Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Separation or purification
Reexamination Certificate
2005-04-05
2005-04-05
Witz, Jean C. (Department: 1651)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Separation or purification
C530S350000, C514S002600, C204S459000
Reexamination Certificate
active
06875849
ABSTRACT:
The present invention provides methods for efficient and concomitant recovery of multiple chaperone proteins and/or chaperone protein complexes from a limited sample source. Disclosed are methods involving the use of Free Solution Iso-Electric Focusing (FS-IEF) which can enrich samples containing chaperone proteins and/or chaperone protein complexes from a given sample. The chaperone proteins can be, but are not restricted to calreticulin, gp96, hsp86, hsp84, hsp70, hsp60 and hsp40. The invention also provides methods of recovering chaperone protein complexes for the preparation of vaccines containing chaperone complexes.
REFERENCES:
patent: 4588492 (1986-05-01), Bier
patent: 5298143 (1994-03-01), Ivory et al.
patent: 5750119 (1998-05-01), Srivastava
patent: 5837251 (1998-11-01), Srivastava
patent: 5935576 (1999-08-01), Srivastava
patent: 5961979 (1999-10-01), Srivastava
patent: 5997873 (1999-12-01), Srivastava
Osuji et al. “Pesticide Inactivation of Peanut Glutamate Dehydrogenase: Biochemical Basis of the Enzyme's Isomerization” (1999) J. Agric. Food Chem., 47(8), 3345-3351.*
Shang et al., “Carrier Ampholyte-Free Solution Isoelectric Focusing as a Prefractionation Method for the Proteomic Analysis of Complex Protein Mixtures” (2003) Electrophoresis, 14(14), 2359-2368.*
Nieves et al. “Covalent Modifications of Membrane Proteins with Unanticipated Acid Shifts in Isoelectric Points” (1998) ABRF 98 Poster Session, Mar. 22-24, 1998, Program #87.*
Rotofor System Bio-Rad Tech Note Summaries.*
Blennow et al., “Isolation and Biochemical Characterization of Highly PurifiedEscherichia coliMolecular Chaperone C[n60 (GroRL) by Affinity Chromatography and Urea-Induced Monomerization” (1995) Biochim. Biophys. Acta, 1252(1), 69-78.*
Eriksson et al., “The Superantigenic Activity of Streptococcal Pyrogenic Exotoxin B is Independent of the Protease Activity” (1999) FEMS Immunol. Med. Microbiol., 25(4), 355-363.*
Large et al., “Properties of the Chaperonin Complex from the Halophilic Archaeon Halofrax volcanii” (2002) FEBS Lett., 532(3), 309-312.*
Quait-Randall et al., “Purification of Chaperonins” (1999) J. Chromatog. B, 722(1-2), 153-177.*
Atkins et al., “Overproduction And Purification Of Mycobacterium Tuberculosis Chaperonin-10; Autographa Californica Nuclear-Polyhedrosis Virus Vector Acrp6.sC Expression in Spodoptera frugiperda Insect Cell Culture” (1994) Gene, vol. 150, No. 1, pp. 145-148.*
Zeng e al., “Tumor-Derived, Chaperone-Rich Cell Lysate Activates Dendritic Cells and Elicits Potent Antitumor Activity” (2003) Blood, 101(11), 4485-4491.*
Joachimiak et al., (Purification of Chaperonins from Thermophilic Bacteria and Archaea (1997) J. Chromatog. A, 773(1-2), 131-138.*
Salvucci et al., “Heat Shock Proteins in Whiteflies, an Insect that Accumulates Sorbitol in Response to Heat Stress” (2000) J. Thermal Biol., 25(5), 363-371.*
Minto et al., “Mycobacterial Cpn10 Promotes Recognition of the Mammalian Homologue by a Mycobacterium-Specific Antiserum” (Jun. 22, 1998) Biochim. Biophys. Acta, vol. 1403, No. 2, pp. 151-157.*
Lucietto et al., “Mycobacterium tuberculosis Chaperonin 10 and N-Truncated Fragments—Their Synthesis and Purification by the Isoelectric Focusing Technique Carried out in Solution” (Apr. 1997) J. Peptide Res., vol. 49, No. 4, pp. 308-323.*
Jethmalani et al., “Partial homology of Stress Glycoprotein GP62 with HSP70”(Apr. 10, 1997) Exp. Cell Res., vol. 232, No. 1, pp. 8-16.*
Mol et al., “Escherichia-ColiPeriplasmic Chaperone Faee is a Homodimer and the Chaperone-K88 Subunit Complex is a Heterotrimer” (Jan. 1994) Molec. Microbiol., vol. 11, No. 2, pp. 391-402.*
Amato et al., 1999, “Active Specific Immunotherapy in Patients with Renal Cell Carcinoma (RCC) Using Autologous Tumor Derived Heat Shock Protein-Peptide Complex-96 (HSPP-96) Vaccine”American Society Clinical Oncology Meeting,abstract 1278.
