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
2006-08-01
2006-08-01
Smith, Lynette R. F. (Department: 1645)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
C435S069200, C435S069300, C435S069700, C435S007100
Reexamination Certificate
active
07083945
ABSTRACT:
The invention overcomes the deficiencies of the prior art by providing a rapid approach for isolating binding proteins capable of binding small molecules and peptides via “display-less” library screening. In the technique, libraries of candidate binding proteins, such as antibody sequences, are expressed in soluble form in the periplasmic space of gram negative bacteria, such asEscherichia coli, and are mixed with a labeled ligand. In clones expressing recombinant polypeptides with affinity for the ligand, the concentration of the labeled ligand bound to the binding protein is increased and allows the cells to be isolated from the rest of the library. Where fluorescent labeling of the target ligand is used, cells may be isolated by fluorescence activated cell sorting (FACS). The approach is more rapid than prior art methods and avoids problems associated with the surface-expression of ligand fusion proteins employed with phage display.
REFERENCES:
patent: 5160974 (1992-11-01), Siegel et al.
patent: 5223409 (1993-06-01), Ladner et al.
patent: 5348867 (1994-09-01), Georgiou et al.
patent: 5571698 (1996-11-01), Ladner et al.
patent: 5648237 (1997-07-01), Carter
patent: 5656015 (1997-08-01), Young
patent: 5744314 (1998-04-01), Menzel et al.
patent: 5759810 (1998-06-01), Honjo et al.
patent: 5780279 (1998-07-01), Matthews et al.
patent: 5824520 (1998-10-01), Mulligan-Kehoe
patent: 5837500 (1998-11-01), Ladner et al.
patent: 5866344 (1999-02-01), Georgiou
patent: 5922545 (1999-07-01), Mattheakis et al.
patent: 6001823 (1999-12-01), Hultgren et al.
patent: WO 98/49286 (1998-11-01), None
patent: WO 99/60096 (1999-11-01), None
patent: WO 02/22861 (2002-03-01), None
Daugherty et al, Protein Engineering, vol. 12, No. 7, p. 613-621.
Pini et al, The Journal of Biological Chemistry, 1998, vol. 273, No. 34, p. 21769-21776.
Bakau et al, Journal of Bacteriology, Jul. 1985, 163(1):61-8.
Webster's Ninth New Collegiate Dictionary , 1990.
Ames, Journal of Bioenergetics and Biomembranes, Feb. 1988, 20(1) 1-17.
Decad et al, Journal of Bacteriology, Oct. 1976, 128(1):325-36.
Nakae et al, The Journal of Biological Chemistry, Vo. 250, No. 18, Sep. 1975.
Higgins et al, Journal of Bioenergetics and Biomembranes, vol. 22., No. 4, 1990.
Ames (Journal of Bioenergetics and Biomnembranes, Feb. 1988, 20(1) 1-17).
Decad et al, (Journal of Bacteriology, Oct. 1976, 128(1):325-36).
Nakae et al (The Journal of Biological Chemistry, vol. 250, No. 18, Sep. 1975), 7359-7365.
Boeke et al., “Effects of Bacteriophage f1 Gene III Protein on the Host Cell Membrane,”Mol. Gen. Genet., 186:185-192, 1982.
Burioni et al., “A new subtraction technique for molecular cloning of rare antiviral antibody specificities from phage display libraries,”Res. Virol., 149:327-330, 1998.
Burman et al., “Murein and the Outer Penetration Barrier ofEscherichia coliK-12,Proteus mirabilis, andPseudomonas aeruginosa,” J. Bacteriol., 112(3):1364-1374, 1972.
Chowdhury and Pastan, “Improving antibody affinity by mimicking somatic hypermutation in vitro,”Nat. Biotech,, 17:568-572, 1999.
Coia et al., “Use of mutator cells as a means for increasing production levels of a recombinant antibody directed against Hepatitis B”,Gene201:203-209, 1997.
Dall'Acqua and Carter, “Antibody engineering,”Curr. Opin. Struct. Biol., 8:443-450, 1998.
Daugherty et al., “Flow cytometric screening of cell-based libraries,”J. Immunol. Methods. 243:211-227, 2000.
Daugherty et al., “Development of an optimized expression system for the screening of antibody libraries displayed on theEscherichia colisurface,”Prot. Eng.,12:613-620, 1999.
De Haard et al., “A Large Non-immunized Human Fab Fragment Phage Library That Permits Rapid Isolation and Kinetic Analysis of High Affinity Antibodies,”J. Biol. Chem.,274(26):18218-18230, 1999.
