Soluble recombinant botulinum toxin proteins

Details Soluble recombinant botulinum toxin proteins Soluble recombinant botulinum toxin proteins

2005-11-22

2005-11-22

Housel, James (Department: 1648)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Recombinant dna technique included in method of making a...

C435S069700, C435S071100, C435S071200, C435S320100, C424S236100, C424S247100

Reexamination Certificate

active

06967088

ABSTRACT:
The present invention includes recombinant proteins derived fromClostridium botulinumtoxins. In particular, soluble recombinantClostridium botulinumtype A, type B and type E toxin proteins are provided. Methods which allow for the isolation of recombinant proteins free of significant endotoxin contamination are provided. The soluble, endotoxin-free recombinant proteins are used as immunogens for the production of vaccines and antitoxins. These vaccines and antitoxins are useful in the treatment of humans and other animals at risk of intoxication with clostridial toxin.

REFERENCES:
patent: 5080895 (1992-01-01), Tokoro
patent: 5310663 (1994-05-01), Dobeli et al.
patent: 5919665 (1999-07-01), Williams
Nassau et al. J. Bacterio. 1996, vol. 178, No. 4, pp. 1047-1052.
Hill et al. Arch. Biochem. And Biophy. 1996, vol. 336, No. 2, pp. 283-289.
Kimura et al. Applied and Environmental Microbiology 1991, vol. 57, No. 4, pp. 1168-1172.
TaKaRa Shuzo Co. Catalog of TAKARA BIO Inc. at the web site: bio:takara.co.jp.
Plotkin et al (Vaccinespublished by W.B. Saunders Company Philadelphia, p. 571), 1988.
Nygren, P.-A. et al. Trends in Biotechnology 12 (5): 184-188, May 1994.
Rudinger, J. in Peptide Hormones, Parsons, J.A. (Ed.), University Park Press, Baltimore, MD, pp. 1-7, 1976.
Thompson, D. E. et al. Eur. J. Biochem. 189: 73-81, Apr. 1990.
Binz, T. et al. J. Biol. Chem. 265: 9153-9158, Jun. 1990.
Roitt, I. Essential Immunology, Sixth Edition, Blackwell Scientific Publications, Boston, MA, pp. 173-178, 1988.
LeClerc, C. et al., J. Immunol. 144 (8): 3174-3182, Apr. 1990.
Kleid, D. G. Annals NY Acad. Sci. 413: 23-30, 1983.
Siegel, L. J. Clin. Microbiol. 26: 2351-2356, Nov. 1988.
Cato et al. (1986) “Clostridium,”inBergey's Manual® of Systematic Bacteriology,2:1141-1200, Sneath (ed.), Williams & Wilkins.
Englekirk et al. (1992) “Classification,” inPrinciples and Practice of Clinical Anaerobic Bacteriology,pp. 22-23, Star Publishing Co., Belmont, CA.
Stephen and Pietrowski (1986) “Toxins Which Traverse Membranes and Deregulate Cells,” inBacterial Toxins,2d ed., pp. 66-67, American Society for Microbiology.
Berkow and Fletcher (eds.) (1992) “Bacterial Diseases,”in Merck Manual of Diagnosis and Therapy,16th ed., pp. 116-126, Merck Research Laboratories, Rahway, NJ.
Sigmund and Fraser (eds.) (1979) “Clostridial Infections,” inMerck Veterinary Manual,5th ed., pp. 396-409, Merck & Co., Rahway, N.J.
Hatheway (1990) “Bacteriophages and plasmids and their roles in coding for botulinal neurotoxins,” Clin. Microbiol. Rev. 3:73-74.
Arnon (1986) “Infant Botulism: Anticipating the Second Decade,” J. Infect. Dis. 154:201-206.
Arnon (1980) “Infant Botulism” Ann. Rev. Med. 31:541-559.
MacDonald et al. (1986) “The Changing Epidemiology of Adult Botulism in the United States,”Am. J. Epidemiol.124:794-799.
Tacket et al. (1984) “Equine Antitoxin Use and Other Factors That Predict Outcome in Type A Foodborne Botulism,” Am. J. Med. 76:794-798.
Swartz (1990) “Anaerobic Spore-Forming Bacilli: The Clostridia,” in B.D.Microbiology,4th edition, pp. 633-646, Davis et al. (eds.), J.B. Lippincott Co.
Holzer (1962) “Botulismus durch Inhalation,” Med. Klin. 41:1735-738.
Franz et al. (1993) inBotulinum and Tetanus Neurotoxins,pp. 473-476, B.R. DasGupta, ed., Plenum Press, NY.
Arnon et al. (1981) “Infant Botulism: Epidemiology and Relation to Sudden Infant Death Syndrome,” Epidemiol. Rev. 3:45-66.
Frankovich and Arnon (1991) “Clinical Trial of Botulism Immune Globulin for Infant Botulism,” West. J. Med. 154:103.
Sugiyama (1980) “Clostridium botoulinumNeurotoxin,” Microbiol. Rev. 44:419-448.
