Drug – bio-affecting and body treating compositions – In vivo diagnosis or in vivo testing – Testing efficacy or toxicity of a compound or composition
Reexamination Certificate
2011-01-25
2011-01-25
Swartz, Rodney P. (Department: 1645)
Drug, bio-affecting and body treating compositions
In vivo diagnosis or in vivo testing
Testing efficacy or toxicity of a compound or composition
C424S009100, C424S130100, C424S184100, C424S185100, C424S278100, C435S325000, C530S300000, C530S350000
Reexamination Certificate
active
07875259
ABSTRACT:
The present invention relates to a method of making a β-form of a prion protein which preferably has more β-sheet than α-helix structure and is soluble in the absence of a denaturant and/or is non-aggregated and exhibits partial resistance to digestion with proteinase K. The invention also relates to use of the β-form in medicine, especially for raising antibodies useful in the treatment and/or diagnosis of prion diseases. The invention also relates to methods of screening for compounds which are capable of inhibiting and/or reversing the conversion of the native α-form of a prion protein to a β-form, and to uses of identified compounds in medicine.
REFERENCES:
patent: 5846533 (1998-12-01), Prusiner et al.
patent: 302 473 (1989-08-01), None
patent: 0 861 900 (1997-02-01), None
patent: 815 872 (1998-07-01), None
patent: WO 88/07378 (1988-10-01), None
patent: WO 91/11201 (1991-08-01), None
patent: WO 93/23432 (1993-11-01), None
patent: WO 96/39834 (1996-12-01), None
patent: WO 98/16834 (1998-04-01), None
patent: WO 98/20022 (1998-05-01), None
patent: WO 98/30909 (1998-07-01), None
patent: WO 98/37210 (1998-08-01), None
patent: WO 98/37411 (1998-08-01), None
patent: WO 98/55132 (1998-12-01), None
Collinge et al. (1995)Lancet346:569-570.
Collinge et al. (1996)Nature383:685-690.
Devereux et al. (1984)Nucl. Acids Res.12:387.
Eliezer D., Yao J., Dyson H.J. & Wright P.E. (1998)Nat. Struct. Biol. 5:148-155.
Ezzeddine et al. (1991)New Biol. 3:608.
Fink (1998)Folding and Design3:R9-23.
Gioia et al. (1994)Journal of Biological Chemistry, 269:7859-7862.
Fink (1997)Folding and Design3:19-25.
Fischer (1996)EMBO J.15:1255:1264.
Hawke et al. (1992)J. Immunol. Methods155:41-48.
Hnatowich et al. (1988)J. Nuclear Medicine. 29:1428-1434.
Hornemann S. & Glockshuber R. (1996)J. Mol. Biiol. 261:614-619.
Hornemann S. & Glockshuber R. (1998)Proc. Natl. Acad. Sci. USA95:6010-6014.
Jackson et al (1999)Science283:1935-7.
James T.L., Liu H., Ulyanov N.B. et al. (1997)Proc. Natl. Acad. Sci. USA94:10086-10091.
Korth et al. (1997)Nature390:74-77.
Leo et al. (1987)Proc. Natl. Acad. Sci. USA84:1374-78.
Mehlhorn et al. (1996)Biochem35:5528-37.
Moolten (1986)Cancer Res. 46:5276.
Michael A. Baldwin, Fred E. Cohen and Stanley B. Prusiner, “Prion Protein Isoforms, a Convergence of Biological and Structural Investigations”,Minireview, The Journal of Biological ChemistryXP-002074799, vol. 270, No. 33, Aug. 18, 1995, pp. 19197-19200.
Tamaki Muramoto, Michael Scott, Fred E. Cohen and Stanley B. Prusiner, “Recombinant Scrapie-Like Prion Protein of 106 Amino Acids is Soluble”,Neurobiology, Proc. Natl. Acad. Sci, USA, vol. 93, pp. 15457-15462, Dec. 1996.
Neuberger et al. (1984)Nature312:604.
Paganelli et al. (1990)Int. J. Cancer, 45:1184-1189.
Pan K.M., Baldwin M.A., Nguyen J., et al. (1993)Proc. Natl. Acad. Sci. USA, 90:10962-10966.
Prusiner S.B. (1991)Science, 252:1515-1522.
Ptitsyn O.B. (1994)Protein Eng. 7:593-596.
Ptitsyn O.B. (1995)Adv. Protein Chem. 47:83-229.
Ptitsyn O.B. (1995)Curr. Opin. Struct. Biol. 5:74-78.
Ptitsyn O.B. [news] (1996)Nat. Struct. Biol. 3:488-490.
Ptitsyn O.B. et al. (1995)Philo. Trans. R. Soc. Land. B. Biol Sci; 348:35041.
