Chemistry: molecular biology and microbiology – Micro-organism – per se ; compositions thereof; proces of... – Bacteria or actinomycetales; media therefor
Reexamination Certificate
2006-04-26
2010-10-19
Steadman, David J (Department: 1656)
Chemistry: molecular biology and microbiology
Micro-organism, per se ; compositions thereof; proces of...
Bacteria or actinomycetales; media therefor
C435S070100, C435S189000
Reexamination Certificate
active
07816117
ABSTRACT:
The invention provides composition and methods for producing proteins of interest which comprise at least one disulfide bond, include proteins which in their mature form do not contain disulfide bonds, but whose precursor molecule contained at least one disulfide bond. The methods employ a host cell modified to more efficiently produce properly folded disulfide bond containing proteins. The host cells generally contain a mutation in one or more reductase genes, and can be further genetically modified to increase their growth rate, and are further optionally modified to increase the expression of a catalyst of disulfide bond formation. Host cells, methods for u sing such to produce proteins of interest, proteins of interest produced by these methods are within the scope of the invention.
REFERENCES:
patent: 6872563 (2005-03-01), Beckwith et al.
Poole et al., Flavin-Dependent Alkyl Hydroperoxide Reductase fromSalmonella typhimurium. 1. Purfication and Enzymatic Activities of Overexpressed AhpF and AhpC proteins, Biochemistry, 1996, vol. 35, pp. 56-64.
Tartaglia et al., Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress, Mol Biol., 1989, vol. 210, pp. 709-719.
Swits-Prot POA251.2 (last viewed on Oct. 28, 2009).
Ellis, H.R., et al., “Roles for the Two Cysteine Residues of AhpC in Catalysis of Peroxide Reduction by Alkyl Hydroperoxide Reductase fromSalmonella typhimurium,” Biochemistry, 36:13349-13356 (1997).
Mittl, P. and Schulz, G. Structure of glutathione reductase fromEscherichia coliat 1.86 Å resolution: Comparison with the enzyme from human erythrocytes, Protein Science 3:799-809 (1994).
Nawrocki et al., “Reduction of LDL Cholesterol by 25% to 60% in Patients with Primary Hypercholesterolemia by Atorvastin, a New HMG-CoA Reductase Inhibitor,” Arterioscier Thromb Vasc Biol., 15:678-682 (1995).
Romero, M. and Canada, A. The Evaluation ofEscherichia colias a model for Oxidant Stress in Mammalian Hepatocytes: Role of Glutathione, Toxicology and Applied Pharmacology, 111:485-495 (1991).
Schallreuter, K. and Wood, J.M., “Azelaic acid as a comptetive inhibitor of thioredoxin reductase in human melanoma cells,” Cancer Letters, 36:297-305 (1987).
Thorstenson et al., “Leaderless Polypeptides Efficiently Extracted form Whole Cells by Osmotic Shock,” J. Bac. 179(17):5333-5339 (1997).
Waksman, G. et al., Crystal Structure ofEscherichia coliThioredoxin Reductase refined at 2 Å Resolution, J. Mol. Biol., 236:800-816 (1994).
Wunderlich et al., “Redox properties of protein disulfide osomerase (DsbA) fromEscherichia coli,” Protein Sci., 2:717-726 (1993).
Aslund, F. et al. (1999), Bridge Over Troubled Waters: Sensing Stress by Disulfide Bond Formation, CELL 96:751-53.
Aslund, F. et al. (1999),Efficient Production of Disulfide Bonded Proteins in the Cytoplasm in “Oxidizing” Mutants of E. Coli, InNOVATIONS 10:11-12 (http://www.novagen.com/SharedImages.TechnicalLiterature/17—nd0d.pdf).
Aslund, F. et al. (1996),Glutaredoxin-3 from Escherichia coli,, J. of Biological Chem. 271(12):6736-45.
Aslund, F. et al. (1997), Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria, J. Biological Chem. 272(49):30780-86.
Aslund, F. et al. (1999), Regulation of the OxyR Transcription Factor by Hydrogen Peroxide and the Cellular Thiol—Disulfide Status, Proc. Natl. Acad. Sci. USA 96:6161-65.
