Muteins of apolipoprotein D

Details Muteins of apolipoprotein D Muteins of apolipoprotein D

2006-10-10

2006-10-10

Wax, Robert A. (Department: 1653)

Chemistry: molecular biology and microbiology

Process of mutation, cell fusion, or genetic modification

C435S472000

Reexamination Certificate

active

07118915

ABSTRACT:
A method for generating a mutein of human apolipoprotein D having detectable affinity to a given non-natural ligand of apolipoprotein D is disclosed, which comprises the steps of: (a) subjecting the apolipoprotein D to mutagenesis at the sequence positions 34 to 38, 60, 62 to 66, 68, 89 to 93, 115, 117 to 121, and 123 resulting in a plurality of muteins of apolipoprotein D; and (b) enriching resulting muteins having binding affinity for a given ligand from the plurality of muteins by selection, and/or isolating said mutein. Muteins of apolipoprotein D obtainable by this method are also disclosed.

REFERENCES:
patent: 5849576 (1998-12-01), Skerra et al.
patent: 6099517 (2000-08-01), Daugherty
patent: 6103493 (2000-08-01), Skerra et al.
patent: 6123936 (2000-09-01), Platz et al.
patent: 44 17 598 (1995-12-01), None
patent: 196 41 876 (1998-04-01), None
patent: 197 42 706 (1999-04-01), None
patent: 199 26 068 (2001-01-01), None
patent: WO 98/16873 (1998-04-01), None
patent: WO 99/16873 (1998-04-01), None
patent: WO 00/75308 (2000-12-01), None
Barbas, “Selection and evolution of high-affinity human anti-viral antibodies”,Trends Biotechnol., 1996, pp. 230-234, vol. 14 (Abstract).
Beck, et al., “Nucleotide sequence and genome organisation of filamentous bacteriophages f1 and fd”,Gene, 1981, pp. 35-58, vol. 16.
Beste, et al., “Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold”,Proc. Natl. Acad. Sci. USA, 1999, pp. 1898-1903, vol. 96.
Flower, Darren R., “The lipocalin protein family : structure and function”,Biochem. J., 1996, pp. 1-14, vol. 318.
Fling, et al., “Peptide and protein molecular weight determination by electrophoresis using a high-molarity tris buffer system without urea”,Anal. Biochem., 1986, pp. 83-88, vol. 155 (Abstract).
Geisselsoder, et al., “Efficient site-directed in vitro mutagenesis”,BioTechniques, 1987, pp. 786-791, vol. 5, No. 8 (Abstract).
Gill, et al., “Calculation of protein extinction coefficients from amino acid sequence data”,Anal. Biochem., 1989, pp. 319-326, vol. 182.
Hengen, Paul N., “Methods and reagents”,Trends Biochem. Sci., 1996, pp. 75-76, vol. 21.
Hoess, Ronald H., “Phage display of peptides and protein domains”,Current Opinion in Structural Biology, 1993, pp. 572-579, vol. 3.
Kraulis, et al., “The serum albumin-binding domain of streptococcal protein G is a three-helical bundle: a heteronuclear NMR study”,FEBS Letters, 1996, pp. 190-194, vol. 378.
Kunkel, et al., “Rapid and efficient site-specific mutagenesis without phenotypic selection”,Methods in Enzymology, 1987, pp. 367-382, vol. 154 (Abstract).
Low, et al., “Mimicking Somatic Hypermutation: Affinity Maturation of Antibodies Displayed on Bacteriophage Using a Bacterial Mutator Strain”,J. Mol. Biol, 1996, pp. 359-368, vol. 260.
Roberts, Richard W., “Totallyin vitroprotein selection using mRNA-protein fusions and ribosome display”,Current Opinion in Chemical Biology, 1999, pp. 268-273, vol. 3.
Schlehuber, et al., “A Novel Type of Receptor Protein, Based on the Lipocalin Scaffold, with Specificity for Digoxigenin”,J. Mol. Biol., 2000, pp. 1105-1120, vol. 297.
Schmidt, et al., “Molecular Interaction Between theStrep-tag Affinity Peptide and its Cognate Target, Streptavidin”,J. Mol. Biol., 1996, pp. 753-766, vol. 255.
Skerra, et al., “Filter screening of antibody Fab fragments secreted from individual bacterial colonies: specific detection of antigen binding with a two-membrane system”,Anal. Biochem., 1991, pp. 151-155, vol. 196 (Abstract).
Vogt, et al., “Bacterially produced apolopoprotein D binds progesterone and arachidonic acid, but not bilirubin or E-3M2H”,Journal of Molecular Recognition, 2001, pp.79-86, vol. 14.
Voss, et al., “Mutagenesis of a flexible loop in streptavidin leads to higher affinity for theStrep-tag II peptide and improved performance in recombinant protein purification”,Protein Engineering, 1997, pp. 975-982, vol. 10, No. 8.
Wells, et al., “Rapid evolution of peptide and protein binding properties invitro”, Current Opinion in Structural Biology, 1992, pp. 597-604, vol. 2.
Yanisch-Perron, et al., “Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors”,Gene, 1985, pp. 103-119, vol. 33 (Abstract).
Arne Skerra, “Anitcalins':A New Class of Engineered Ligand-Binding Proteins With Antibody-Like Properties,”Molecular Biotechnology, Jun. 2001, pp. 257-275, vol. 74, XP001079016.
D. Flower, “Multiple Molecular Recognition Properties of the Lipocalin Proteinfamily,”Journal of Molecular Recognition, Heyden&Son Ltd., London, GB, 1995, pp. 185-195, vol. 8, XP002095125.

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