Sodium dodecyl sulfate compositions for inactivating prions

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Radical -xh acid – or anhydride – acid halide or salt thereof...

Reexamination Certificate

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C514S558000, C424S405000, C426S335000, C426S532000

Reexamination Certificate

active

06720355

ABSTRACT:

FIELD OF THE INVENTION
The present invention relates generally to compositions for inactivating infectious prions on infected surfaces and in a range of different products including, blood, organ and tissue products, food products and livestock feed.
BACKGROUND OF THE INVENTION
Antiseptic compositions have been known for over 100 years. In addition to various compositions there are a range of different methods, which are known to be effective in killing bacteria and inactivating viruses. Such methods include the use of high temperature, alone or in combination with radiation, over sufficient periods of time to kill bacteria or disrupt viruses and thereby inactivate them. These methods are extreme, and can damage sensitive medical equipment, thus decreasing its useful life.
Examples of fast acting topical antiseptic compositions are disclosed n U.S. Pat. No. 6,110,908, issued Aug. 29, 2000. Another antibacterial composition is disclosed in U.S. Pat. No. 6,025,312, issued Feb. 15, 2000. Examples of other antiseptic compositions are taught within U.S. Pat. Nos. 5,336,432, issued Aug. 9, 1994; U.S. Pat. No. 5,308,611, issued May 3, 1994; U.S. Pat. No. 6,106,773, issued Aug. 22, 2000 and U.S. Pat. No. 6,096,216, issued Aug. 1, 2000.
Conventional antiseptic compositions and antiseptic methodologies are generally insufficient for inactivating infectious proteins such as prions. Although prions can be inactivated by relatively high temperatures over very long periods of time, the temperature ranges and time periods generally used to kill bacteria and inactivate the viruses are insufficient to inactivate prions. One approach to solving this problem is to attempt to remove prions from solutions. A chromographic removal process is disclosed within U.S. Pat. No. 5,808,011. Further, others have attempted to provide compositions and methodologies that are intended to inactivate prions as taught within U.S. Pat. No. 5,633,349. However, such processes generally take relatively long periods of time (e.g., more than 12 hours) and generally do not provide a solution that could be readily and economically utilized in order to inactivate prions on food products, biological materials, medical equipment, and livestock feed.
The present invention offers antiseptic compositions and methods, which may be utilized under mild conditions, for inactivating prions that will not damage any existing equipment, food, or biological substance, as described below.


