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Volumn 153, Issue 2, 2013, Pages 139-145

Species-barrier phenomenon in prion transmissibility from a viewpoint of protein science

Author keywords

amyloid; left handed parallel helix; prion; species barrier; spiral model

Indexed keywords

PRION PROTEIN;

EID: 84878188613     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvs148     Document Type: Review
Times cited : (23)

References (54)
  • 1
    • 0003661592 scopus 로고    scopus 로고
    • 2nd edn. Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • Prusiner, S.B. (2004) Prion Biology and Disease. 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (2004) Prion Biology and Disease
    • Prusiner, S.B.1
  • 2
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper, T., Cramp, W.A., Haig, D.A., and Clarke, M.C. (1967) Does the agent of scrapie replicate without nucleic acid? Nature 214, 764-766
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 3
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S.B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 8
    • 0034705020 scopus 로고    scopus 로고
    • Interactions between heterologous forms of prion protein: Vbinding, inhibition of conversion, and species barriers
    • Horiuchi, M, Priola, S.A., Chabry, J., and Caughey, B. (2000) Interactions between heterologous forms of prion protein: Vbinding, inhibition of conversion, and species barriers. Proc. Natl. Acad. Sci. U S A. 97, 5836-5841
    • (2000) Proc. Natl. Acad. Sci. U S A. , vol.97 , pp. 5836-5841
    • Horiuchi, M.1    Priola, S.A.2    Chabry, J.3    Caughey, B.4
  • 9
    • 57249089081 scopus 로고    scopus 로고
    • Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy
    • Veith, N.M., Plattner, H., Stuermer, C.A.O., Schulz- Schaeffer, W.J., and Bürkle, A. (2009) Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy. Eur. J. Cell Biol. 88, 45-63
    • (2009) Eur. J. Cell Biol , vol.88 , pp. 45-63
    • Veith, N.M.1    Plattner, H.2    Stuermer, C.A.O.3    Schulz-Schaeffer, W.J.4    Bürkle, A.5
  • 11
    • 33846818651 scopus 로고    scopus 로고
    • Efficient dissemination of prions through preferential transmission to nearby cells
    • Paquet, S., Langevin, C., Chapuis, J., Jackson, G.S., Laude, H., and Vilette, D. (2007) Efficient dissemination of prions through preferential transmission to nearby cells. J. Gen. Virol. 88, 706-713
    • (2007) J. Gen. Virol , vol.88 , pp. 706-713
    • Paquet, S.1    Langevin, C.2    Chapuis, J.3    Jackson, G.S.4    Laude, H.5    Vilette, D.6
  • 13
    • 11144221186 scopus 로고    scopus 로고
    • Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections
    • Neuendorf, E., Weber, A., Saalmueller, A., Schatzl, H., Reifenberg, K., Pfaff, E., and Groschup, M.H. (2004) Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections. J. Biol. Chem. 279, 53306-53316
    • (2004) J. Biol. Chem , vol.27 , pp. 53306-53316
    • Neuendorf, E.1    Weber, A.2    Saalmueller, A.3    Schatzl, H.4    Reifenberg, K.5    Pfaff, E.6    Groschup, M.H.7
  • 15
    • 0025103308 scopus 로고
    • Rapid detection of Creutzfeldt- Jakob disease and scrapie prion proteins
    • Serban, D., Taraboulos, A., DeArmond, S.J., and Prusiner, S.B. (1990) Rapid detection of Creutzfeldt- Jakob disease and scrapie prion proteins. Neurology 40, 110-117
    • (1990) Neurology , vol.40 , pp. 110-117
    • Serban, D.1    Taraboulos, A.2    DeArmond, S.J.3    Prusiner, S.B.4
  • 16
    • 62149128180 scopus 로고    scopus 로고
    • High-resolution differentiation of transmissible spongiform encephalopathy strains by quantitative N-terminal amino acid profiling (N-TAAP) of PK-digested abnormal prion protein
    • Gielbert, A., Davis, L.A., Sayers, A.R., Hope, J., Gill, A.C., and Sauer, M.J. (2009) High-resolution differentiation of transmissible spongiform encephalopathy strains by quantitative N-terminal amino acid profiling (N-TAAP) of PK-digested abnormal prion protein. J. Mass Spectrom. 44, 384-396
