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Volumn 27, Issue 11, 2006, Pages 2695-2705

A single prion protein peptide can elicit a panel of isoform specific monoclonal antibodies

Author keywords

Anti TSE vaccine; Epitope conformation; Immune tolerance; Monoclonal antibody; Peptide antigen; Prion protein

Indexed keywords

ASPARTYLGLUTAMYLTYROSYLSERYLASPARAGINYLGLUTAMINYLASPARAGINYLASPARAGINYL PHENYLALANYLVALYLHISTIDYLASPARTYLCYSTEINYL; CYSTEINYLISOLEUCYLHISTIDYLPHENYLALANYLGLYCYLSERYLASPARTYLTYROSYLGLUTAMYL ASPARTYLARGINYLTYROSYLTYROSYL; CYSTEINYLISOLEUCYLTHREONYLGLUTAMINYLTYROSYLGLUTAMYLARGINYLGLUTAMYLSERYL GLUTAMINYLALANYLTYROSYLTYROSYL; HEMOCYANIN; IMMUNOGLOBULIN G ANTIBODY; MONOCLONAL ANTIBODY; PEPTIDE; PRION PROTEIN; PROTEIN ANTIBODY; UNCLASSIFIED DRUG;

EID: 33750081141     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2006.05.026     Document Type: Article
Times cited : (12)

