-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
• Brazier MW, Lewis V, Ciccotosto GD, Klug GM, Lawson VA, Cappai R, Ironside JW, Masters CL, Hill AF, White AR, et al. Correlative studies support lipid peroxidation is linked to PrP(res) propagation as an early primary pathogenic event in prion disease. Brain Res Bull 2006; 68:346–54; PMID:16377442; http://dx.doi.org/10.1016/j.brainresbull.2005.09.010
   PubMed Web of Science ®Google Scholar
• Guentchev M, Siedlak SL, Jarius C, Tagliavini F, Castellani RJ, Perry G, Smith MA, Budka H. Oxidative damage to nucleic acids in human prion disease. Neurobiol Dis 2002; 9:275–81; PMID:11950273; http://dx.doi.org/10.1006/nbdi.2002.0477
   PubMed Web of Science ®Google Scholar
• Yun SW, Gerlach M, Riederer P, Klein MA. Oxidative stress in the brain at early preclinical stages of mouse scrapie. Exp Neurol 2006; 201:90–8; PMID:16806186; http://dx.doi.org/10.1016/j.expneurol.2006.03.025
   PubMed Web of Science ®Google Scholar