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Volumn 454, Issue 3, 2013, Pages 417-425

Epitope scanning indicates structural differences in brain-derived monomeric and aggregated mutant prion proteins related to genetic prion diseases

Author keywords

Genetic prion disease; Prion protein (PrP); Protein aggregation; Protein misfolding

Indexed keywords

EPITOPE; MONOCLONAL ANTIBODY; MUTANT PROTEIN; PRION PROTEIN; RECOMBINANT PROTEIN;

EID: 84883427878     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130563     Document Type: Article
Times cited : (11)

References (50)
  • 1
    • 77951499689 scopus 로고    scopus 로고
    • The genetics of prion diseases
    • Mastrianni, J. A. (2010) The genetics of prion diseases. Genet. Med. 12, 187-195
    • (2010) Genet. Med. , vol.12 , pp. 187-195
    • Mastrianni, J.A.1
  • 3
    • 0030011971 scopus 로고    scopus 로고
    • Experimental transmission of Creutzfeldt-Jakob disease and related diseases to rodents
    • Tateishi, J., Kitamoto, T., Hoque, M. Z. and Furukawa, H. (1996) Experimental transmission of Creutzfeldt-Jakob disease and related diseases to rodents. Neurology 46, 532-537
    • (1996) Neurology , vol.46 , pp. 532-537
    • Tateishi, J.1    Kitamoto, T.2    Hoque, M.Z.3    Furukawa, H.4
  • 4
    • 0035168351 scopus 로고    scopus 로고
    • Prion diseases: What is the neurotoxic molecule?
    • Chiesa, R. and Harris, D. A. (2001) Prion diseases: what is the neurotoxic molecule? Neurobiol. Dis. 8, 743-763
    • (2001) Neurobiol. Dis. , vol.8 , pp. 743-763
    • Chiesa, R.1    Harris, D.A.2
  • 7
    • 39749094951 scopus 로고    scopus 로고
    • Multiple biochemical similarities between infectious and non-infectious aggregates of a prion protein carrying an octapeptide insertion
    • Biasini, E., Medrano, A. Z., Thellung, S., Chiesa, R. and Harris, D. A. (2008) Multiple biochemical similarities between infectious and non-infectious aggregates of a prion protein carrying an octapeptide insertion. J. Neurochem. 104, 1293-1308
    • (2008) J. Neurochem. , vol.104 , pp. 1293-1308
    • Biasini, E.1    Medrano, A.Z.2    Thellung, S.3    Chiesa, R.4    Harris, D.A.5
  • 9
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki, W., Petersen, R. B., Gambetti, P. and Surewicz, W. K. (1998) Familial mutations and the thermodynamic stability of the recombinant human prion protein. J. Biol. Chem. 273, 31048-31052
    • (1998) J. Biol. Chem. , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 10
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
    • Liemann, S. and Glockshuber, R. (1999) Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry 38, 3258-3267
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 11
    • 0034721767 scopus 로고    scopus 로고
    • 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, M. G., Surewicz, W. K. and Sonnichsen, F. D. (2000) Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J. Biol. Chem. 275, 33650-33654
    • (2000) J. Biol. Chem. , vol.275 , pp. 33650-33654
    • Zhang, Y.1    Swietnicki, W.2    Zagorski, M.G.3    Surewicz, W.K.4    Sonnichsen, F.D.5
  • 12
    • 75649120399 scopus 로고    scopus 로고
    • Conformational diversity in prion protein variants influences intermolecular β-sheet formation
    • Lee, S., Antony, L., Hartmann, R., Knaus, K. J., Surewicz, K., Surewicz, W. K. and Yee, V. C. (2010) Conformational diversity in prion protein variants influences intermolecular β-sheet formation. EMBO J. 29, 251-262
    • (2010) EMBO J. , vol.29 , pp. 251-262
    • Lee, S.1    Antony, L.2    Hartmann, R.3    Knaus, K.J.4    Surewicz, K.5    Surewicz, W.K.6    Yee, V.C.7
  • 13
    • 77955367206 scopus 로고    scopus 로고
    • NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features
    • Ilc, G., Giachin, G., Jaremko, M., Jaremko, L., Benetti, F., Plavec, J., Zhukov, I. and Legname, G. (2010) NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features. PLoS ONE 5, e11715
    • (2010) PLoS ONE , vol.5
