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Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases.

Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Sönnichsen FD
J Biol Chem 275 33650-4 (2000)
Cited: 80 times
EuropePMC logo PMID: 10954699

Abstract

Prion propagation in transmissible spongiform encephalopathies involves the conversion of cellular prion protein, PrP(C), into a pathogenic conformer, PrP(Sc). Hereditary forms of the disease are linked to specific mutations in the gene coding for the prion protein. To gain insight into the molecular basis of these disorders, the solution structure of the familial Creutzfeldt-Jakob disease-related E200K variant of human prion protein was determined by multi-dimensional nuclear magnetic resonance spectroscopy. Remarkably, apart from minor differences in flexible regions, the backbone tertiary structure of the E200K variant is nearly identical to that reported for the wild-type human prion protein. The only major consequence of the mutation is the perturbation of surface electrostatic potential. The present structural data strongly suggest that protein surface defects leading to abnormalities in the interaction of prion protein with auxiliary proteins/chaperones or cellular membranes should be considered key determinants of a spontaneous PrP(C) --> PrP(Sc) conversion in the E200K form of hereditary prion disease.

Reviews - 1fo7 mentioned but not cited (2)

  1. A structural overview of the vertebrate prion proteins. Pastore A, Zagari A. Prion 1 185-197 (2007)
  2. Probing early misfolding events in prion protein mutants by NMR spectroscopy. Giachin G, Biljan I, Ilc G, Plavec J, Legname G. Molecules 18 9451-9476 (2013)

Articles - 1fo7 mentioned but not cited (7)

  1. Search for allosteric disulfide bonds in NMR structures. Schmidt B, Hogg PJ. BMC Struct Biol 7 49 (2007)
  2. NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features. Ilc G, Giachin G, Jaremko M, Jaremko Ł, Benetti F, Plavec J, Zhukov I, Legname G. PLoS One 5 e11715 (2010)
  3. A generic approach to evaluate how B-cell epitopes are surface-exposed on protein structures. Lollier V, Denery-Papini S, Larré C, Tessier D. Mol Immunol 48 577-585 (2011)
  4. Solution structure of the influenza A virus cRNA promoter: implications for differential recognition of viral promoter structures by RNA-dependent RNA polymerase. Park CJ, Bae SH, Lee MK, Varani G, Choi BS. Nucleic Acids Res 31 2824-2832 (2003)
  5. Fragment molecular orbital calculations reveal that the E200K mutation markedly alters local structural stability in the human prion protein. Hasegawa K, Mohri S, Yokoyama T. Prion 4 38-44 (2010)
  6. The landscape of the prion protein's structural response to mutation revealed by principal component analysis of multiple NMR ensembles. Gendoo DM, Harrison PM. PLoS Comput Biol 8 e1002646 (2012)
  7. Hampering the early aggregation of PrP-E200K protein by charge-based inhibitors: a computational study. Agamennone M, Storchi L, Marrone A, Paciotti R. J Comput Aided Mol Des 35 751-770 (2021)


Reviews citing this publication (19)

