Directed evolution of novel binding proteins

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

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S069100, C435S006120, C435S440000, C435S005000, C435S070100, C530S412000

Reexamination Certificate

active

09893878

ABSTRACT:
In order to obtain a novel binding protein against a chosen target, DNA molecules, each encoding a protein comprising one of a family of similar potential binding domains and a structural signal calling for the display of the protein on the outer surface of a chosen bacterial cell, bacterial spore or phage (genetic package) are introduced into a genetic package. The protein is expressed and the potential binding domain is displayed on the outer surface of the package. The cells or viruses bearing the binding domains which recognize the target molecule are isolated and amplified. The successful binding domains are then characterized. One or more of these successful binding domains is used as a model for the design of a new family of potential binding domains, and the process is repeated until a novel binding domain having a desired affinity for the target molecule is obtained. In one embodiment, the first family of potential binding domains is related to bovine pancreatic trypsin inhibitor, the genetic package is M13 phage, and the protein includes the outer surface transport signal of the M13 gene III protein.

REFERENCES:
patent: 4304863 (1981-12-01), Collins et al.
patent: 4332897 (1982-06-01), Nakano et al.
patent: 4338397 (1982-07-01), Gilbert et al.
patent: 4348477 (1982-09-01), Nakano et al.
patent: 4348478 (1982-09-01), Nakano et al.
patent: 4359535 (1982-11-01), Pieczenik
patent: 4411994 (1983-10-01), Gilbert et al.
patent: 4508826 (1985-04-01), Foor et al.
patent: 4528266 (1985-07-01), Pieczenik
patent: 4593002 (1986-06-01), Dulbecco
patent: 4595658 (1986-06-01), Zinder et al.
patent: 4595674 (1986-06-01), Tschesche et al.
patent: 4603112 (1986-07-01), Paoletti et al.
patent: 4642334 (1987-02-01), Moore et al.
patent: 4683202 (1987-07-01), Mullis
patent: 4703004 (1987-10-01), Hopp et al.
patent: 4704692 (1987-11-01), Ladner
patent: 4752473 (1988-06-01), Nayak et al.
patent: 4757013 (1988-07-01), Inouye et al.
patent: 4769326 (1988-09-01), Rutter
patent: 4769327 (1988-09-01), Stephens et al.
patent: 4769328 (1988-09-01), Murray et al.
patent: 4774180 (1988-09-01), Toth et al.
patent: 4786719 (1988-11-01), Kudo et al.
patent: 4797363 (1989-01-01), Teodorescu et al.
patent: 4829052 (1989-05-01), Glover et al.
patent: 4894436 (1990-01-01), Auerswald et al.
patent: 4908773 (1990-03-01), Pantoliano et al.
patent: 5010175 (1991-04-01), Rutter et al.
patent: 5101024 (1992-03-01), Kudo et al.
patent: 5223409 (1993-06-01), Ladner et al.
patent: 5225539 (1993-07-01), Winter
patent: 5403484 (1995-04-01), Ladner et al.
patent: 5432018 (1995-07-01), Dower et al.
patent: 5432155 (1995-07-01), Olivera et al.
patent: 5498538 (1996-03-01), Kay et al.
patent: 5571698 (1996-11-01), Ladner et al.
patent: 5616463 (1997-04-01), Fornace, Jr. et al.
patent: 5723286 (1998-03-01), Dower et al.
patent: 5789538 (1998-08-01), Rebar et al.
patent: 5837500 (1998-11-01), Ladner et al.
patent: 5866363 (1999-02-01), Pieczenik
patent: 5891640 (1999-04-01), De Leys
patent: 5955582 (1999-09-01), Newman et al.
patent: 5969108 (1999-10-01), McCafferty et al.
patent: 6291158 (2001-09-01), Winter et al.
patent: 6979538 (2005-12-01), Ladner et al.
patent: 2002/0150881 (2002-10-01), Ladner et al.
patent: 2003/0113717 (2003-06-01), Ladner et al.
patent: 2003/0219886 (2003-11-01), Ladner et al.
patent: 2004/0005539 (2004-01-01), Ladner et al.
patent: 2004/0023205 (2004-02-01), Ladner et al.
patent: 0 184 187 (1986-06-01), None
patent: 0 274 394 (1988-07-01), None
patent: 0 285 123 (1988-10-01), None
patent: 0 286 239 (1988-10-01), None
patent: 0 297 362 (1989-01-01), None
patent: 0 339 942 (1989-11-01), None
patent: 0 341 444 (1989-11-01), None
patent: 1 279 731 (1991-03-01), None
patent: 2 188 322 (1987-09-01), None
patent: 2 188 933 (1987-10-01), None
patent: 2 208 511 (1989-05-01), None
patent: WO 87/01374 (1987-03-01), None
patent: 2 183 661 (1987-06-01), None
patent: WO 88/01649 (1988-03-01), None
patent: WO 88/06601 (1988-09-01), None
patent: WO 88/06630 (1988-09-01), None
patent: WO 89/01968 (1989-03-01), None
