Recombinant vaccine against botulinum neurotoxin

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

Reexamination Certificate

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C536S023100, C514S04400A, C435S071100, C435S071200, C435S069100

Reexamination Certificate

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09611419

ABSTRACT:
This invention is directed to preparation and expression of synthetic genes encoding polypeptides containing protective epitopes of botulinum neurotoxin (BoNT). The invention is also directed to production of immunogenic peptides encoded by the synthetic genes, as weel as recovery and purification of the immunogenic peptides from recombinant organisms. The invention is also directed to methods of vaccination against botulism using the expressed peptides.

REFERENCES:
patent: 4664911 (1987-05-01), Uhr et al.
patent: 5196193 (1993-03-01), Carroll
patent: 5601823 (1997-02-01), Williams
patent: 5736139 (1998-04-01), Kink et al.
patent: 5919665 (1999-07-01), Williams
patent: 5965406 (1999-10-01), Murphy
patent: 6290960 (2001-09-01), Kink et al.
patent: 6348450 (2002-02-01), Tang et al.
patent: 6495143 (2002-12-01), Lee et al.
patent: 6632440 (2003-10-01), Quinn et al.
patent: 0639081 (1993-11-01), None
patent: 91/13090 (1991-09-01), None
patent: 9715394 (1998-05-01), None
patent: 0012890 (2000-11-01), None
Clayton et al, Infection and Immunity, vol. 63(7), pp. 2738-2742, 1995.
Thompson, DE et al, Eur. J. Biochemistry, vol. 189(1), pp. 73-81, 1990.
Halpern, J. L. et al, Journal of Biological Chemistry, vol. 268(15), pp. 11186-11192, May 25, 1993.
Binz, T et al, Journal of Biological Chemistry, vol. 265, pp. 9153-9158, 1990.
Clayton, MA et al, Infection and Immunity, vol. 63(7), pp. 2738-2742, Jul. 1995, Protective Vaccination with a Recombinant Fragment ofClostridium botulinumneurotoxin serotype A expressed from a synthetic gene inEscherichia coli.
Szabo, EA et al, Applied and Environmental Microbiology, vol. 59(9), Sep. 1993, pp. 3011-3020, Detection of the genes encoding Botulinum neurotoxin types A to E. by the polymerase chain reaction.
Promega pSP73 Vector sequence and product map.
Thompson, DE et al, 1990, European J. Biochem, vol. 189, pp. 73-81.
Ledoux, DN et al, Toxicon, vol. 33(9), pagtes 1095-1104, 1994 (best copy).
LaPenotiere, HP et al, Presentation at the International Conference on Botulinum, Tetanus, Neurotoxins: Neurotransmission and Biomedical Aspects, May 11-13, 1992, Madison, Wisconsin, also found in Botulinum and Tetanus Neurotoxins, pp. 463-465 Development of a Molecular Engineered vaccine for C. Botulinum Neurotoxins, Plenum Press, New York, 1993.
New England Biolab product description for pMAL System, product No. #800.
Swiss Prot Accession No. P10845, botulinum neurotoxin type A.
Dertzbaugh, M.T. et al, Vaccine, Nov. 1996, vol. 14(16), apges 1538-1544, Mapping of protective and cross-reactive domains of type A neurotoxin ofClostridium botulinum.
Kurazono, H et al, Journal of Biological Chemistry, Jul. 25, 1992, vol. 267(21), pates 14721-14729.
LaPenotiere, Hugh F et al, Toxicon, vol. 33(10), pp. 1383-1386, Expression of a large, nontoxic fragment of botulinum neurotoxin serotype A and its use as an immunogen, 1993.
Roseneberg, JS et al, Immunological investigations, Jun. 1997, vol. 26(4), pp. 491-504, Localization of the regions on the C-terminal domain of the heavy chain of botulinum A recognized by T lymphocytes and by antibodies after immunization of mice.
Kurazono et al (1992) reference of record.
Dertzbaugh et al (reference of record).
Binz et al (reference of record.) accession No. P10845, previously cited.
LaPenotiere et al (1992) reference of record.
Thompson et al (1990) reference of record.
Romanos et al (1991) reference of record.
Atassi et al (1999), Critical Review in Immunology, vol. 19(3), pp. 219-260, Structure, Activity and immune (T and B cell).
Rosenberg, JS et al, Immunolol Investig., vol. 26(4), p. 491-504, Jun. (1997), Localization of the regions on the C-terminal domain of the heavy chain of bot.toxin A recognized by T lymph and by antibodies after immunization of mice w pentavalent toxoid.