References (36)
  • 2
    • 4544359288 scopus 로고    scopus 로고
    • PrPSc binding antibodies are potent inhibitors of prion replication in cell lines
    • Beringue V., Vilette D., Mallinson G., Archer F., Kaisar M., Tayebi M., et al. PrPSc binding antibodies are potent inhibitors of prion replication in cell lines. J Biol Chem 279 38 (2004) 39671-39676
    • (2004) J Biol Chem , vol.279 , Issue.38 , pp. 39671-39676
    • Beringue, V.1    Vilette, D.2    Mallinson, G.3    Archer, F.4    Kaisar, M.5    Tayebi, M.6
  • 3
    • 0041315527 scopus 로고    scopus 로고
    • Influence of pH on NMR structure and stability of the human prion protein globular domain
    • Calzolai L., and Zahn R. Influence of pH on NMR structure and stability of the human prion protein globular domain. J Biol Chem 278 37 (2003) 35592-35596
    • (2003) J Biol Chem , vol.278 , Issue.37 , pp. 35592-35596
    • Calzolai, L.1    Zahn, R.2
  • 4
    • 6444225674 scopus 로고    scopus 로고
    • Prion diseases-close to effective therapy?
    • Cashman N.R., and Caughey B. Prion diseases-close to effective therapy?. Nat Rev Drug Discov 3 10 (2004) 874-884
    • (2004) Nat Rev Drug Discov , vol.3 , Issue.10 , pp. 874-884
    • Cashman, N.R.1    Caughey, B.2
  • 5
    • 3543030409 scopus 로고    scopus 로고
    • Hydration and packing effects on prion folding and beta-sheet conversion. High pressure spectroscopy and pressure perturbation calorimetry studies
    • Cordeiro Y., Kraineva J., Ravindra R., Lima L.M., Gomes M.P., Foguel D., et al. Hydration and packing effects on prion folding and beta-sheet conversion. High pressure spectroscopy and pressure perturbation calorimetry studies. J Biol Chem 279 31 (2004) 32354-32359
    • (2004) J Biol Chem , vol.279 , Issue.31 , pp. 32354-32359
    • Cordeiro, Y.1    Kraineva, J.2    Ravindra, R.3    Lima, L.M.4    Gomes, M.P.5    Foguel, D.6
  • 6
    • 9144258359 scopus 로고    scopus 로고
    • Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeldt-Jakob disease-affected and normal brain tissue
    • Čurin Šerbec V., Bresjanac M., Popović M., Pretnar Hartman K., Galvani V., Rupreht R., et al. Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeldt-Jakob disease-affected and normal brain tissue. J Biol Chem 279 5 (2004) 3694-3698
    • (2004) J Biol Chem , vol.279 , Issue.5 , pp. 3694-3698
    • Čurin Šerbec, V.1    Bresjanac, M.2    Popović, M.3    Pretnar Hartman, K.4    Galvani, V.5    Rupreht, R.6
  • 7
    • 7444240183 scopus 로고    scopus 로고
    • Probing the instabilities in the dynamics of helical fragments from mouse PrPC
    • Dima R.I., and Thirumalai D. Probing the instabilities in the dynamics of helical fragments from mouse PrPC. Proc Natl Acad Sci USA 101 43 (2004) 15335-15340
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.43 , pp. 15335-15340
    • Dima, R.I.1    Thirumalai, D.2
  • 8
    • 0035979274 scopus 로고    scopus 로고
    • Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody
    • Enari M., Flechsig E., and Weissmann C. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc Natl Acad Sci USA 98 16 (2001) 9295-9299
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.16 , pp. 9295-9299
    • Enari, M.1    Flechsig, E.2    Weissmann, C.3
  • 9
    • 0026656122 scopus 로고
    • Spot-synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support
    • Frank R. Spot-synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron 48 22 (1992) 9217-9232
    • (1992) Tetrahedron , vol.48 , Issue.22 , pp. 9217-9232
    • Frank, R.1
  • 10
    • 20444471962 scopus 로고    scopus 로고
    • Genetic risk factors associated with Creutzfeld-Jakob disease in Slovenians and a rapid typing for PRNP codon 129 single nucleotide polymorphism
    • Galvani V., Rupreht R.R., Čurin Šerbec V., and Vidan-Jeras B. Genetic risk factors associated with Creutzfeld-Jakob disease in Slovenians and a rapid typing for PRNP codon 129 single nucleotide polymorphism. Transfus Med 15 3 (2005) 197-207
    • (2005) Transfus Med , vol.15 , Issue.3 , pp. 197-207
    • Galvani, V.1    Rupreht, R.R.2    Čurin Šerbec, V.3    Vidan-Jeras, B.4
  • 11
    • 0038692924 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the unfolding of the human prion protein domain under low pH and high temperature conditions
    • Gu W., Wang T., Zhu J., Shi Y., and Liu H. Molecular dynamics simulation of the unfolding of the human prion protein domain under low pH and high temperature conditions. Biophys Chem 104 1 (2003) 79-94
    • (2003) Biophys Chem , vol.104 , Issue.1 , pp. 79-94
    • Gu, W.1    Wang, T.2    Zhu, J.3    Shi, Y.4    Liu, H.5
  • 12
    • 0031957898 scopus 로고    scopus 로고
    • Synthetic peptide vaccines yield monoclonal antibodies to cellular and pathological prion proteins of ruminants