Balady (1991) “Botulism Antitoxin Fielded for Operation Desert Storm,” USAMRDC Newsletter, p. 6.
Schwarz and Arnon (1992)( “Botulism Immune Globulin for Infant Botulism Arrives-One Year and A Gulf War Later,” Western J. Med. 156:197-198.
Peterson et al. (1979) “The Sudden Infant Death Syndrome and Infant Botulism,” Rev. Infect. Dis. 1:630-634.
Arnon et al. (1978) “Intestinal Infection and Toxin Production byClostridium Botulinumas One Cause of Sudden Infant Death Syndrome,” Lancet, pp. 1273-1277.
Informational Brochure for the Pentavalent (ABCDE) Botulinum Toxoid, Centers for Disease Control, Rev. 1995, pp. 1-3 and 3 unnumbered pages.
Brooks et al. (eds.) (1991) “Infections Caused by Anaerobic Bacteria,” inJawetz, Melnick,&Adelberg's Medical Microbiology,19th ed., pp. 257-262, Appleton & Lange, San Mateo, CA.
Engelkirk et al. (1992) Principles and Practice of Clinical Anaerobic Bacteriology, pp. 64-67, Star Publishing Co., Belmont, CA.
Lyerly et al. (1992) “Characterization of a Toxin A-Negative, Toxin B-Positive Strain ofClostridium difficile,” Infect. Immun. 60:4633-4639.
Borriello et al. (1990 “Virulence Factors ofClostridium difficile,” Rev. Infect. Dis., 12(Suppl. 2):S185-S191.
Lyerly et al. (1985) “Effects ofClostridium difficileToxins Given Intragastrically to Animals,” Infect. Immun. 47:349-352.
Rolfe (1990) “Binding Kinetics ofClostridium difficileToxins A and B to Intestinal Brush Border Membranes from Infant and Adult Hamsters,” Infect. Immun. 59:1223-1230.
Kim and Rolfe (1987) “The Protective Role of Antibody to Toxin A inClostridium difficile—Induced Ileoceeitis,” Abstr. Ann. Meet. Am. Soc. Microbiol. 69:62.
Banno et al. (1984) “Biochemical Characterization and Biologic Actions of Two Toxins (D-1 and D-2) FromClostridium difficile,” Rev. Infect. Dis. 6(Suppl. 1:S11-S20).
Rihn et al. (1984) “A New Purification Procedure forClostridium difficileEnterotoxin,” Biochem. Biophys. Res. Comm. 124:690-695.
Justus et al. (1982) “Myoelectric Effects ofClostridium difficile:Motility-Altering Factors Distinct From its Cytotoxin and Enterotoxin in Rabbits,” Gasroenterol. 83:836-843.
Finegold et al. (1992) “Antimicrobial-Associated pseudomembranous Colitis,” inClinical Guide to Anaerobic Infections,pp. 88-89, Star Publishing Co., Belmont, CA.
United States Pharmacopeia (1990) United States Pharmacopeial Convention, vol. XXII:1515-1516 Rockville, MD.
FDA Guidelines for Parenteral Drugs (Dec. 1987) i.e., Guideline on Validation of the Limulus Ameobycte Lysate Test as an End-Product Endotoxin Test for Human and Animal Parenteral Drugs. Biological Products and Medical Devices.
Pearson (1985) “Equivalency of LAL and USP Rabbit Pyrogen Tests,” inPyrogens: endotoxins, lal testing and depyrogenation,Marcel Dekker, NY, pp. 150-155.
Minton (1995) “Molecular Genetics of Clostridial Neurotoxins,” Curr. Top. Microbiol. Immunol. 195:161-194.
Benedict and Yamaga (1966) “Immunoglobulins and Antibody Production in Avian Species,” inComparative Immunology,pp. 335-375 (JJ. Marchaloni, ed.), Blackwell, Oxford.
Patterson et al. (1962) “Antibody Production and Transfer to Egg Yolk in Chickens,” Immunol. 89:272-278.
Carroll and Stollar (1983) “Antibodies of Calf Thymus RNA Polymerase II from Egg Yolks of Immunized Hens,” J. Biol. Chem. 258:24-26.
Polson et al. (1980) “Antibodies to Proteins from Yolk of Immunized Hens,” Immunol. Comm. 9:495-514.
DasGupta and Sugiyama (1972) “A Common Subunit Structure InClostridium BotulinumType A, B. and E Toxins,” Biochem. Biophys. Res. Commun. 48:108-112.
DasGupta (1990) “Structure and Biological Activity of Botulinum Neurotoxin,” J. Physiol. 84:220-228.
Halpern and Loftus (1993) “Characterization of the Receptor-binding Domain of Tetanus Toxin,” J. Biol. Chem. 268:11188-11192.
Whelan et al. (1992) “Molecular Cloning of theClostridium botulinumStructural Gene Encoding the Type B Neurotoxin and Determination of Its Entire Nucleotide Sequence,” Appl. Environ. Microbi

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