REFERENCES:
patent: 4300905 (1981-11-01), Bleisteiner et al.
patent: 4320086 (1982-03-01), Reiss
patent: 4587329 (1986-05-01), Tomalia et al.
patent: 4806627 (1989-02-01), Wisniewski et al.
patent: 5308611 (1994-05-01), Thompson
patent: 5336432 (1994-08-01), Petchul et al.
patent: 5499979 (1996-03-01), Wong et al.
patent: 5521060 (1996-05-01), Hoenes et al.
patent: 5547576 (1996-08-01), Onishi et al.
patent: 5565186 (1996-10-01), Prusiner et al.
patent: 5633349 (1997-05-01), Reichl
patent: 5757361 (1998-05-01), Hirshik
patent: 5780288 (1998-07-01), Rohwer
patent: 5808011 (1998-09-01), Gawryl et al.
patent: 5834020 (1998-11-01), Margerum et al.
patent: 5846533 (1998-12-01), Prusiner et al.
patent: 5858326 (1999-01-01), Kislievsky et al.
patent: 5919442 (1999-07-01), Yin et al.
patent: 5977324 (1999-11-01), Prusiner et al.
patent: 6025312 (2000-02-01), Saito et al.
patent: 6096216 (2000-08-01), Shanbrom et al.
patent: 6106773 (2000-08-01), Miekka et al.
patent: 6110908 (2000-08-01), Guthery
patent: 6127448 (2000-10-01), Domb
patent: 6150172 (2000-11-01), Schmerr et al.
patent: 6190650 (2001-02-01), Matthews et al.
patent: 6197207 (2001-03-01), Chapman et al.
patent: 6197935 (2001-03-01), Doillon et al.
patent: 1244759 (1988-11-01), None
patent: 3229097 (1984-02-01), None
patent: WO 93/10227 (1993-05-01), None
patent: WO 93/23432 (1993-11-01), None
patent: WO 95/31466 (1995-11-01), None
patent: WO 97/43649 (1997-11-01), None
patent: WO 98/15297 (1998-04-01), None
patent: WO 98/32334 (1998-07-01), None
patent: WO 98/37411 (1998-08-01), None
patent: WO 99/42102 (1999-08-01), None
patent: WO 99/42487 (1999-08-01), None
patent: WO 00/65344 (2000-11-01), None
patent: WO 00/72851 (2000-12-01), None
West et al: Textbook of Biochemistry: Proteins p. 342-346, 326, 1966.*
Alpatova, N.M., et al., (1994) “Comparison of Electrochemical Behavior of Heteropolyacids in Solution and Immobilized in a Conducting Polymer Film,” Chemical Abstracts, vol. 121, No. 16.
Anderson, et al., (1996) “Transmission dynamics and epidemiology of BSE in British cattle,” Nature 382: 779-88.
Barry, R.A., et al., (1986) “Monoclonal Antibodies to the Cellular and Scrapie Prion Proteins,” Journal of Infectious Diseases 154:518-521.
Basler, et al., (1986) “Scrapie and Cellular PrP Isoforms Are Encoded by the Same Chromosomal Gene,” Cell, 46:417-28.
Bendheim, et al., (1984) “Antibodies to a Scrapie Prior Protein,” Nature 310:418-421.
Bode, et al., (1985) “Characterization of Antisera Against Scrapie-Associated Fibrils (SAF) from Affected Hamster and Cross-Reactivity with SAF from Scarpie-Affected Mice and from Patients with Creutzfeldt-Jacob Disease,” J. Gen. Virol. 66:2471-2478.
Bolton, et al., (1982) “Identification of a Protein That Purifies with the Scrapie Prion,” Science 218: 1309-11.
Brown, et al., (1992) “‘Friendly Fire’ in Medicine: Hormones, Homografts, and Creutzfeldt-Jakob Disease,” Lancet 340: 24-27.
Bruce, M.E., et al. (1997) “Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent,”Nature,vol. 389:498-501.
Buchanan, et al., (1991) “Mortality, Neoplasia, and Creutzfeldt-Jakob Disease in Patients Treated with Human Pituitary Growth Hormone in the United Kingdom”, BMJ 302:824-828.
Bueler, et al., (1992) “Normal Development and Behavior of Mice Lacking the Neuronal Cell-surface PrP Protein,” Nature 356:577-582.
Carter, et al., (1992) “High LevelEscherichia coliExpression and Production of a Bivalent Humanized Antibody Fragment,” Biotechnology 10:163-7.
Cochius, et al., (1990) “Creutzfeldt-Jakob Disease is a Recipient of Human Pituitary-Derived Gonadotropin,” Aust. N.Z. J. Med. 20:592-593.
Cochius, et al., (1992) “Creutzfeldt-Jakob Disease in a Recipient of Human Pituitary-Derived Gonadotrophin: A Second Case,” J. Neurol. Neurosurg. Psychiatry 55:1094-1095.
Collinge, et al., (1996) “Prion protein gene analysis in new variant cases of Creutzfeldt-Jakob disease,” Lancet 348:56.
Combs, et al, (1999) “Identification of Microglial Signal Transduction Pathways Mediating a Neruotoxic Response to Amyloidogenic Fragments of .beta.-Amyloid and Prion Proteins,” The Journal of Neuroscience, 19(3):928-939.
Cousens, S.N., et al., (1997) “Predicting the CJD epidemic in humans,”Nature,vol. 385:197-198.
Gabizon, et al., (1988) “Immunoaffinity purification and neutralization of scrapie prion infectivity,” Proc. Natl. Acad. Sci. USA, vol. 85, pp. 6617-6621.
Gajdusek, (1977) “Unconventional Viruses and the Origin and Disappearance of Kuru” Science, 197(4307):943-960.
Gajdusek, D.C., et al., (1996) “Experimental transmission of a kuru-like syndrome to chimpanzees,”Nature,209:794-976.
Gibbs, C.J., Jr., et al., (1968) “Creutzfeldt-Jakob disease (spongiform encephalopathy): transmission to the chimpanzee,”Science,vol. 161:388-389.
Gibbs, Jr., et al., (1993) “Creutzfeldt-Jakob Disease Infectivity of Growth Hormone Derived from Human Pituitary Glands,” N. Engl. J. Med. 328:358-359.
Gioia et al., (1994) “Conformational Polymorphism of the Amyloidogenic and Neurotoxic Peptide Homologous to Residues 106-126 of the Prion Protein,”Journal of Biological Chemistry,vol. 269(11):7859-7862.
Glenner, et al., (1989) “Amyloidosis of the nervous system,” J. Neurol. Sci., 94:1-28.
Goldfarb, et al., (1992) “Fatal Familial Insomnia and Familial Creutzfeldt-Jakob Disease: Disease Phenotype Determined by a DNA Polymorphism,” Science 258:806-808.
Greenberg, et al., (1993)Neurology,vol. 43:2073-9.
Haan, et al., (1990) “Amyloid in Central Nervous System Disease,” Clin. Neurol Neurosurg. 92(4):305-310.
Hardy, (1997) “Amyloid, the Presenilins and Alzheimer's Disease,” Trends Neurosci. 20(4):154-159.
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