    • (2009) J. Mass Spectrom , vol.44 , pp. 384-396
    • Gielbert, A.1    Davis, L.A.2    Sayers, A.R.3    Hope, J.4    Gill, A.C.5    Sauer, M.J.6
  • 18
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey, B.W., Dong, A., Bhat, K.S., Ernst, D., Hayes, S.F., and Caughey, W.S. (1991) Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30, 7672-7680
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 22
    • 1542357669 scopus 로고    scopus 로고
    • Identification of a second bovine amyloidotic spongiform encephalopathy: Molecular similarities with sporadic Creutzfeldt-Jakob disease
    • Casalone, C., Zanusso, G., Acutis, P., Ferrari, S., Capucci, L., Tagliavini, F., Monaco, S., and Caramelli, M. (2004) Identification of a second bovine amyloidotic spongiform encephalopathy: Molecular similarities with sporadic Creutzfeldt-Jakob disease. Proc. Natl. Acad. Sci. U S A. 101, 3065-3070
    • (2004) Proc. Natl. Acad. Sci. U S A. , vol.10 , pp. 3065-3070
    • Casalone, C.1    Zanusso, G.2    Acutis, P.3    Ferrari, S.4    Capucci, L.5    Tagliavini, F.6    Monaco, S.7    Caramelli, M.8
  • 23
    • 34948853876 scopus 로고    scopus 로고
    • Accumulation of mono-glycosylated form-rich, plaque-forming PrPSc in the second atypical bovine encephalopathy case in Japan
    • Hagiwara, K., Yamakawa, Y., Sato, Y., Nakamura, Y., Tobiume, M., Shinagawa, M., and Sata, T. (2007) Accumulation of mono-glycosylated form-rich, plaque-forming PrPSc in the second atypical bovine encephalopathy case in Japan. Jpn. J. Infect. Dis. 60, 305-308
    • (2007) Jpn. J. Infect. Dis , vol.60 , pp. 305-308
    • Hagiwara, K.1    Yamakawa, Y.2    Sato, Y.3    Nakamura, Y.4    Tobiume, M.5    Shinagawa, M.6    Sata, T.7
  • 25
    • 65649094124 scopus 로고    scopus 로고
    • Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle
    • Masujin, K., Shu, Y., Yamakawa, Y., Hagiwara, K., Sata, T., Matsuura, Y., Iwamaru, Y., Imamura, M., Okada, H., Mohri, S., and Yokoyama, T. (2008) Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle. Prion 2, 123-128
    • (2008) Prion , vol.2 , pp. 123-128
    • Masujin, K.1    Shu, Y.2    Yamakawa, Y.3    Hagiwara, K.4    Sata, T.5    Matsuura, Y.6    Iwamaru, Y.7    Imamura, M.8    Okada, H.9    Mohri, S.10    Yokoyama, T.11
  • 28
    • 78951482397 scopus 로고    scopus 로고
    • Strain-specific barriers against bovine prions in hamsters
    • Nicot, S. and Baron, T. (2011) Strain-specific barriers against bovine prions in hamsters. J. Virol. 85, 1906-1908
    • (2011) J. Virol , vol.85 , pp. 1906-1908
    • Nicot, S.1    Baron, T.2
  • 39
  • 40
    • 0028844306 scopus 로고
    • A left-handed parallel b helix in the structure of UDP-N- acetylglucosamine acyltransferase
    • Raetz, C.R.H. and Roderick, S.L (1995) A left-handed parallel b helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270, 997-1000
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.H.1    Roderick, S.L.2
  • 41
    • 22144432561 scopus 로고    scopus 로고
    • Molecular dynamics simulations indicate a possible role of parallel b-helices in seeded aggregation of poly-Gln
    • Stork, M., Giese, A., Kretzschmar, H.A., and Tavan, P. (2005) Molecular dynamics simulations indicate a possible role of parallel b-helices in seeded aggregation of poly-Gln. Biophys. J. 88, 2442-2451
    • (2005) Biophys. J. , vol.88 , pp. 2442-2451
    • Stork, M.1    Giese, A.2    Kretzschmar, H.A.3    Tavan, P.4
  • 42
    • 33745620145 scopus 로고    scopus 로고
    • Two-rung models of a left-handed b-helix for prions explains species barrier and strain variation in transmissible spongiform encephalopathies
    • Langedijk, J.P.M., Fuentes, G., Boshuizen, R., and Bonvin, A.M.J.J. (2006) Two-rung models of a left-handed b-helix for prions explains species barrier and strain variation in transmissible spongiform encephalopathies. J. Mol. Biol. 360, 907-920
    • (2006) J. Mol. Biol , vol.36 , pp. 907-920