    • Ilc, G.1    Giachin, G.2    Jaremko, M.3    Jaremko, L.4    Benetti, F.5    Plavec, J.6    Zhukov, I.7    Legname, G.8
  • 14
    • 84866666997 scopus 로고    scopus 로고
    • Structural rearrangements at physiological pH: Nuclear magnetic resonance insights from the V210I human prion protein mutant
    • Biljan, I., Ilc, G., Giachin, G., Plavec, J. and Legname, G. (2012) Structural rearrangements at physiological pH: nuclear magnetic resonance insights from the V210I human prion protein mutant. Biochemistry 51, 7465-7474
    • (2012) Biochemistry , vol.51 , pp. 7465-7474
    • Biljan, I.1    Ilc, G.2    Giachin, G.3    Plavec, J.4    Legname, G.5
  • 15
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • Chiesa, R., Piccardo, P., Ghetti, B. and Harris, D. A. (1998) Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21, 1339-1351
    • (1998) Neuron , vol.21 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 16
    • 15744395826 scopus 로고    scopus 로고
    • Cytosolic prion protein (PrP) is not toxic in N2a cells and primary neurons expressing pathogenic PrP mutations
    • Fioriti, L., Dossena, S., Stewart, L. R., Stewart, R. S., Harris, D. A., Forloni, G. and Chiesa, R. (2005) Cytosolic prion protein (PrP) is not toxic in N2a cells and primary neurons expressing pathogenic PrP mutations. J. Biol. Chem. 280, 11320-11328
    • (2005) J. Biol. Chem. , vol.280 , pp. 11320-11328
    • Fioriti, L.1    Dossena, S.2    Stewart, L.R.3    Stewart, R.S.4    Harris, D.A.5    Forloni, G.6    Chiesa, R.7
  • 19
    • 33750002310 scopus 로고    scopus 로고
    • Exploring "one-shot" kinetics and small molecule analysis using the ProteOn XPR36 array biosensor
    • Bravman, T., Bronner, V., Lavie, K., Notcovich, A., Papalia, G. A. and Myszka, D. G. (2006) Exploring "one-shot" kinetics and small molecule analysis using the ProteOn XPR36 array biosensor. Anal. Biochem. 358, 281-288
    • (2006) Anal. Biochem. , vol.358 , pp. 281-288
    • Bravman, T.1    Bronner, V.2    Lavie, K.3    Notcovich, A.4    Papalia, G.A.5    Myszka, D.G.6
  • 22
    • 34249690678 scopus 로고    scopus 로고
    • CpG oligodeoxynucleotide-enhanced humoral immune response and production of antibodies to prion protein PrPSc in mice immunized with 139A scrapie-associated fibrils
    • Spinner, D. S., Kascsak, R. B., Lafauci, G., Meeker, H. C., Ye, X., Flory, M. J., Kim, J. I., Schuller-Levis, G. B., Levis, W. R., Wisniewski, T. et al. (2007) CpG oligodeoxynucleotide-enhanced humoral immune response and production of antibodies to prion protein PrPSc in mice immunized with 139A scrapie-associated fibrils. J. Leukocyte Biol. 81, 1374-1385
    • (2007) J. Leukocyte Biol. , vol.81 , pp. 1374-1385
    • Spinner, D.S.1    Kascsak, R.B.2    Lafauci, G.3    Meeker, H.C.4    Ye, X.5    Flory, M.J.6    Kim, J.I.7    Schuller-Levis, G.B.8    Levis, W.R.9    Wisniewski, T.10
  • 23
    • 77952061162 scopus 로고    scopus 로고
    • Reiterating the epitope specificity of prion-specific mAb 3F4
    • author reply le6
    • Kascsak, R. (2010) Reiterating the epitope specificity of prion-specific mAb 3F4. J. Biol. Chem. 285, le5, author reply le6
    • (2010) J. Biol. Chem. , vol.285
    • Kascsak, R.1
  • 24
  • 28
    • 4444356433 scopus 로고    scopus 로고
    • Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion
    • Pan, T., Li, R., Kang, S. C., Wong, B. S., Wisniewski, T. and Sy, M. S. (2004) Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion. J. Neurochem. 90, 1205-1217
    • (2004) J. Neurochem. , vol.90 , pp. 1205-1217
    • Pan, T.1    Li, R.2    Kang, S.C.3    Wong, B.S.4    Wisniewski, T.5    Sy, M.S.6
  • 29
    • 25144445814 scopus 로고    scopus 로고
    • An aggregation-specific enzyme-linked immunosorbent assay: Detection of conformational differences between recombinant PrP protein dimers and PrPSc aggregates
    • Pan, T., Chang, B., Wong, P., Li, C., Li, R., Kang, S. C., Robinson, J. D., Thompsett, A. R., Tein, P., Yin, S. et al. (2005) An aggregation-specific enzyme-linked immunosorbent assay: detection of conformational differences between recombinant PrP protein dimers and PrPSc aggregates. J. Virol. 79, 12355-12364
