PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2012 | 59 | 2 |

Tytuł artykułu

Nature of cross-seeding barriers of amyloidogenesis

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The epidemics of bovine spongiform encephalopathy (BSE) several decades ago and present epidemics of chronic wasting disease (CWD) among cervids posed a threat of cross-species infections to humans or other animals. Therefore, the question as to the molecular nature of the species barriers to transmissibility of prion diseases is very important. We approached this problem theoretically, first developing a model of template-monomer interaction based on logical and topological grounds and on experimental data about cross-seeding of PrP 23-144 protein orthologs. Further, we propose that the strength of the cross-seeding barriers is proportional to dissimilarity of key amyloidogenic regions of the proteins. This dissimilarity can be measured by dissimilarity function we propose. Scaled on experimental data, this function predicts if cross-seeding can occur between different variants of PrP23-144. The resemblance of PrP23-144 cross-seeding barriers to the barriers of cross-species transmissibility of prion diseases is discussed. We suggest that a similar theoretical approach could be applied to predicting the occurrence of species barriers of prion diseases at least in part corresponding to the process of multiplication of infectious agent.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

59

Numer

2

Opis fizyczny

p.307-312,fig.,ref.

Twórcy

  • Laboratory of Molecular Basis of Cell Motility, Nencki Institute of Experimental Biology, Warsaw, Poland
autor

Bibliografia

  • Apostol MI, Wiltzius JJ, Sawaya MR, Cascio D, Eisenberg D (2011) Atomic structures suggest determinants of transmission barriers in mammalian prion disease. Biochemistry 50: 2456-2463. 
  • Bellotti V, Chiti F (2008) Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. Curr Opin Struct Biol 18: 771-779. 
  • Bruce KL, Chernoff YO (2011) Sequence specificity and fidelity of prion transmission in yeast. Semin Cell Dev Biol 22: 444-451. 
  • Chen B, Newnam GP, Chernoff YO (2007) Prion species barrier between the closely related yeast proteins is detected despite coaggregation. Proc Natl Acad Sci USA 104: 2791-2796. 
  • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366. 
  • Ciani B, Hutchinson EG, Sessions RB, Woolfson DN (2002) A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins. J Biol Chem 277: 10150-10155. 
  • Cobb NJ, Apetri AC, Surewicz WK (2008) Prion protein amyloid formation under native-like conditions involves refolding of the C-terminal alpha-helical domain. J Biol Chem 283: 34704-34711. 
  • Colletier JP, Laganowsky A, Landau M, Zhao M, Soriaga AB, Goldschmidt L, Flot D, Cascio D, Sawaya MR, Eisenberg D (2011) Molecular basis for amyloid-beta polymorphism. Proc Natl Acad Sci USA 108: 16938-16943 
  • Esteras-Chopo A, Serrano L, López de la Paz M (2005) The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc Natl Acad Sci USA 102: 16672-16677. 
  • Gambetti P, Petersen RB, Parchi P, Chen SG, Capellari S, Goldfarb L, Gabizon R, Montagna P, Lugaresi E, Picardo P, Ghetti B (1999) in Prion Biology and Diseases. Prusiner SB ed. pp 509-583. Cold Spring Harbor Laboratory Press, Plainview, NY. 
  • Garnier J, Osguthorpe DJ, Robson B (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 120: 97-120. 
  • Garnier J, Gibrat J-F, Robson B (1996) GOR secondary structure prediction method version IV. Methods Enzymol 266: 540-553.
  • de Groot NS, Aviles FX, Vendrell J, Ventura S ( 2006) Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities. FEBS J 273: 658-668. 
  • Hall D, Hirota N, Dobson CM (2005) A toy model for predicting the rate of amyloid formation from unfolded protein. J Mol Biol 351: 195-205. 
  • Helmus JJ, Surewicz K, Apostol MI, Surewicz WK, Jaroniec CP (2011) Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy. J Am Chem Soc 133: 13934-13937. 
  • Hills RD Jr, Brooks CL 3rd (2007) Hydrophobic cooperativity as a mechanism for amyloid nucleation. J Mol Biol 368: 894-901. 
  • 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, Wu B, Surewicz K, Nadaud PS, Helmus JJ, Chen S, Jaroniec CP, Surewicz WK (2011) Structural polymorphism in amyloids: New insights from studies with Y145Stop prion protein fibrils. J Biol Chem 286: 42777-42784. 
  • Kim W, Hecht MH (2006) Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Abeta42 peptide. Proc Natl Acad Sci USA 103: 15824-15829. 
  • Kim W, Hecht MH (2008) Mutations Enhance the Aggregation Propensity of the Alzheimer's Abeta Peptide. J Mol Biol 377: 565-574. 
  • Kundu B, Maiti NR, Jones EM, Surewicz KA, Vanik DL, Surewicz WK (2003) Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation. Proc Natl Acad Sci USA 100: 12069-12074. 
  • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132. 
  • Lu X, Wintrode PL, Surewicz WK (2007) Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc Natl Acad Sci USA 104: 1510-1515. 
  • Margittai M, Langen R (2008) Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy. Q Rev Biophys 41: 265-297. 
  • Panza G, Luers L, Stohr J, Nagel-Steger L, Weiss J, Riesner D, Willbold D, Birkmann E (2010) Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro. PLOS One 5: e14283. 
  • Prusiner SB (1982 ) Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144. 
  • Saiki M, Honda S, Kawasaki K, Zhou D, Kaito A, Konakahara T, Mori H (2005) Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains. J Mol Biol 348: 983-998. 
  • Senguen FT, Lee NR, Gu X, Ryan DM, Doran TM, Anderson EA, Nilsson BL (2011a) Probing aromatic, hydrophobic, and steric effects on the self-assembly of an amyloid-β fragment peptide. Mol Biosyst 7: 486-496. 
  • Senguen FT, Doran TM, Anderson EA, Nilsson BL (2011b) Clarifying the influence of core amino acid hydrophobicity, secondary structure propensity, and molecular volume on amyloid-β 16-22 self-assembly. Mol Biosyst 7: 497-510. 
  • Surewicz WK, Jones EM, Apetri AC (2006) The emerging principles of mammalian prion propagation and transmissibility barriers: Insight from studies in vitro. Acc Chem Res 39: 654-662. 
  • Tartaglia GG, Cavalli A, Pellarin R, Caflisch A (2005) Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Sci 14: 2723-2734. 
  • Tsemekhman K, Goldschmidt L, Eisenberg D, Baker D (2007) Cooperative hydrogen bonding in amyloid formation. Protein Sci 16: 761-764. 
  • Vanik DL, Surewicz KA, Surewicz WK (2004) Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol Cell 14: 139-145.

Uwagi

PL
Rekord w opracowaniu.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-868e0758-8274-49b0-bb35-f5fb803d8bc6
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.