    • Langedijk, J.P.M.1    Fuentes, G.2    Boshuizen, R.3    Bonvin, A.M.J.J.4
  • 43
    • 62449276454 scopus 로고    scopus 로고
    • Left handed b helix models for mammalian prion fibrils
    • Kunes, K.C., Clark, S.C., Cox, D.L., and Singh, R.R.P. (2008) Left handed b helix models for mammalian prion fibrils. Prion 2, 81-90
    • (2008) Prion , vol.2 , pp. 81-90
    • Kunes, K.C.1    Clark, S.C.2    Cox, D.L.3    Singh, R.R.P.4
  • 44
    • 67650001844 scopus 로고    scopus 로고
    • Site-directed mutagenesis demonstrates the plasticity of the b helix: Implications for the structure of the misfolded prion protein
    • Choi, J.H., May, B.C.H., Govaerts, C., and Cohen, F.E. (2009) Site-directed mutagenesis demonstrates the plasticity of the b helix: Implications for the structure of the misfolded prion protein. Structure 17, 1014-1023
    • (2009) Structure , vol.17 , pp. 1014-1023
    • Choi, J.H.1    May, B.C.H.2    Govaerts, C.3    Cohen, F.E.4
  • 45
    • 84861309388 scopus 로고    scopus 로고
    • Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrPC to PrPSc in prion-infected neuroblastoma cells
    • Hara, H., Okemoto-Nakamura, Y., Shinkai-Ouchi, F., Hanada, K., Yamakawa, Y., and Hagiwara, K. (2012) Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrPC to PrPSc in prion-infected neuroblastoma cells. J. Virol. 86, 5626-5636
    • (2012) J. Virol , vol.86 , pp. 5626-5636
    • Hara, H.1    Okemoto-Nakamura, Y.2    Shinkai-Ouchi, F.3    Hanada, K.4    Yamakawa, Y.5    Hagiwara, K.6
  • 47
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: Protofibril formation of the prion protein
    • DeMarco, M.L. and Daggett, V. (2004) From conversion to aggregation: Protofibril formation of the prion protein. Proc. Natl. Acad. Sci. U S A. 101, 2293-2298
    • (2004) Proc. Natl. Acad. Sci. U S A. , vol.10 , pp. 2293-2298
    • DeMarco, M.L.1    Daggett, V.2
  • 48
    • 33845932931 scopus 로고    scopus 로고
    • Structural properties of prion protein protofibrils and fibrils: An experimental assessment of atomic models
    • DeMarco, M.L., Silveira, J., Caughey, B., and Daggett, V. (2006) Structural properties of prion protein protofibrils and fibrils: An experimental assessment of atomic models. Biochemistry 45, 15573-15582
    • (2006) Biochemistry , vol.45 , pp. 15573-15582
    • DeMarco, M.L.1    Silveira, J.2    Caughey, B.3    Daggett, V.4
  • 49
    • 84860469091 scopus 로고    scopus 로고
    • Disruption of the X-loop turn of the prion protein linked to scrapie resistance
    • Scouras, A.D. and Daggett, V. (2012) Disruption of the X-loop turn of the prion protein linked to scrapie resistance. Protein Eng. Des. Sel. 25, 243-249
    • (2012) Protein Eng. Des. Sel , vol.25 , pp. 243-249
    • Scouras, A.D.1    Daggett, V.2
  • 50
    • 0028822204 scopus 로고
    • A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells
    • Priola, S.A. and Chesebro, B. (1995) A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells. J. Virol. 69, 7754-7758
    • (1995) J. Virol , vol.69 , pp. 7754-7758
    • Priola, S.A.1    Chesebro, B.2
  • 51
    • 79953183597 scopus 로고    scopus 로고
    • Atomic structures suggest determinants of transmission barriers in mammalian prion disease
    • Apostol, M.I., Wiltzius, J.J.W., Sawaya, M.R., Cascio, D., and Eisenberg, D. (2011) Atomic structures suggest determinants of transmission barriers in mammalian prion disease. Biochemistry 50, 2456-2463
    • (2011) Biochemistry , vol.50 , pp. 2456-2463
    • Apostol, M.I.1    Wiltzius, J.J.W.2    Sawaya, M.R.3    Cascio, D.4    Eisenberg, D.5
  • 52
    • 79952916684 scopus 로고    scopus 로고
    • Normal modes of prion proteins: From native to infectious particle
    • Samson, A.O. and Levitt, M. (2011) Normal modes of prion proteins: From native to infectious particle. Biochemistry 50, 2243-2448
    • (2011) Biochemistry , vol.50 , pp. 2243-2448
    • Samson, A.O.1    Levitt, M.2


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