  1. Peptide aggregation in neurodegenerative disease. Murphy RM. Annu Rev Biomed Eng 4 155-174 (2002)
  2. Genetic Creutzfeldt-Jakob disease and fatal familial insomnia: insights into phenotypic variability and disease pathogenesis. Capellari S, Strammiello R, Saverioni D, Kretzschmar H, Parchi P. Acta Neuropathol 121 21-37 (2011)
  3. Characterization of mutations in PRNP (prion) gene and their possible roles in neurodegenerative diseases. Bagyinszky E, Giau VV, Youn YC, An SSA, Kim S. Neuropsychiatr Dis Treat 14 2067-2085 (2018)
  4. The consequences of pathogenic mutations to the human prion protein. van der Kamp MW, Daggett V. Protein Eng Des Sel 22 461-468 (2009)
  5. Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions. Poggiolini I, Saverioni D, Parchi P. Int J Cell Biol 2013 910314 (2013)
  6. The prion gene complex encoding PrP(C) and Doppel: insights from mutational analysis. Mastrangelo P, Westaway D. Gene 275 1-18 (2001)
  7. Role of prion protein aggregation in neurotoxicity. Corsaro A, Thellung S, Villa V, Nizzari M, Florio T, Florio T. Int J Mol Sci 13 8648-8669 (2012)
  8. Folding aggregated proteins into functionally active forms. Swietnicki W. Curr Opin Biotechnol 17 367-372 (2006)
  9. Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion. Silva JL, Vieira TC, Gomes MP, Rangel LP, Scapin SM, Cordeiro Y. Methods 53 306-317 (2011)
  10. Similar and divergent features in mammalian and yeast prions. Bousset L, Melki R. Microbes Infect 4 461-469 (2002)
  11. Conformational conversion of prion protein in prion diseases. Zhou Z, Xiao G. Acta Biochim Biophys Sin (Shanghai) 45 465-476 (2013)
  12. Subcellular distribution of the prion protein in sickness and in health. Godsave SF, Peters PJ, Wille H. Virus Res 207 136-145 (2015)
  13. Structural mechanisms of oligomer and amyloid fibril formation by the prion protein. Sengupta I, Udgaonkar JB. Chem Commun (Camb) 54 6230-6242 (2018)
  14. Methionine oxidation within the prion protein. Bettinger J, Ghaemmaghami S. Prion 14 193-205 (2020)
  15. Cerebral organoids as a new model for prion disease. Groveman BR, Smith A, Williams K, Haigh CL. PLoS Pathog 17 e1009747 (2021)
  16. Early structural features in mammalian prion conformation conversion. Legname G. Prion 6 37-39 (2012)
  17. Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications. Hackl S, Becker CFW. J Pept Sci 25 e3216 (2019)
  18. Molecular advances in understanding inherited prion diseases. Brown DR. Mol Neurobiol 25 287-302 (2002)
  19. Three-dimensional structures of the prion protein and its doppel. Riek R, Lührs T. Clin Lab Med 23 209-225 (2003)

