Oligomeric forms of peptide fragment PrP(214-226) in solution are preferentially recognized by PrPSc-specific antibody

Biochemical and Biophysical Research Communications

Volumn 344, Issue 4, 2006, Pages 1320-1326

  Ulrih, Nataša Poklar ^a   Skrt, Mihaela ^a   Veranič, Peter ^a   Galvani, Vesna ^b   Vranac, Tanja ^b   Šerbec, Vladka Čurin ^b  

^a UNIVERSITY OF LJUBLJANA   (Slovenia)

^b BLOOD TRANSFUSION CENTRE OF SLOVENIA   (Slovenia)

Author keywords

Amyloid like fibrils; Monoclonal PrPSc specific antibody; Prion protein; Specific epitope

Indexed keywords

MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY V5B2; OLIGOMER; PEPTIDE FRAGMENT; PEPTIDE P1; PRION PROTEIN; UNCLASSIFIED DRUG; EPITOPE; ISOPROTEIN; PRION PROTEIN (214 226); PRION PROTEIN (214-226);

ANTIBODY LABELING; ANTIBODY SPECIFICITY; ANTIGEN ANTIBODY REACTION; ANTIGEN RECOGNITION; ANTIGEN SPECIFICITY; ARTICLE; ENZYME LINKED IMMUNOSORBENT ASSAY; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE; TEMPERATURE SENSITIVITY; CHEMISTRY; CREUTZFELDT JAKOB DISEASE; DIMERIZATION; HUMAN; IMMUNOLOGY; PRION; SOLUTION AND SOLUBILITY; TEMPERATURE;

ANTIBODIES, MONOCLONAL; CREUTZFELDT-JAKOB SYNDROME; DIMERIZATION; HUMANS; HYDROGEN-ION CONCENTRATION; IMMUNODOMINANT EPITOPES; PEPTIDE FRAGMENTS; PRIONS; PROTEIN ISOFORMS; PRPSC PROTEINS; SOLUTIONS; TEMPERATURE;

EID: 33745998002     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.04.046     Document Type: Article

References (27)