    • (2005) J. Virol. , vol.79 , pp. 12355-12364
    • Pan, T.1    Chang, B.2    Wong, P.3    Li, C.4    Li, R.5    Kang, S.C.6    Robinson, J.D.7    Thompsett, A.R.8    Tein, P.9    Yin, S.10
  • 31
    • 1542270865 scopus 로고    scopus 로고
    • Antigenic characterization of an abnormal isoform of prion protein using a new diverse panel of monoclonal antibodies
    • Kim, C. L., Umetani, A., Matsui, T., Ishiguro, N., Shinagawa, M. and Horiuchi, M. (2004) Antigenic characterization of an abnormal isoform of prion protein using a new diverse panel of monoclonal antibodies. Virology 320, 40-51
    • (2004) Virology , vol.320 , pp. 40-51
    • Kim, C.L.1    Umetani, A.2    Matsui, T.3    Ishiguro, N.4    Shinagawa, M.5    Horiuchi, M.6
  • 32
    • 15744401372 scopus 로고    scopus 로고
    • Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells
    • Feraudet, C., Morel, N., Simon, S., Volland, H., Frobert, Y., Creminon, C., Vilette, D., Lehmann, S. and Grassi, J. (2005) Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells. J. Biol. Chem. 280, 11247-11258
    • (2005) J. Biol. Chem. , vol.280 , pp. 11247-11258
    • Feraudet, C.1    Morel, N.2    Simon, S.3    Volland, H.4    Frobert, Y.5    Creminon, C.6    Vilette, D.7    Lehmann, S.8    Grassi, J.9
  • 35
    • 78049519681 scopus 로고    scopus 로고
    • Distinct stability states of disease-associated human prion protein identified by conformation-dependent immunoassay
    • Choi, Y. P., Peden, A. H., Groner, A., Ironside, J. W. and Head, M. W. (2010) Distinct stability states of disease-associated human prion protein identified by conformation-dependent immunoassay. J. Virol. 84, 12030-12038
    • (2010) J. Virol. , vol.84 , pp. 12030-12038
    • Choi, Y.P.1    Peden, A.H.2    Groner, A.3    Ironside, J.W.4    Head, M.W.5
  • 36
    • 80053451037 scopus 로고    scopus 로고
    • Protease-sensitive conformers in broad spectrum of distinct PrP structures in sporadic Creutzfeldt-Jakob disease are indicator of progression rate
    • Kim, C., Haldiman, T., Cohen, Y., Chen, W., Blevins, J., Sy, M. S., Cohen, M. and Safar, J. G. (2011) Protease-sensitive conformers in broad spectrum of distinct PrP structures in sporadic Creutzfeldt-Jakob disease are indicator of progression rate. PLoS Pathog. 7, e1002242
    • (2011) PLoS Pathog , vol.7
    • Kim, C.1    Haldiman, T.2    Cohen, Y.3    Chen, W.4    Blevins, J.5    Sy, M.S.6    Cohen, M.7    Safar, J.G.8
  • 37
    • 0030069023 scopus 로고    scopus 로고
    • Insoluble wild-type and protease-resistant mutant prion protein in brains of patients with inherited prion disease
    • Gabizon, R., Telling, G., Meiner, Z., Halimi, M., Kahana, I. and Prusiner, S. B. (1996) Insoluble wild-type and protease-resistant mutant prion protein in brains of patients with inherited prion disease. Nat. Med. 2, 59-64
    • (1996) Nat. Med. , vol.2 , pp. 59-64
    • Gabizon, R.1    Telling, G.2    Meiner, Z.3    Halimi, M.4    Kahana, I.5    Prusiner, S.B.6
  • 38
    • 0030902421 scopus 로고    scopus 로고
    • Identification of the prion protein allotypes which accumulate in the brain of sporadic and familial Creutzfeldt-Jakob disease patients
    • Silvestrini, M. C., Cardone, F., Maras, B., Pucci, P., Barra, D., Brunori, M. and Pocchiari, M. (1997) Identification of the prion protein allotypes which accumulate in the brain of sporadic and familial Creutzfeldt-Jakob disease patients. Nat. Med. 3, 521-525
    • (1997) Nat. Med. , vol.3 , pp. 521-525
    • Silvestrini, M.C.1    Cardone, F.2    Maras, B.3    Pucci, P.4    Barra, D.5    Brunori, M.6    Pocchiari, M.7
  • 41
    • 84857517525 scopus 로고    scopus 로고
    • Allelic origin of protease-sensitive and protease-resistant prion protein isoforms in Gerstmann-Straussler-Scheinker disease with the P102L mutation