Makoff, AJ et al (1989), reference of record.
Ahmed SA et al., 2001, “Enzymatic autocatalysis of botulinium A neurotoxin light chain”J. Protein Chem. 20(3):221-231.
Schmidt JJ et al., 2001, “High-throughput assays for botulinum neurotoxin proteolytic activity: serotypes A, B, D, and F”Analytical Biochemistry296:130-137.
URL:http://www.cdc.gov
cidod/srp/drugservice/immunodrugs.htm, 2001, “Immunobiologic Agents and Drugs Available from the Centers for Disease Control. Descriptions, Recommedations, Adverse Reactions and Serologic Response” Centers for Disease Control, Atlanta, GA.
Ahmed SA et al., 2000, “Light chain of botulinum A neurotoxin expressed as an inclusion body from a synthetic gene is catalytically and functionally active”J. Protein Chem. 19(6):475-487.
Alderton JM et al., 2000, “Evidence for a vesicle-mediated maintenance of store-operated calcium channels in a human embryonic kidney cell line”Cell. Calcium28(3):161-169.
Byrne MP et al., 2000, “Fermentation, purification, and efficacy of a recombinant vaccine candidate against botulinum neurotoxin type F fromPichia pastoris” Protein Expr Purif.18(3):327-337.
Dalbey RE et al., 2000, “Evolutionarily related insertion pathways of bacterial, mitochondrial, and thylakoid membrane proteins”Annu. Rev. Cell Dev. Biol. 16:51-87.
Ettinger RA et al., 2000, “Beta 57-Asp plays an essential role in the unique SDS stability of HLA-DQA1*0102/DQB1*0602 alpha beta protein dimer, the class II MHC allele associated with protection from insulin-dependent diabetes mellitus”J. Immunol165:3232-3238.
Kadkhodayan S et al., 2000, “Cloning, expression, and one-step purification of the minimal essential domain of the light chain of botulinum neurotoxin type A”Protein Expr. Purif.19(1):125-130.
Knapp M et al., 2000, “The crystal structure of botulinum toxin A zinc protease domain.” Presented at the 37th Annual Meeting of the Interagency Botulinum Research Coordinating Committee, Oct. 17-20, 2000, Alisomar, California.
Li L et al., 2000, “Role of zinc binding in type A botulinum neurotoxin light chain's toxic structure”Biochemistry39:10581-10586.
Strasser A et al., 2000, “Apoptosis signaling”Annu. Rev. Biochem69:217-245.
Cai S et al., 1999, “Enhancement of the endopeptidase activity of botulinum neurotoxin by its associated proteins and dithiothreitol”Biochemistry38;6903-6910.
Claiborne A et al., 1999, “Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation”Biochemistry38:15407-15416.
Lacy DB et al., 1999, “Sequence homology and structural analysis of the clostridial neurotoxins”J. Mol. Biol.291:1091-1104.
Li L et al., 1999, “High-level expression, purification, and characterization of recombinant type A botulinum neurotoxin light chain”Protein Expr. Purif. 17:339-344.
Li L et al., 1999, “In vitro translation of type AClostridium botulinumneurotoxin heavy chain an analysis of its binding to rat synaptosomes”J Protein Chem. 18(1):89-95.
Byrne MP et al., 1998, “Purification, Potency, and Efficacy of the Botulinum Neurotoxin Type A Binding Domain fromPichia pastorisas a Recombinant Vaccine Candidate,”Infect. Immun.66:4817-4822.
Fu F et al., 1998, “Role of zinc in the structure of toxic activity of botulinum neurotoxin”Biochemistry37:5267-5278.
Lacy DB et al., 1998, “Crystal Structure of Botulinum Neurotoxin Type A and Implications for Toxicity,”Nat. Struct. Biol. 5:898-902.
Nowakowski JL et al., 1998, “Production of an expression system for a synaptobrevin fragment to monitor cleavage by botulinum neurotoxin B”J. Protein Chem. 17:453-462.
Potter KJ et al., 1998, “Production and purification of the heavy-chain fragment C of botulinum neurotoxin, serotype B, expressed in the methylotrophic yeastPichia pastoris” Protein Expr Purif. 13(3):357-365.
Schmidt JJ et al., 1998, “Type A botulinum neurotoxin proteolytic activity: development of competitive inhibitors and implications for substrate specificity at the S1′ binding subsite”FEBS Lett. 435:61-64.
Smith LA

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