1. Oesch B., Westaway D., Wälchli M., McKinley M.P., Kent S.B.H., Aebersold R., Barry R.A., Tempst P., Teplow D.B., Hood L.E., Prusiner S.B., and Weissmann C. A cellular gene encodes scrapie prp 27-30 protein. Cell 40 (1985) 735-746
2. McMeyer R.K., McKinly M.P., Bowman K.A., Braunfeld M.B., Barry R.A., and Prusiner S.B. Separation and properties of cellular and scrapie prion proteins. Proc. Natl. Acad. Sci. USA 83 (1986) 2310-2314
3. Pan K.-M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D., Mehlhorn I., Huang Z., Fletterick R.J., Cohen F., and Prusiner S.B. Conversion of alfa-helices into beta-sheets features in the formation of the scrapie prion protein. Proc. Natl. Acad. Sci. USA 90 (1993) 10962-10966
4. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA 95 (1998) 13363-13368
5. Riek R., Hornemann S., Wider G., Billeter M., Glockshuber R., and Wütrich K. NMR structure of the mouse prion protein domain PrP(121-231). Nature (London) 382 (1996) 180-182
6. Zahn R., Liu A., Luhrs T., Riek R., von Schroetter C., Garcia F.L., Billeter M., Calzolai L., Wider G., and Wütrich K. NMR solution structure of the human prion protein. Proc. Natl. Acad. Sci. USA 97 (2000) 145-149
7. Donne D.G., Viles J.H., Groth D., Mehlhorn I., James T.L., Cohen F.E., Prusiner F.S.B., Wright P.E., and Dyson H.J. Structure of the recombinant full-length hamster prion protein PrP(29-231). Proc. Natl. Acad. Sci. USA 94 (1997) 13452-13457
8. 2+ binding sites in the C-terminal domain of the murine prion protein: a pulse EPR and ENDOR study. J. Phys. Chem. B 105 (2001) 1631-1639
9. Govaerts C., Wille H., Prusiner S.B., and Cohen F.E. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl. Acad. Sci. USA 101 (2004) 8342-8347
10. Čurin-Šerbec V., Bresjanac M., Popović M., Pretnar-Hartman K., Galvani V., Rupreht R., Černilec M., Vranac T., Hafner I., and Jerala R. Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeldt-Jacob's disease-affected and normal brain tissue. J. Biol. Chem. 279 (2004) 3694-3698
11. Korth C., Stierli B., Streit P., Moser M., Schaller O., Fisher R., Schultz-Schaeffer W., Kretzschmar H.H., Raeber A., Braun U., Ehrensperger F., Hornemann S., Glockshuber R.R., Riek R., Billeter M., and Wütrich K. Prion (PrPSc)-specific epitope defined by monoclonal antibody. Nature 390 (1997) 74-77
12. Paramithiotis E., Pinard M., Lawton T., LaBoissiere S., Leathers V.L., Zou W.Q., Estey L.A., Lamontagne J., Lehto M.T., Kondejewski L.H., Francoeur G.P., Papadopoulos M., Haghighat A., Spatz S.J., Head M., Will R., Ironside J., O'Rourke K., Tonelli Q., Ledebur H.C., Chakrabartty A., and Cashman N.R. A prion protein epitope selective for the pathologically misfolded conformation. Nat. Med. 9 (2003) 893-899
13. R.C. Judd, The Protein Protocols Handbook: SDS-Polyacrylamide Gel Electrophoresis of Peptide, in: J.M. Walker (Ed.), Humana Press, Totowa, New Jersey, 1996, pp. 101-107.
14. Ellman G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82 (1959) 70-77
15. Adler A., Greenfield N.J., and Fasman G.D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. In: Hirsh C.H.V., and Timasheff S.D. (Eds). Methods in Enzymology 27 (1973), Academic Press, New York 657-735
16. Sreerama N., and Woody R.W. Circular dichroism of peptides and proteins. In: Berova N., Nakanishi K., and Woody R.W. (Eds). Circular Dichroism: Principles and Applications (2000), A John Willey & Sons Inc Publication, New York 601-620
17. Cantor C.R., and Schimmel P.R. The behaviour of biological macromolecules (part III). Biophysical Chemistry (1980), W.H. Freeman and Company, San Francisco 1041-1073
18. Zou W.-Q., Yang D.-S., Fraser P.E., Cashman N.R., and Chakrabartty A. All or none fibrillogenesis of prion peptide. Eur. J. Biochem. 268 (2001) 4885-4891
19. ox. Eur. J. Biochem. 268 (2001) 5930-5936
20. Jamin N., Coic Y.-M., Landon C., Ovtracht L., Baleux F., Neumann J.-M., and Sanson A. Most of the structural elements of the globular domain of murine prion protein form fibrils with predominant β-sheet structure. FEBS Lett. 529 (2002) 256-260
21. Hornemann S., and Glockshuber R. A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acid pH. Proc. Natl. Acad. Sci. USA 95 (1998) 6010-6014
22. Swietnicki W., Morillas M., Chen S.G., Gambetti P., and Surewicz W.K. Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry 39 (2000) 424-431
23. Sc?. Biochemistry 41 (2002) 12277-12283
24. Knaus K.J., Morillas M., Swietnicki W., Malone M., Surewicz W., and Yee V.C. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat. Struct. Biol. 8 (2001) 770-774
25. Kallberg Y., Gustafsson M., Persson B., Thyberg J., and Johnsson J. Prediction of amyloid fibril-forming proteins. J. Biol. Chem. 276 (2001) 12945-12950
26. C to form β sheet using NMR structures and sequence alignments. Biophys. J. 83 (2002) 1268-1280
27. Nelsom R., Sawaya M.R., Balbirnie M., Madsen A.Ø., Riekel C., Grothe R., and Eisenberg D. Structure of the cross-β spine of amyloid-like fibrils. Nature 435 (2005) 773-777