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  1. Structural studies of the scrapie prion protein by electron crystallography. Wille H, Michelitsch MD, Guenebaut V, Supattapone S, Serban A, Cohen FE, Agard DA, Prusiner SB. Proc Natl Acad Sci U S A 99 3563-3568 (2002)
  2. Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. Lee S, Antony L, Hartmann R, Knaus KJ, Surewicz K, Surewicz WK, Yee VC. EMBO J 29 251-262 (2010)
  3. Unique structural characteristics of the rabbit prion protein. Wen Y, Li J, Yao W, Xiong M, Hong J, Peng Y, Xiao G, Lin D. J Biol Chem 285 31682-31693 (2010)
  4. Zinc drives a tertiary fold in the prion protein with familial disease mutation sites at the interface. Spevacek AR, Evans EG, Miller JL, Meyer HC, Pelton JG, Millhauser GL. Structure 21 236-246 (2013)
  5. Characterization of prion protein (PrP)-derived peptides that discriminate full-length PrPSc from PrPC. Lau AL, Yam AY, Michelitsch MM, Wang X, Gao C, Goodson RJ, Shimizu R, Timoteo G, Hall J, Medina-Selby A, Coit D, McCoin C, Phelps B, Wu P, Hu C, Chien D, Peretz D. Proc Natl Acad Sci U S A 104 11551-11556 (2007)
  6. An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity. Solomon IH, Khatri N, Biasini E, Massignan T, Huettner JE, Harris DA. J Biol Chem 286 14724-14736 (2011)
  7. Influence of pH on the human prion protein: insights into the early steps of misfolding. van der Kamp MW, Daggett V. Biophys J 99 2289-2298 (2010)
  8. Neurotoxic mutants of the prion protein induce spontaneous ionic currents in cultured cells. Solomon IH, Huettner JE, Harris DA. J Biol Chem 285 26719-26726 (2010)
  9. Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans. Yin S, Pham N, Yu S, Li C, Wong P, Chang B, Kang SC, Biasini E, Tien P, Harris DA, Sy MS. Proc Natl Acad Sci U S A 104 7546-7551 (2007)
  10. Prion proteins with pathogenic and protective mutations show similar structure and dynamics. Bae SH, Legname G, Serban A, Prusiner SB, Wright PE, Dyson HJ. Biochemistry 48 8120-8128 (2009)
  11. Common structural traits across pathogenic mutants of the human prion protein and their implications for familial prion diseases. Rossetti G, Cong X, Caliandro R, Legname G, Carloni P. J Mol Biol 411 700-712 (2011)
  12. Oxidation of Helix-3 methionines precedes the formation of PK resistant PrP. Canello T, Frid K, Gabizon R, Lisa S, Friedler A, Moskovitz J, Gasset M, Gabizon R. PLoS Pathog 6 e1000977 (2010)
  13. Conformational preferences of the amylin nucleation site in SDS micelles: an NMR study. Mascioni A, Porcelli F, Ilangovan U, Ramamoorthy A, Veglia G. Biopolymers 69 29-41 (2003)
  14. Identification of a conserved N-capping box important for the structural autonomy of the prion alpha 3-helix: the disease associated D202N mutation destabilizes the helical conformation. Gallo M, Paludi D, Cicero DO, Chiovitti K, Millo E, Salis A, Damonte G, Corsaro A, Thellung S, Schettini G, Melino S, Florio T, Paci M, Aceto A. Int J Immunopathol Pharmacol 18 95-112 (2005)
  15. Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/doppel-induced Neurodegeneration. Atarashi R, Nishida N, Shigematsu K, Goto S, Kondo T, Sakaguchi S, Katamine S. J Biol Chem 278 28944-28949 (2003)
  16. Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target. Meli M, Gasset M, Colombo G. PLoS One 6 e19093 (2011)
  17. Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation. Biljan I, Ilc G, Giachin G, Raspadori A, Zhukov I, Plavec J, Legname G. J Mol Biol 412 660-673 (2011)
  18. Structural basis for the protective effect of the human prion protein carrying the dominant-negative E219K polymorphism. Biljan I, Giachin G, Ilc G, Zhukov I, Plavec J, Legname G. Biochem J 446 243-251 (2012)
  19. Structural facets of disease-linked human prion protein mutants: a molecular dynamic study. Rossetti G, Giachin G, Legname G, Carloni P. Proteins 78 3270-3280 (2010)
  20. Solution structure and dynamics of the I214V mutant of the rabbit prion protein. Wen Y, Li J, Xiong M, Peng Y, Yao W, Hong J, Lin D. PLoS One 5 e13273 (2010)
  21. High hydrophobic amino acid exposure is responsible of the neurotoxic effects induced by E200K or D202N disease-related mutations of the human prion protein. Corsaro A, Thellung S, Bucciarelli T, Scotti L, Chiovitti K, Villa V, D'Arrigo C, Aceto A, Florio T. Int J Biochem Cell Biol 43 372-382 (2011)
  22. Impact of the tail and mutations G131V and M129V on prion protein flexibility. Santini S, Claude JB, Audic S, Derreumaux P. Proteins 51 258-265 (2003)
  23. Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice. Li A, Piccardo P, Barmada SJ, Ghetti B, Harris DA. EMBO J 26 2777-2785 (2007)
  24. Electrostatics in the stability and misfolding of the prion protein: salt bridges, self energy, and solvation. Guest WC, Cashman NR, Plotkin SS. Biochem Cell Biol 88 371-381 (2010)
  25. Studies of the transmissibility of the agent of bovine spongiform encephalopathy to the domestic chicken. Moore J, Hawkins SA, Austin AR, Konold T, Green RB, Blamire IW, Dexter I, Stack MJ, Chaplin MJ, Langeveld JP, Simmons MM, Spencer YI, Webb PR, Dawson M, Wells GA. BMC Res Notes 4 501 (2011)
