Prion (PrP(Sc))-specific epitope defined by a monoclonal antibody

Nature

Volumn 390, Issue 6655, 1997, Pages 74-77

  Korth, C ^a   Stierli, B ^a   Streit, P ^a   Moser, M ^a   Schaller, O ^a   Fischer, R ^b   Schulz Schaeffer, W ^c   Kretzschmar, H ^c   Raeber, A ^a   Braun, U ^a   Ehrensperger, F ^a   Hornemann, S ^b   Glockshuber, R ^b   Riek, R ^b   Billeter, M ^b   Wuthrich K ^b   Oesch, B ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

^b ETH ZURICH   (Switzerland)

^c UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; MONOCLONAL ANTIBODY; PRION PROTEIN; PROTEINASE K;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BOVINE SPONGIFORM ENCEPHALOPATHY; BRAIN HOMOGENATE; BRAIN SPONGIOSIS; CATTLE; CONTROLLED STUDY; CREUTZFELDT JAKOB DISEASE; HUMAN; HUMAN TISSUE; IMMUNOPRECIPITATION; MOUSE; MYELOMA CELL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRION; PRIORITY JOURNAL; PROTEIN CONFORMATION; SPLEEN CELL; AMINO ACID SEQUENCE; ANIMAL; ANTIBODY SPECIFICITY; CHEMICAL STRUCTURE; CHEMISTRY; EPITOPE MAPPING; IMMUNOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SERODIAGNOSIS; SPECIES DIFFERENCE;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIBODY SPECIFICITY; CATTLE; EPITOPE MAPPING; EPITOPES, B-LYMPHOCYTE; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PRECIPITIN TESTS; PRIONS; PRPSC PROTEINS; SPECIES SPECIFICITY;

EID: 0030613755     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/36337     Document Type: Article

References (27)

1. Pan, K. M. et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA 90, 10962-10966 (1993).
2. McKinley, M. P., Bolton, D. C. & Prusiner, S. B. A protease-resistant protein is a structural component of the scrapie prion. Cell 35, 57-62 (1983).
3. Oesch, B. et al. A cellular gene encodes scrapie PrP 27-30 protein. Cell 40, 735-746 (1985).
4. Daude, N., Lehmann, S. & Harris, D. A. Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J. Biol. Chem. 272, 11604-11612 (1997).
5. Fischer, M. et al. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 15, 1255-1264 (1996).
6. Mehlhorn, I. et al. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35, 5528-5537 (1996).
7. Weiss, S., Rieger, R., Edenhofer, F., Fisch, E. & Winnacker, E. L. Recombinant prion protein rPrP27-30 from Syrian golden hamster reveals proteinase K sensitivity. Biochem. Biophys. Res. Commun. 219, 173-179 (1996).
8. Kaneko, K. et al. Molecular properties of complexes formed between the prion protein and synthetic peptides. J. Mol. Biol. 270, 574-586 (1997).
9. Lansbury, P. T. & Caughey, B. The chemistry of scrapie infection: implications of the 'ice 9' metaphor. Chem. Biol. 2, 1-5 (1995).
10. Parchi, P. et al. Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann. Neurol. 39, 767-778 (1996).
11. Schätzl, H. M., Da Costa, M., Taylor, L., Cohen, F. E. & Prusiner, S. B. Prion protein gene variation among primates. J. Mol. Biol. 245, 362-374 (1995).
12. Riek, R. et al. NMR structure of the mouse prion protein domain PrP(121-231). Nature 382, 180-182 (1996).
13. Glockshuber, R. et al. Three-dimensional NMR structure of a self-folding domain of the prion protein PrP (121-231). Trends Biochem. Sci. 22, 241-242 (1997).
14. Telling, G. C. et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83, 79-900 (1995).
15. Billeter, M. et al. Prion protein NMR structure and species barrier for prion diseases. Proc. Natl Acad. Sci. USA 84, 7281-7285 (1997).
16. Warwicker, J. & Gane, P. J. A model for prion protein dimersization based on alpha-helical packing. Biochem. Biophys. Res. Commun. 226, 777-782 (1996).
17. Padian, E. A. & Love, W. E. Refined crystal structure of deoxyhemoglobin S. II. Molecular interactions in the crystal. J. Biol. Chem. 260, 8280-8291 (1985).
18. Huang, Z., Prusiner, S. B. & Cohen, F. E. Scrapie prions: a three-dimensional model of an infectious fragment. Fold. Design 1, 13-19 (1996).
19. Kitamoto, T., Mohri, S. & Tateishi, J. Organ distribution of proteinase-resistant prion protein in humans and mice with Creutzfeldt-Jakob disease. J. Gen. Virol. 70, 3371-3379 (1989).
20. Chandler, R. L. Encephalopathy in mice produced by inoculation with scrapie brain material. Lancet i, 1378-1379 (1961).
21. Goldmann, W., Hunter, N., Martin, T., Dawson, M. & Hope, J. Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein-coding exon. J. Gen. Virol. 72, 201-204 (1991).
22. Bueler, H. et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356, 577-582 (1992).
23. Kennett, R. H. Monoclonal Antibodies. Hybridomas: A New Dimension in Biological Analysis (eds Kennett, R. H., McKearn, T. J. & Bechtol, K. B.) 365-367 (Plenum, New York, 1980).
24. Oesch, B., Jensen, M., Nilsson, P. & Fogh, J. Properties of the scrapie prion protein: quantitative analysis of protease resistance. Biochemistry 33, 5926-5931 (1994).
25. Priola, S. A., Caughey, B., Wehrly, K. & Chesebro, B. A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP. J. Biol. Chem. 270, 3299-3305 (1995).
26. Riek, R., Hornemann, S., Wider, G., Glockshuber, R. & Wüthrich, K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413, 282-288 (1997).
27. Koradi, R., Billeter, M. & Wüthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55 (1996).