    • Monaco, S., Fiorini, M., Farinazzo, A., Ferrari, S., Gelati, M., Piccardo, P., Zanusso, G. and Ghetti, B. (2012) Allelic origin of protease-sensitive and protease-resistant prion protein isoforms in Gerstmann-Straussler-Scheinker disease with the P102L mutation. PLoS ONE 7, e32382
    • (2012) PLoS ONE , vol.7
    • Monaco, S.1    Fiorini, M.2    Farinazzo, A.3    Ferrari, S.4    Gelati, M.5    Piccardo, P.6    Zanusso, G.7    Ghetti, B.8
  • 42
    • 80055066890 scopus 로고    scopus 로고
    • Copper alters aggregation behavior of prion protein and induces novel interactions between its Nand C-terminal regions
    • Thakur, A. K., Srivastava, A. K., Srinivas, V., Chary, K. V. and Rao, C. M. (2011) Copper alters aggregation behavior of prion protein and induces novel interactions between its Nand C-terminal regions. J. Biol. Chem. 286, 38533-38545
    • (2011) J. Biol. Chem. , vol.286 , pp. 38533-38545
    • Thakur, A.K.1    Srivastava, A.K.2    Srinivas, V.3    Chary, K.V.4    Rao, C.M.5
  • 43
    • 84873407042 scopus 로고    scopus 로고
    • Zinc drives a tertiary fold in the prion protein with familial disease mutation sites at the interface
    • Spevacek, A. R., Evans, E. G., Miller, J. L., Meyer, H. C., Pelton, J. G. and Millhauser, G. L. (2012) Zinc drives a tertiary fold in the prion protein with familial disease mutation sites at the interface. Structure 21, 236-246
    • (2012) Structure , vol.21 , pp. 236-246
    • Spevacek, A.R.1    Evans, E.G.2    Miller, J.L.3    Meyer, H.C.4    Pelton, J.G.5    Millhauser, G.L.6
  • 44
    • 0034682866 scopus 로고    scopus 로고
    • Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus
    • Li, R., Liu, T., Wong, B. S., Pan, T., Morillas, M., Swietnicki, W., O'Rourke, K., Gambetti, P., Surewicz, W. K. and Sy, M. S. (2000) Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus. J. Mol. Biol. 301, 567-573
    • (2000) J. Mol. Biol. , vol.301 , pp. 567-573
    • Li, R.1    Liu, T.2    Wong, B.S.3    Pan, T.4    Morillas, M.5    Swietnicki, W.6    O'Rourke, K.7    Gambetti, P.8    Surewicz, W.K.9    Sy, M.S.10
  • 45
    • 79955729783 scopus 로고    scopus 로고
    • Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target
    • Meli, M., Gasset, M. and Colombo, G. (2011) Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target. PLoS ONE 6, e19093
    • (2011) PLoS ONE , vol.6
    • Meli, M.1    Gasset, M.2    Colombo, G.3
  • 47
    • 77954238207 scopus 로고    scopus 로고
    • Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3
    • Adrover, M., Pauwels, K., Prigent, S., de Chiara, C., Xu, Z., Chapuis, C., Pastore, A. and Rezaei, H. (2010) Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3. J. Biol. Chem. 285, 21004-21012
    • (2010) J. Biol. Chem. , vol.285 , pp. 21004-21012
    • Adrover, M.1    Pauwels, K.2    Prigent, S.3    De Chiara, C.4    Xu, Z.5    Chapuis, C.6    Pastore, A.7    Rezaei, H.8
  • 48
    • 67650812321 scopus 로고    scopus 로고
    • Aptamers against prion proteins and prions
    • Gilch, S. and Schatzl, H. M. (2009) Aptamers against prion proteins and prions. Cell. Mol. Life Sci. 66, 2445-2455
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2445-2455
    • Gilch, S.1    Schatzl, H.M.2
  • 49
    • 28544443624 scopus 로고    scopus 로고
    • Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231
    • Apetri, A. C., Vanik, D. L. and Surewicz, W. K. (2005) Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231. Biochemistry 44, 15880-15888
    • (2005) Biochemistry , vol.44 , pp. 15880-15888
    • Apetri, A.C.1    Vanik, D.L.2    Surewicz, W.K.3
  • 50
    • 34250644988 scopus 로고    scopus 로고
    • 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, S. C., Biasini, E., Tien, P., Harris, D. A. and Sy, M. S. (2007) Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans. Proc. Natl. Acad. Sci. U.S.A. 104, 7546-7551
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7546-7551
    • Yin, S.1    Pham, N.2    Yu, S.3    Li, C.4    Wong, P.5    Chang, B.6    Kang, S.C.7    Biasini, E.8    Tien, P.9    Harris, D.A.10    Sy, M.S.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.