Aslund, F. et al (1999), The Thioredoxin Superfamily: Redundancy, Specificity, and Gray-Area Genomics, J. of Bacteriology 181(5):1375-79.
Bessette, P.H. et al. (Nov. 23, 1999), Efficient Folding of Proteins with Multiple Disulfide Bonds in theEscherichia coliCytoplasm, PNAS 96(24):13703-08.
Debarbieux, L. et al. (2000), On the Functional Interchangeability, Oxidanmt versus Reductant, of Members of the Thioredoxin Superfamily, J. of Bacteriology 182(3):723-27.
Debarbieux, L. et al. (1998), The Reductive Enzyme Thioredoxin 1 Acts as an Oxidant When it is Exported to theEscherichia coliPeriplasm, Proc. Natl. Acad. Sci. USA 95:10751-56.
Derman, A. et al. (1993), Mutations that Allow Disulfide Bond Formation in the Cytoplasm ofEscherichia coli, Science 262:1744-47.
Ferrante, A. A, et al. (1995), Cloning of an organic solvent-resistance gene inEscherichia coli: The unexpected role of the alkylhydroperxide reductase, Applied Biological Sciences 92:7617-21.
Jordan, A. et al. (1997),Characterization of Escherichia coli NrdH, J. Biological Chem. 272(29):18044-50.
Kurokawa, Y. et al. (2000), Overexpression of Protein Disulfide Isomerase DsbC Stabilizes Multiple-Disulfide-Bonded Recombinant Protein Produced and Transported to the Periplasm inEscherichia coli, Applied and Environmental Microbiology 66(9):3960-65.
Martin, J. (1995),Thioredoxin—A Fold for All Reasons, Structure 3:245-50.
Mossner, E. et al. (1998), Characterization ofEscherichia coliThioredoxin Variants Mimicking the Active-Sites of Other Thiol/Disulfide Oxidoreductases, Protein Science 7:1233-44.
Mossner, E. et al. (1999), Importance of Redox Potential for the in Vivo Function of theCytoplasmic Disulfide Reductant Thioredoxin fromEscherichia coli, J. Biol. Chem. 274(36):25254-59.
Prinz, W. A. et al. (1997), The Role of the Thioredoxin and Glutaredoxin Pathways in Reducing Protein Disulfide Bonds in theEscherichia coliCytoplasm, J. Biol. Chem. 272(25):15661-67.
Qiu, J. et al. (1998), Expression of Active Human Tissue-Type Plasminogen Activator inEscherichia coli, Applied and Environ. Microbiol. 64(12):4891-96.
Rietsch, A. et al. (1998),The Genetics of Disulfide Bond Metabolism, Annu. Rev. Genet. 32:163-84.
Ritz, D. et al. (2001), Conversion of a Peroxiredoxin into a Disulfide Reductase by a Triplet Repeat Expansion, Science 294:158-160.
Ritz, D. et al. (1999), Thioredoxin 2 is Involved in the Oxidative Stress Response inEscherichia coli, J. Bio. Chem. 275:2505-12.
Stewart, E.J. et al. (1998), Disulfide Bond Formation in theEscherichia colicytoplasm: an in vivo Role Reversal for the Thioredoxins, EMBO J. 17(19):5543-50.
Ribnicky, B. M.: “Ph.D. Dissertation—Facs: A high throughput method for protein export and engineering”; Dec. 2006, University of Texas at Austin, XP002483751 pp. I-XV Bacterial strain: MJF256. 10 p. 80.
International Search Report PCT/US2007/067306, (2008).
Beckwith Jonathan
Faulkner Melinda
Georgiou George
Gon Stephanie
Ritz Daniel
Foley & Hoag LLP
Kim Alexander D
President and Fellows Of Harvard College
Steadman David J
The University of Texas System
LandOfFree
Prokaryotic host cells for expressing proteins rich in... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Prokaryotic host cells for expressing proteins rich in..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Prokaryotic host cells for expressing proteins rich in... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4169220