Arnold et al., 1995, “Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96”J. Exp. Med.182:885.
Basu and Srivastava, 1999, “Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity”J. Exp. Med.189:797.
Ciupitu et al., 1998, “Immunization with a lymphocytic choriomeningitis virus peptide mixed with heat shock protein 70 results in protective antiviral immunity and specific cytotoxic T lymphocytes”J. Exp. Med5: 685.
Graner et al., 2000, “Tumor-derived multiple chaperone enrichment by free-solution isoelectric focusing yields potent antitumor vaccines”Cancer Immunol. Immunother.49:476.
Graner et al. 2000, “Immunprotective activities of multiple chaperone proteins isolated from murine B-cell leukemia/lymphoma”Clin. Can. Res.6:909.
Janetzki et al., 2000, “Immunization of cancer patients with autologous cancer-derived heat shock protein gp96 preparations: a pilot study”Int. J. of Cancer88:232.
Ishii et al., 1999, “Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96”J. Immunol.162:1303.
Katsanis et al., 2000, “Augmentation of Tumor Lysate Immunogencity by enrichment of Chaperone Proteins Using Free Solution Isoelectric Focusing (FS-IEF)”Keystone Symposia on Cellular Immunity and Immunotherapy of Cancer,abstract 431.
Lewis et al., 1999, “Pilot Trial of Vaccination wwih Autologous Tumor-Derived gp96 Heat Shock Protein-Peptide Complex (HSPPC-96) in Patients with Resected Pancreatic Adenocarcinoma”American Society Clinical Oncology Meeting,abstract 1687.
Ménoret and Chandawarkar, 1998, “Heat-shock protein-based anticancer immunotherapy: an idea whose time has come”Semin. in Oncology25:654.
Nair et al., 1999, “Careticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptide”Immunol.162:6426.
Nieland et al., 1996, “Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein GP96/GRP94”PNAS93:6135.
Peng et al., 1997, “Purification of immunogenic heat shock protein 70-protein 70-peptide complexes by ADP-affinity chromatogrpahy”J. Immunol. Meth.204:13.
Srivatava et al., 1986, “Tumor rejection antigens of chemically induced sarcomas of inbred mice” P.N.A.S. 83:3407.
Srivastava et al., 1988, “Chromosomal assignment of the gene encoding the mouse tumor rejection antigen gp9”Immunogenetics28:205.
Srivastava et al., 1991, “Stress-induced proteins in immune response to cancer”Curr. Top. Microbiol. Immunol.167:109.
Srivastava, 1993, “Peptide-binding heat shock proteins in the endoplasmic reticulum: role in immune response to cancer and in antigen presentation”Adv. Cancer Res.62:153.
Srivastava and Udono, 1994, “Heat shock protein-peptide complexes in cancer immunotherapy”Curr. Opin. Immunol.6:728.
Srivastava et al., 1998, “Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world”Immunity8:657.
Tamura et al., 1997, “Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations”Science278:117.
Yedavelli et al., 1999, “Preventive and therapeutic effect of tumor derived heat shock protein, gp96, in an experimental prostate cancer model”Int. J. Mol. Med.3:243.
Ullrich et al., 1986, “A mouse tumor-specific transplantation antigen is a heat shock-related protein”PNAS83:3121.
Graner Michael
Katsanis Emmanuel
Arizona Board of Regents of behalf of The University of Arizona
Hanley Susan
Jones Day
Witz Jean C.
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