  26. Evidence that the 127-164 region of prion proteins has two equi-energetic conformations with beta or alpha features. Derreumaux P. Biophys J 81 1657-1665 (2001)
  27. Use of bovine recombinant prion protein and real-time quaking-induced conversion to detect cattle transmissible mink encephalopathy prions and discriminate classical and atypical L- and H-Type bovine spongiform encephalopathy. Hwang S, Greenlee JJ, Nicholson EM. PLoS One 12 e0172391 (2017)
  28. Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease. Zheng Z, Zhang M, Wang Y, Ma R, Guo C, Feng L, Wu J, Yao H, Lin D. Sci Rep 8 13211 (2018)
  29. Binding of recombinant but not endogenous prion protein to DNA causes DNA internalization and expression in mammalian cells. Yin S, Fan X, Yu S, Li C, Sy MS. J Biol Chem 283 25446-25454 (2008)
  30. Identification of I137M and other mutations that modulate incubation periods for two human prion strains. Giles K, De Nicola GF, Patel S, Glidden DV, Korth C, Oehler A, DeArmond SJ, Prusiner SB. J Virol 86 6033-6041 (2012)
  31. Investigation of the molecular similarity in closely related protein systems: The PrP case study. Storchi L, Paciotti R, Re N, Marrone A. Proteins 83 1751-1765 (2015)
  32. Epitope scanning indicates structural differences in brain-derived monomeric and aggregated mutant prion proteins related to genetic prion diseases. Tapella L, Stravalaci M, Bastone A, Biasini E, Gobbi M, Chiesa R. Biochem J 454 417-425 (2013)
  33. Salt-Mediated Oligomerization of the Mouse Prion Protein Monitored by Real-Time NMR. Sengupta I, Bhate SH, Das R, Udgaonkar JB. J Mol Biol 429 1852-1872 (2017)
  34. An insight of early PrP-E200K aggregation by combined molecular dynamics/fragment molecular orbital approaches. Paciotti R, Storchi L, Marrone A. Proteins 87 51-61 (2019)
  35. Introducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitro. Kyle LM, John TR, Schätzl HM, Lewis RV. PLoS One 8 e66715 (2013)
  36. pH effects on the conformational preferences of amyloid beta-peptide (1-40) in HFIP aqueous solution by NMR spectroscopy. Valerio M, Porcelli F, Zbilut JP, Giuliani A, Manetti C, Conti F. ChemMedChem 3 833-843 (2008)
  37. Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2-α2 loop and α2-α3. Chandrasekaran P, Rajasekaran R. Mol Biosyst 12 3223-3233 (2016)
  38. Molecular dynamics study of the dominant-negative E219K polymorphism in human prion protein. Jahandideh S, Jamalan M, Faridounnia M. J Biomol Struct Dyn 33 1315-1325 (2015)
  39. On the Dependence of Prion and Amyloid Structure on the Folding Environment. Roterman I, Stapor K, Gądek K, Gubała T, Nowakowski P, Fabian P, Konieczny L. Int J Mol Sci 22 13494 (2021)
  40. Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding. Cheng CJ, Koldsø H, Van der Kamp MW, Schiøtt B, Daggett V. J Neurochem 142 171-182 (2017)
  41. The Effects of Ca2+ Concentration and E200K Mutation on the Aggregation Propensity of PrPC: A Computational Study. Marrone A, Re N, Storchi L. PLoS One 11 e0168039 (2016)
  42. Detecting early stage structural changes in wild type, pathogenic and non-pathogenic prion variants using Markov state model. Jani V, Sonavane U, Joshi R. RSC Adv 9 14567-14579 (2019)
  43. Homodimeric complexes of the 90-231 human prion: a multilayered computational study based on FMO/GRID-DRY approach. Paciotti R, Storchi L, Marrone A. J Mol Model 28 241 (2022)
  44. Molecular dynamics studies on the buffalo prion protein. Zhang J, Wang F, Chatterjee S. J Biomol Struct Dyn 34 762-777 (2016)
  45. Novel quaternary structures of the human prion protein globular domain. Bortot LO, Rangel VL, Pavlovici FA, El Omari K, Wagner A, Brandao-Neto J, Talon R, von Delft F, Reidenbach AG, Vallabh SM, Minikel EV, Schreiber S, Nonato MC. Biochimie 191 118-125 (2021)
  46. Why don't humans get scrapie from eating sheep? A possible explanation based on secondary structure predictions. Concepcion GP, David MP, Padlan EA. Med Hypotheses 64 919-924 (2005)
  47. A cluster of familial Creutzfeldt-Jakob disease mutations recapitulate conserved residues in Doppel: a case of molecular mimicry? Mastrangelo P, Serpell L, Dafforn T, Lesk A, Fraser P, Westaway D. FEBS Lett 532 21-26 (2002)
  48. Refinement of under-determined loops of Human Prion Protein by database-derived distance constraints. Cui F, Mukhopadhyay K, Young WB, Jernigan RL, Wu Z. Int J Data Min Bioinform 3 454-468 (2009)
  49. Searching for factors that distinguish disease-prone and disease-resistant prions via sequence analysis. Kedarisetti KD, Dick S, Kurgan L. Bioinform Biol Insights 2 133-144 (2008)
  50. Stress and viral insults do not trigger E200K PrP conversion in human cerebral organoids. Smith A, Groveman BR, Winkler C, Williams K, Walters R, Yuan J, Zou W, Peterson K, Foliaki ST, Haigh CL. PLoS One 17 e0277051 (2022)
  51. Distinct effects of mutations on biophysical properties of human prion protein monomers and oligomers. Yu Y, Yu Z, Zheng Z, Wang H, Wu X, Guo C, Lin D. Acta Biochim Biophys Sin (Shanghai) 48 1016-1025 (2016)
  52. Thermodynamic characterization for the denatured state of bovine prion protein and the BSE Associated variant E211K. Hwang S, Nicholson EM. Prion 12 301-309 (2018)


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