    • Harmeyer S., Pfaff E., and Groschup M.H. Synthetic peptide vaccines yield monoclonal antibodies to cellular and pathological prion proteins of ruminants. J Gen Virol 79 (1998) 937-945
    • (1998) J Gen Virol , vol.79 , pp. 937-945
    • Harmeyer, S.1    Pfaff, E.2    Groschup, M.H.3
  • 13
    • 0032568592 scopus 로고    scopus 로고
    • A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH
    • Hornemann S., and Glockshuber R. A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc Natl Acad Sci USA 95 11 (1998) 6010-6014
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.11 , pp. 6010-6014
    • Hornemann, S.1    Glockshuber, R.2
  • 14
    • 4444345862 scopus 로고    scopus 로고
    • Neuropathological lesions in the first case of bovine spongiform encephalopathy in Slovenia
    • [English edition]
    • Juntes P., Zabavnik Piano J., Čurin Šerbec V., Kovač Z., and Pogačnik M. Neuropathological lesions in the first case of bovine spongiform encephalopathy in Slovenia. S:lo Vet Res 39 2 (2002) 105-114 [English edition]
    • (2002) S:lo Vet Res , vol.39 , Issue.2 , pp. 105-114
    • Juntes, P.1    Zabavnik Piano, J.2    Čurin Šerbec, V.3    Kovač, Z.4    Pogačnik, M.5
  • 15
    • 0030931519 scopus 로고    scopus 로고
    • Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
    • Kaneko K., Zulianello L., Scott M., Cooper C.M., Wallace A.C., James T.L., et al. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc Natl Acad Sci USA 94 19 (1997) 10069-10074
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.19 , pp. 10069-10074
    • Kaneko, K.1    Zulianello, L.2    Scott, M.3    Cooper, C.M.4    Wallace, A.C.5    James, T.L.6
  • 16
  • 17
    • 0030613755 scopus 로고    scopus 로고
    • Prion (PrPSc)-specific epitope defined by a monoclonal antibody
    • Korth C., Stierli B., Streit P., Moser M., Schaller O., Fischer R., et al. Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature 390 (1997) 74-77
    • (1997) Nature , vol.390 , pp. 74-77
    • Korth, C.1    Stierli, B.2    Streit, P.3    Moser, M.4    Schaller, O.5    Fischer, R.6
  • 18
    • 4544335297 scopus 로고    scopus 로고
    • Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding
    • Kuczius T., Buschmann A., Zhang W., Karch H., Becker K., Peters G., et al. Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding. Biol Chem 385 8 (2004) 739-747
    • (2004) Biol Chem , vol.385 , Issue.8 , pp. 739-747
    • Kuczius, T.1    Buschmann, A.2    Zhang, W.3    Karch, H.4    Becker, K.5    Peters, G.6
  • 19
    • 0037195113 scopus 로고    scopus 로고
    • JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors
    • Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., and Reddy E.P. JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors. Proc Natl Acad Sci USA 99 22 (2002) 14189-14194
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.22 , pp. 14189-14194
    • Lee, C.M.1    Onesime, D.2    Reddy, C.D.3    Dhanasekaran, N.4    Reddy, E.P.5
  • 20
    • 0021645733 scopus 로고
    • Antibodies of predetermined specificity in biology and medicine
    • Lerner R.A. Antibodies of predetermined specificity in biology and medicine. Adv Immunol 36 (1984) 1-44
    • (1984) Adv Immunol , vol.36 , pp. 1-44
    • Lerner, R.A.1
  • 22
    • 1942533390 scopus 로고    scopus 로고
    • Effects of different experimental conditions on the PrPSc core generated by protease digestion: implications for strain typing and molecular classification of CJD
    • Notari S., Capellari S., Giese A., Westner I., Baruzzi A., Ghetti B., et al. Effects of different experimental conditions on the PrPSc core generated by protease digestion: implications for strain typing and molecular classification of CJD. J Biol Chem 279 16 (2004) 16797-16804
    • (2004) J Biol Chem , vol.279 , Issue.16 , pp. 16797-16804
    • Notari, S.1    Capellari, S.2    Giese, A.3    Westner, I.4    Baruzzi, A.5    Ghetti, B.6
  • 23
    • 0038717543 scopus 로고    scopus 로고
    • A prion protein epitope selective for the pathologically misfolded conformation
    • Paramithiotis E., Pinard M., Lawton T., LaBoissiere S., Leathers V.L., Zou W.Q., et al. A prion protein epitope selective for the pathologically misfolded conformation. Nat Med 9 7 (2003) 893-899
    • (2003) Nat Med , vol.9 , Issue.7 , pp. 893-899
    • Paramithiotis, E.1    Pinard, M.2    Lawton, T.3    LaBoissiere, S.4    Leathers, V.L.5    Zou, W.Q.6
  • 24
    • 0035899413 scopus 로고    scopus 로고
    • Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
    • Peretz D., Williamson R.A., Kaneko K., Vergara J., Leclerc E., Schmitt-Ulms G., et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412 6848 (2001) 739-743
    • (2001) Nature , vol.412 , Issue.6848 , pp. 739-743
    • Peretz, D.1    Williamson, R.A.2    Kaneko, K.3    Vergara, J.4    Leclerc, E.5    Schmitt-Ulms, G.6
