Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Enzymatic production of a protein or polypeptide
Reexamination Certificate
2007-06-12
2007-06-12
Swope, Sheridan (Department: 1652)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Enzymatic production of a protein or polypeptide
C435S212000, C536S023200
Reexamination Certificate
active
11131035
ABSTRACT:
A gram-negative bacterial cell is described that is deficient in a chromosomal gene present in a wild-type such cell which gene shares at least 80% sequence identity with the native sequence of the yfcK gene and encodes an aminopeptidase. Alternatively, a gram-negative bacterial cell is deficient in a chromosomal gene present in a wild-type such cell which gene encodes an aminopeptidase that shares at least 80% sequence identity with the native sequence of aminopeptidase b2324. Either of these types of cells, when comprising a nucleic acid encoding a heterologous polypeptide, produces an N-terminal unclipped polypeptide when it is cultured and the polypeptide recovered, with virtually no N-terminal clipped polypeptide produced as an impurity. Conversely, a method is provided for cleaving an N-terminal amino acid from a polypeptide comprising contacting the polypeptide with an aminopeptidase sharing at least 80% sequence identity with the native sequence of aminopeptidase b2324.
REFERENCES:
patent: 4865974 (1989-09-01), Ben-Bassat et al.
patent: 4946783 (1990-08-01), Beckwith et al.
patent: 5304472 (1994-04-01), Bass et al.
patent: 5508192 (1996-04-01), Georgiou et al.
patent: 5639635 (1997-06-01), Joly et al.
patent: 5789199 (1998-08-01), Joly et al.
patent: 6127144 (2000-10-01), Bartfeld et al.
patent: 6428997 (2002-08-01), Lee et al.
patent: 0 489 711 (2003-10-01), None
patent: 2002044601 (2002-06-01), None
patent: WO 86/01229 (1986-02-01), None
patent: WO 88/05821 (1988-08-01), None
patent: WO 00/34452 (2000-06-01), None
patent: WO 00/66761 (2000-11-01), None
patent: WO 03/023030 (2003-03-01), None
Fowler et al, Removal of N-terminal blocking groups from proteins. In: Current protocols in Protein Science p. 11.7.1 (1996).
Alberts et al., “Normal Genes can be Easily Replaced by Mutant Ones in Bacteria and Some Lower Eucaryotes”Molecular Biology of the Cell, 3rd edition, New York:Garland Publishing, Inc. pp. 325-326.
Andersen et al., “Metabolic Oscillations in anE. coliFermentation.”Biotechnol. Bioeng.75(2) :212-218 (Oct. 2001).
Ausubel et al., “Chapter 16: Protein Expression”Current Protocols in Molecular Biology(Online), John Wiley & Sons, Inc. (2002).
Bachmann., “Derivations and Genotypes of Some Mutant Derivatives ofEscherichia coliK-12.”Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. (Washington, DC: American Society for Microbiology.), Chapter 72, 2:1190-1219 (1987).
Bachmann., “Pedigrees of Some Mutant Strains ofEscherichia coliK-12.”Bact. Rev.36(4) :525-557 (Dec. 1972).
Baneyx and Georgiou., “Expression of Proteolytically Sensitive Polypeptides inEscherichia coli.” Stability of Protein Pharmaceuticals., Ahern and Manning, eds., NY:Plenum Press, Chapter 3, pp. 69-108 (1992).
Blattner et al., “The Complete Genome ofEscherichia coliK-12.”Science(Database SwissProt on GenCore, Compugen, Ltd. GenBank, Gene Sequence) 277:1453-1474 (Sep. 1997).
Blattner et al., “The Complete Genome Sequence ofEscherichia coliK-12”Science277:1453-1462 (Sep. 1997).
Chang et al., “High-Level Secretion of Human Growth Hormone byEscherichia coli.”Gene.55:189-196 (1987).
Chaudhury and Smith., “Escherichia colirecBC Deletion Mutants.” 160(2):788-791 (Nov. 1984).
Elish et al., “Biochemical Analysis of Spontaneous fepA Mutants ofEscherichia coli.” J. Gene. Microbiol.134:1355-1364 (1988).
Gonzales and Robert-Baodouy., “Bacterial Aminopeptidases: Properties and Functions.”FEMS Microbiology Reviews18(4):319-344 (1996).
Joly et al., “Overexpression ofEscherichia coliOxidoreductases Increases Recombinant Insulin-Like Growth Gactor-I Accumulation”Proc. Natl. Acad. Sci. USA95:2773-2777 (Mar. 1998).
Kleckner et al., “Genetic Engineering in Vivo Using Translocatable Drug-Resistance Elements: New Methods in Bacterial Genetics.”J. Mol. Biol.116:125-159 (1977).
Knappik et al., “The Effect of Folding Catalysts in the In Vivo Folding Process of Different Antibody Fragments Expressed inEscherichia coli” Bio/Technology11:77-83 (Jan. 1993).
Lawther et al., “Molecular Basis of Valine Resistance inEscherichia coliK-12.”Proc. Natl. Acad. Sci. USA78:922-925 (Feb. 1981).
Mark et al., “Genetic Mapping of trxA, a Gene Affecting Thioredoxin inEscherichia coliK12.”Mol. Gen. Genet.155:145-152 (1977).
Metcalf et al., “Use of the rep Technique for Allele Replacement to Construct NewEscherichia coliHosts for Maintenance of R6Kγ Origin Plasmids at Different Copy Numbers.”Gene.138:1-7 (1994).
Miller, Charles G., “Protein Degradation and Proteolytic Modification.”Escherichia coli and Salmonella., Frederick C. Neidhardt, ASM Press, Chapter 62, pp. 938-954 (1996).
Park et al., “Secretory Production of Recombinant Protein by a High Cell Density Culture of a Protease Negative MutantEscherichia coliStrain.”Biotechnol. Prog.15:164-167 (1999).
Wulfing and Pluckthun. “Correctly Folded T-Cell Receptor Fragments in the Periplasm ofEscherichia coli” J. Mol. Biol.242:655-669 (1994).
Ben-Bassat et al., “Processing of the Initiation Methionine from Proteins: Properties of theEscherichia coliMethionine Aminopeptidase and its Gene Structure”Journal of Bacteriology169(2):751-757 (1987).
Blattner, F.R. et al., “The complete genome sequence ofEscherichia coliK-12”NCBI Database(Acc. No. AE000321; XP-002368679) (Dec. 1, 2000).
Blattner, F.R., et al., “The complete genome sequence osEscherichia coliK-12”NCBI Database(Acc. No. AAC75384; XP-002368680) (Dec. 1, 2000).
Bujnicki, J. M. et al., “Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA”RNA, Cold Spring Harbor Laboratory Press vol. 10(8):1236-1242 (2004).
Genentech Inc.
Hasak Janet E.
Swope Sheridan
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