Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Reexamination Certificate
2007-08-13
2009-10-27
Noakes, Suzanne M. (Department: 1656)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
Reexamination Certificate
active
07608424
ABSTRACT:
This invention provides a recombinant protein expression system using a host and cell-free translation system, and is capable of universally expressing a large amount of any protein as soluble protein, while preventing toxicity in hosts, formation of inclusion bodies, and decompositions with proteases. Such may be achieved by expressing the desired protein as a fusion protein with chaperoning, such as about 60 kDa molecular chaperons, 60 kDa heat shock proteins, or thermosomes, and accommodating the desired protein inside of a stereostructure of a chaperonin. The present invention provides a process for producing a protein, which comprises transcribing and translating a gene containing a gene encoding the linked chaperonin subunits and a gene encoding a desired protein thereby synthesizing a fusion protein having the desired protein linked via a peptide linkage to the linked chaperonin subunits.
REFERENCES:
patent: WO 93/13200 (1993-04-01), None
patent: WO 00/66756 (2000-11-01), None
patent: WO 00/75346 (2000-12-01), None
patent: WO 01/83804 (2001-11-01), None
Furutani et al. An Engineered Chaperonin Caging a Guest Protein: Structural Insights and Potential as a Protein Expression Tool. Protein Science, 2005, vol. 14, pp. 341-350.
Oliveira et al., “Recombinant Brucella Abortus Proteins That Induce Proliferation and Gamma-Interferon Secretion by CD4+ T cells from Brucella-Vaccinated Mice and Delayed-Type Hypersensitivity in Senstized Guinea Pigs”, Cellular Immunology, 1996, vol. 172, pp. 262-268.
Zondlo et al., “Monomer-Haptamer Equilibrium of theEscherichia coliChaperonin GroES”, Biochemistry, 1995, vol. 34, pp. 10334-10339.
Ishii et al., “Production of MBP (Maltose Binding Protein)-GroES Fusion Protein and Utilization to Stimulate GroEL-Medicated Protein Refolding”, Journal of Fermentation and Bioengineering, 1998, vol. 85, No. 1, pp. 69-73.
Andrew Hayhurst, “Improved Expression Characteristics of Single-Chain Fv Fragments when Fused Downstream of theEscherichia coliMaltose-Binding Protein or Upstream of a Single Immunoglobuln-Constant Domain”, Protein Expression and Purification, vol. 18, No. 1, Feb. 2000, pp. 1-10.
Rachel B. Kapust et al., “Escherichia coliMaltose-Binding Protein is Uncommonly Effective at Promoting the Solubility of Polypeptides to which it is Fused”, Protein Science, vol. 8, No. 9, 1999, pp. 1668-1674.
George Farr et al, “Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin Groel”, Cell, vol. 100, No. 5, Mar. 3, 2000, pp. 561-573.
Kazuyo Nishihara et al., “Chaperone Coexpression Plasmids: Differential and Synergistic Roles of Dnak-NdaJ-GrpE and GroEL-GroES in Assisting Folding of an Allergen of Japanese Cedar Pollen, Cryj2, inEscherichia coli”,Applied and Environmental Microbiology, May 1998, vol. 64, No. 5, pp. 1694-1699.
Duenas M. et al., “Intra-and Extracellular Expression an ScFv Antibody Fragment inE. coli: Effect of Bacterial Strains and Pathway Engineering using GroES/L Chaperonins.”, Biotechniques, Mar. 1994, vol. 16, No. 3, pp. 476, 477, and 480-483.
Furutani Masahiro
Hata Junichi
Togi Akiko
Noakes Suzanne M.
Sekisui Chemical Co. Ltd.
Sughrue & Mion, PLLC
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