De Wildt et al., “Antibody arrays for high-throughput screening of antibody—antigen interactions,”Nat. Biotechnol.18:989-994, 2000.
Decad and Nikaido, “Outer Membrane of Gram-Negative Bacteria, XII Molecular-Sieving Function of Cell Wall,”J. Bacteriol., 128(1):325-336, 1976.
Deng et al., “Selection of Antibody Single-chain Variable Fragments with Improved Carbohydrate Binding by Phage Display,”J. Biol. Chem.,269:9533-9538, 1994.
Deng et al., “Basis for selection of improved carbohydrate-binding single-chain antibodies from synthetic gene libraries,”Proc. Natl. Acad. Sci. USA.92:4992-7996, 1995.
Duenas and Borrebaeck, “Clonal selection and Amplification of Phage Displayed Antibodies by Linking Antigen Recognition and Phage Replication,”Biotechnology, 12:999-1002, 1994.
Farmer et al., “Penetration of β-lactamase inhibitors into the periplasm of Gram-negative bacteria,”FEMS Microbiol. Lett., 176:11-15, 1999.
Georgiou et al., “Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines,”Nat. Biotechnol.15:29-34, 1997.
Griep et al., “pSKAP/S: An Expression Vector for the Production of Single-Chain Fv Alkaline Phosphatase Fusion Proteins,”Prot. Exp. Purif., 16:63-69, 1999.
Griffiths et al., “Isolation of high affinity human antibodies directly formlarge synthetic repertoires,”EMBO J., 13(14) 3245-3260, 1994.
Hawkins et al., “Selection of Phage Antibodies by Binding Affinity,”J. Mol. Biol., 226:889-896, 1992.
Hobot et al., “Periplasmic Gel: New Concept Resulting from the Reinvestigation of Bacterial Cell Envelope Ultrastructure by New Methods,”J. Bacteriol., 160(1):143-152, 1984.
Hoogenboom et al., “Creating and engineering human antibodies from immunotherapy,”Adv. Drug. Deliv. Rev., 31:5, 1998.
Hudson, “Recombinant antibody fragments,”Curr. Opin, Biotechnol., 9:395-402, 1998.
Johns et al., “In vivo selection of sFv from phage display libraries,”J. Immunol. Methods, 239:137-151, 2000.
Jouenne and Junter, “Do β-lactam antibiotics permeabilize the outer membrane of Gram-negative bacteria? An electrochemical investigation,”FEMS Microbiol. Lett., 68:313-318, 1990.
Kjaer et al., “Glycerol diversifies phage repertoire selections and lowers non-specific phage absorption,”FEBS Lett., 431:448-452, 1998.
Knappick et al., “Fully Synthetic Human Combinatorial Antibody Libraries (HuCAL) Based on Modular Consensus Frameworks and CDRs Randomized with Trinucleotides,”J. Mol. Biol., 296:57-86, 2000.
Krebber et al., “Inclusion of an upstream transcriptional terminator in phage display vectors abolishes background expression of toxic fusions with coat protein g3p,”Gene, 178:71-74, 1996.
Krebber et al., “Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system,”J. Immunol. Methods, 201:35-55, 1997.
Levitan, “Stochastic Modeling and Optimization of Phage Display,”J. Mol. Biol., 277:893-916, 1998.
MacKenzie and To, “The role of valency in the selection of anti-carbohydrate singl-chain Fvs from phage display libraries,”J. Immunol. Methods, 220:39-49, 1998.
MacKenzie et al., “Analysis by Surface Plasmon Resonance of the Influence of Valence on the Ligand Binding Affinity and Kinetics of an Anti-carbohydrate Antibody,”J. Biol. Chem., 271(3):1527-1533, 1996.
Malmborg et al., “Selection of binders from phage displayed antibody libraries using the BIAcore biosensor,”J. Immunol. Methods, 198:51-57, 1996.
Martinez et al., “Accurate Kinetic Modeling of Alkaline Phosphatase in theEscherichia coliPeriplasm: Implications for Enzyme Properitres and Substrate Diffusion,”Biochemistry, 35:1179-1186, 1996.
Martinez et al., “Steady-state enzyme kinetics in theEscherichia coliperiplasm: a model of a whole cell biocatalyst,”J. Biotechno
Chen Gang
Georgiou George
Hayhurst Andrew
Iverson Brent L.
Thomas Jeffrey G.
Ford Vanessa L.
Fulbright & Jaworksi L.L.P.
Smith Lynette R. F.
The Board of Regents of The University of Texas System
LandOfFree
Isolation of binding proteins with high affinity to ligands does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Isolation of binding proteins with high affinity to ligands, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Isolation of binding proteins with high affinity to ligands will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3615286