  • 25
    • 2942738331 scopus 로고
    • Production and characterisation of synthetic peptide-derived antibodies
    • Ritter M.A., and Ladyman (Eds), Cambridge University Press
    • Price K.M. Production and characterisation of synthetic peptide-derived antibodies. In: Ritter M.A., and Ladyman (Eds). Monoclonal antibodies: production, engineering and clinical application (1995), Cambridge University Press 60-84
    • (1995) Monoclonal antibodies: production, engineering and clinical application , pp. 60-84
    • Price, K.M.1
  • 27
    • 0034856996 scopus 로고    scopus 로고
    • Modulation of proteinase-K resistant prion protein by prion peptide immunization
    • Souan L., Tal Y., Felling Y., Cohen I.R., Taraboulos A., and Mor F. Modulation of proteinase-K resistant prion protein by prion peptide immunization. Eur J Immunol 31 8 (2001) 2338-2346
    • (2001) Eur J Immunol , vol.31 , Issue.8 , pp. 2338-2346
    • Souan, L.1    Tal, Y.2    Felling, Y.3    Cohen, I.R.4    Taraboulos, A.5    Mor, F.6
  • 28
    • 0030781922 scopus 로고    scopus 로고
    • pH-Dependent stability and conformation of the recombinant human prion protein PrP(90-231)
    • Swietnicki W., Petersen R., Gambetti P., and Surewicz W.K. pH-Dependent stability and conformation of the recombinant human prion protein PrP(90-231). J Biol Chem 272 44 (1997) 27517-27520
    • (1997) J Biol Chem , vol.272 , Issue.44 , pp. 27517-27520
    • Swietnicki, W.1    Petersen, R.2    Gambetti, P.3    Surewicz, W.K.4
  • 30
    • 33745998002 scopus 로고    scopus 로고
    • Oligomeric forms of peptide fragment PrP(214-226) in solution are preferentially recognized by PrP(Sc)-specific antibody
    • Ulrih N.P., Skrt M., Veranic P., Galvani V., Veranič T., and Čurin Šerbec V. Oligomeric forms of peptide fragment PrP(214-226) in solution are preferentially recognized by PrP(Sc)-specific antibody. Biochem Biophys Res Commun 344 4 (2006) 1320-1326
    • (2006) Biochem Biophys Res Commun , vol.344 , Issue.4 , pp. 1320-1326
    • Ulrih, N.P.1    Skrt, M.2    Veranic, P.3    Galvani, V.4    Veranič, T.5    Čurin Šerbec, V.6
  • 31
    • 0000237623 scopus 로고
    • Antigenic cross-reactivity between proteins and peptides: new insights and applications
    • Van Regenmortel M.H.V. Antigenic cross-reactivity between proteins and peptides: new insights and applications. Trends Biochem Sci 12 (1987) 237-240
    • (1987) Trends Biochem Sci , vol.12 , pp. 237-240
    • Van Regenmortel, M.H.V.1
  • 32
    • 0002597936 scopus 로고
    • Which structural features determine protein antigenicity?
    • Van Regenmortel M.H.V. Which structural features determine protein antigenicity?. Trends Biochem Sci 11 (1986) 36-39
    • (1986) Trends Biochem Sci , vol.11 , pp. 36-39
    • Van Regenmortel, M.H.V.1
  • 33
    • 0041731605 scopus 로고    scopus 로고
    • Antimalarial drug quinacrine binds to C-terminal helix of cellular prion protein
    • Vogtherr M., Grimme S., Elshorst B., Jacobs D.M., Fiebig K., Griesinger C., et al. Antimalarial drug quinacrine binds to C-terminal helix of cellular prion protein. J Med Chem 46 17 (2003) 3563-3564
    • (2003) J Med Chem , vol.46 , Issue.17 , pp. 3563-3564
    • Vogtherr, M.1    Grimme, S.2    Elshorst, B.3    Jacobs, D.M.4    Fiebig, K.5    Griesinger, C.6
  • 34
    • 0036734612 scopus 로고    scopus 로고
    • Purification and identification of secernin, a novel cytosolic protein that regulates exocytosis in mast cells
    • Way G., Morrice N., Smythe C., and O'Sullivan A.J. Purification and identification of secernin, a novel cytosolic protein that regulates exocytosis in mast cells. Mol Biol Cell 13 9 (2002) 3344-3354
    • (2002) Mol Biol Cell , vol.13 , Issue.9 , pp. 3344-3354
    • Way, G.1    Morrice, N.2    Smythe, C.3    O'Sullivan, A.J.4
  • 35
    • 0037422133 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit prion replication and delay the development of prion disease
    • White A.R., Enever P., Tayebi M., Mushens R., Linehan J., Brandner S., et al. Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 422 6927 (2003) 80-83
    • (2003) Nature , vol.422 , Issue.6927 , pp. 80-83
    • White, A.R.1    Enever, P.2    Tayebi, M.3    Mushens, R.4    Linehan, J.5    Brandner, S.6
  • 36
    • 0028961050 scopus 로고
    • Preparation and characterization of antibodies against mouse prion protein (PrP) peptides
    • Yokoyama T., Kimura K., Tagawa Y., and Yuasa N. Preparation and characterization of antibodies against mouse prion protein (PrP) peptides. Clin Diagn Lab Immunol 2 2 (1995) 172-176
    • (1995) Clin Diagn Lab Immunol , vol.2 , Issue.2 , pp. 172-176
    • Yokoyama, T.1    Kimura, K.2    Tagawa, Y.3    Yuasa, N.4


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