patent: WO 89/02461 (1989-03-01), None
patent: WO 90/02809 (1990-03-01), None
patent: WO 91/17271 (1991-11-01), None
patent: WO 91/18980 (1991-12-01), None
patent: WO 91/19818 (1991-12-01), None
patent: WO 92/01047 (1992-01-01), None
patent: WO 92/06176 (1992-04-01), None
patent: WO 92/06204 (1992-04-01), None
patent: WO 92/11272 (1992-07-01), None
patent: WO 92/15605 (1992-09-01), None
patent: WO 92/15677 (1992-09-01), None
patent: WO 94/18220 (1994-08-01), None
patent: WO 95/19431 (1994-08-01), None
patent: WO 96/06166 (1996-02-01), None
Huston et al., PNAS USA 85:5879-5883 (1988).
Sharon et al., PNAS USA 83:2628-2631 (1986).
Reske et al., Eur. J. Immunol. 17:909-914 (1987).
Abarzua et al., Enzymatic techniques for the isolation of random single-base substitutions in vitro at high frequency. Proc Natl Acad Sci U S A. Apr. 1984;81(7):2030-4.
Adamson et al., Inhibition of human leukocyte elastase (HLE) by disulfide-cyclized analogs of alpha-antitrypsin (alphaAT). in Smith et al., eds., Peptides: Chemistry & Biology, Proceedings of the Twelfth American Peptide Symposium. Jun. 16-21, 1991; Cambridge, Massachusetts, USA (ESCOM, Leiden: 1992). p. 895-60.
Agterberg et al., Use of outer membrane protein PhoE as a carrier for the transport of a foreign antigenic determinant to the cell surface ofEscherichia coliK-12. Gene. 1987;59(1):145-50.
Altman et al., Intracellular expression of BPTI fusion proteins and single column cleavage/affinity purification by chymotrypsin. Protein Eng. 1991;4(5):593-600.
Araki et al., Four disulfide bonds′ allocation of Na+, K(+)-ATPase inhibitor (SPAI). Biochem Biophys Res Commun. Oct. 15, 1990;172(1):42-6.
Argos et al., Analysis of sequence-similar pentapeptides in unrelated protein tertiary structures. Strategies for protein folding and a guide for site-directed mutagenesis. J Mol Biol. Sep. 20, 1987;197(2):331-48.
Ausubel et al., eds. Current Protocols in Molecular Biology. John Wiley and Sons, publisher. New York, 1987; p. 8.0.1-8.3.6.
Barbas et al., Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc Natl Acad Sci U S A Sep. 15, 1991;88(18):7978-82.
Bass et al., Hormone phage: an enrichment method for variant proteins with altered bindind properties. Proteins. 1990;8(4):309-14.
Becker et al., Synthesis and characterization of mu-conotoxin IIIa. Eur J Biochem. Oct. 20, 1989;185(1):79-84.
Beckwith et al., Genetic analysis of protein export inEscherichia coli. Methods Enzymol. 1983;97:3-11.
Bedouelle et al., [Expression, export and one-step purification of proteins by fusion to the MalE protein ofE. coli] C R Acad Sci III. 1987;305(17):623-6. French.
Bedouelle et al., Production inEscherichia coliand one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space. Eur J Biochem. Feb. 1, 1988;171(3):541-9.
Benson et al., Intragenic regions required for LamB export. Proc Natl Acad Sci U S A. Jun. 1984;81(12):3830-4.
Benson et al., In vivi selection and characterization of internal deletions in the lamB::lacZ gene fusion. Gene. 1987;52(2-3):165-73.
Benson et al., Signal sequence mutations that alter coupling of secretion and translation of anEscherichia coliouter membrane protein. J Bacteriol. Oct. 1987;169(10):4686-91.
Benz et al., Structure and function of porins from gram-negative bacteria. Annu Rev Microbiol. 1988;42:359-93.
Berg et al., Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins. Proc. Natl Acad Sci U S A. Jan. 1988;85(1):99-102.
Bhatnagar et al., Synthesis and antigenic activity ofE. coliST and its analogues. Dev Biol Stand. 1986;63:79-87.
Bienstock et al., Conformation of highly potent bicyclic GnRH antagonist by combined molecular dynamics and two-dimensional NMR analyses. in Smith et al., eds. Peptides: Chemistry & Biology, Proceedings of the Twelfth American Peptide Symposium. Jun. 16-21, 1991; Cambridge, Massachusetts, USA (ESCOM, Leiden: 1992). p. 262-4.
Boeke et al., Processing of filament

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Directed evolution of novel binding proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Directed evolution of novel binding proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Directed evolution of novel binding proteins will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3797266

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.