Riek R., Hornemann S., Wider G., Billeter M., Glockshuber R. & Wuthrich K. (1996)Nature382:180-182(PRIVATE).
Safar et al. (1993)J. Biol. Chem268:20276-20284.
Senter (1988)Proc. Natl. Acad. Sci. USA85:4842.
Shyng et al. (1993)J. Biol. Chem. 268:15922-8.
Swietnicki et al. (1993)J. Biol. Chem. 272(44):27517-27520.
Swietnicki et al. (2000)J. Biol. Chem. 39:424-431.
Zahn R., Von Schroetter C. & Wüthrich K. (1997)FEBS Lett. 417:400-404.
Zhan et al. (1994)Biochem. 33:11254-63.
Zhang et al. (1997)Biochem. 36(12):3543-3553.
Scott et al, “Identification of a Prion Protein Epitope Modulating Transmission of Bovine Spongiform Encephalopathy Prions to Transgenic Mice”, Proc. Nat'l. Acad. Sci. USA, vol. 94, pp. 14279-14284, Dec. 1997.
Hosszu et al, “Structural Mobility of the Human Prion Protein Probed by Backbone Hydrogen Exchange”,Nature Structural Biology, vol. 6, No. 8, pp. 740-743, Aug. 1999.
P.M. Harrison et al, “The Prion Folding Problem”,Current Opinion in Structural Biology, 1997, vol. 7, pp. 53-59.
Jack Nguyen, Michael A. Baldwin, Fred E. Cohen and Stanley B. Prusiner, “Prion Protein Induce α-Helix to β-Sheet Conformational Transitions”, Biochemistry 1995, 34, pp. 4186-4192.
Alexandrescu, A.T., Evans, P.A., Pitkeathly, M., Baum, J. & Dobson, C.M. (1993)Biochemistry32:1707-1718.
Bagshawe (1987)Brit. J. Cancer56:531.
Bagshawe et al. (1988)Brit. J. Cancer58:700.
Büeler (1992)Nature356:577-582.
Bridgewater et al. (1995)Eur. J. Cancer31A:2362-2370.
Chen Y.H., Yang J.T. & Martinex H.M. (1972)Biochemistry11:4120-4131.
Chyan C.L., Wornald C., Dobson C.M., Evans, P.A. & Baum J. (1993)Biochemistry, 32:5681-5691.
Clarke A.R. & Waltho J.P. (1997)Curr. Opin. Biotechnol. 8:400-410.
Collinge J. (1997)Hum. Mol. Genetics6:1699-1705.
Collinge J., Palmer M.S. & Dryden A.J. (1991)Lancet337:1441-1442.
Heppner et al, “Prevention of Scrapie Pathogenesis by Transgenic Expression of Anti-Prion Protein”,Science, vol. 294, pp. 178-182, Oct. 5, 2001.
Bendheim et al., Antibodies to a Scrapie Prion Protein, Nature, 1984, 310:418-421 (Abstract only).
Beringue et al., Regional Heterogeneity of Cellular Prion Protein Isoforms in the Mouse Brain, Brain, 2003, 126:2065-2073.
Beringue et al., PrPSc Binding Antibodies are Potent Inhibitors of Prion Replication in Cell Lines, JBC, 2004, 279:39671-39676.
Butler et al., Scrapie-infected Murine Neuroblastoma Cells Produce Protease-Resistant Prion Proteins, J Virol, 1998, 62:1558-1564.
Chiswell & McCafferty, Phage Antibodies: Will New ‘coliclonal’ Antibodies Replace monoclonal Antibodies?, Trends Biotechnol, 1992, 10:80-84.
Gabizon et al., Immunoaffinity Purification and Neutralization of Scrapie Prion Infectivity, PNAS, 1998, 85:6617-6621.
Khalili-Shirazi et al., Protein Conformation Significantly Influences Immune Responses to Prion Protein, J. Immunol, 2005, 174:3256-3263.
Khalili-Shirazi et al., PrP Glycoforms are Associated in a Strain-specific Ratio in native PrPSc, J Gen Virol, 2005, 86:2635-2644.
Khalili-Shirazi et al., β-PrP Form of Human Prion Protein Stimulates Production of Monoclonal . . . , J. Biochim Biophys Acta, 2007, 1774:1438-1450.
Ptitsyn et al., The Molten Globule is a Third Thermodynamical State of Protein Molecules, FEBS Letters, 1994, 341:15-18.
White et al., Monoclonal Antibodies Inhibit Prion Replication and Delay the Development of Prion Disease, Nature, 2003, 422:80-83.
Clarke Anthony R.
Collinge John
Jackson Graham S.
D-Gen Limited
Mersereau C. G.
Nikolai & Mersereau , P.A.
Swartz Rodney P.
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