Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2007-05-14
2010-06-08
Haddad, Maher M (Department: 1644)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
C530S387100, C530S387300, C530S388100
Reexamination Certificate
active
07732570
ABSTRACT:
The present invention provides for a modified Fc-fusion protein in which at least one amino acid from the heavy chain constant region selected from the group consisting of amino acid residues 250, 314, and 428 is substituted with another amino acid which is different from that present in the unmodified Fc-fusion protein, thereby altering the binding affinity for FcRn and/or the serum half-life in comparison to the unmodified Fc-fusion protein.
REFERENCES:
patent: 5530101 (1996-06-01), Queen et al.
patent: 5834597 (1998-11-01), Tso et al.
patent: 5994514 (1999-11-01), Jardieu et al.
patent: 6165745 (2000-12-01), Ward et al.
patent: 6197297 (2001-03-01), Kunikata et al.
patent: 6277375 (2001-08-01), Ward
patent: 6329511 (2001-12-01), Landolfi et al.
patent: 6383487 (2002-05-01), Amlot et al.
patent: 6528624 (2003-03-01), Idusogie et al.
patent: 6699472 (2004-03-01), Jardieu
patent: 6797493 (2004-09-01), Sun et al.
patent: 7083784 (2006-08-01), Dall'Acqua et al.
patent: 7163681 (2007-01-01), Giles-Komar et al.
patent: 7217797 (2007-05-01), Hinton et al.
patent: 7217798 (2007-05-01), Hinton et al.
patent: 7361740 (2008-04-01), Hinton et al.
patent: 7365168 (2008-04-01), Hinton et al.
patent: 2002/0098193 (2002-07-01), Ward
patent: 2002/0142000 (2002-10-01), Digan et al.
patent: 2003/0003098 (2003-01-01), Strom
patent: 2003/0044858 (2003-03-01), Jardieu et al.
patent: 2006/0198840 (2006-09-01), Dall'Acqua et al.
patent: 1 260 521 (2002-11-01), None
patent: WO93/04173 (1993-03-01), None
patent: WO98/05787 (1996-08-01), None
patent: WO96/31229 (1997-08-01), None
patent: WO97/28267 (1997-09-01), None
patent: WO97/34621 (1997-09-01), None
patent: WO97/34631 (1998-02-01), None
patent: WO98/23289 (1998-06-01), None
patent: WO98/47531 (1998-10-01), None
patent: WO99/02709 (1999-01-01), None
patent: WO99/51642 (1999-10-01), None
patent: WO99/58572 (1999-11-01), None
patent: WO00/42072 (2000-07-01), None
patent: WO00/47625 (2000-08-01), None
patent: WO00/68381 (2000-11-01), None
patent: WO01/58957 (2001-08-01), None
patent: WO02/060919 (2002-08-01), None
patent: WO2004/035752 (2004-04-01), None
patent: WO2004/092219 (2004-10-01), None
patent: WO2005/037867 (2005-04-01), None
patent: WO2005/123780 (2005-12-01), None
Achatz et al. “The IgE antigen Receptor: a Key Regulator for the Production of IgE Antibodies”,Int. Arch. Allergy Immunol, (2001) 124(1-3):31-4.
Alegre et al. “Effect of a single amino acid mutation on the activating and immunosuppressive properties of a humanized OKT3 monoclonal antibody”,J. Immunol.(1992) 148(11):3461-8.
Angal et al. “A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody”,Mol. Immunol(1993) 30(1):105-8.
Armour et al. “Recombinant human IgG molecules lacking Fcgamma receptor 1 binding and monocyte triggering activities”,Eur J. Immunol.(1999) 29(8):2613-24.
Armour et al. The Contrasting IgG-Binding Interactions of Human and Herpes Simplex Virus Fc Receptors,Biochem Soc. Trans.(2002) 30(4):495-500.
Arya et al. “Mapping of amino acid residues in the C mu 3 domain of mouse IgM important in macromolecular assembly and complement-dependent cytolysis”,J. Immunol(1994) 152(3):1206-12.
Attwood “Genomics: The Babel of Bioinformatics”Science(2000) 290:1-5.
Batra et al. “Insertion of Constant Region Domains of Human IgG1 into CD4-PE40 Increases Its Plasma Half-Life”,Molec. Immunol.(1993) 30(4):379-386.
Brekke et al. “Human IgG isotype-specific amino acid residues affecting complment-mediated cell lysis and phagocytosis”,Eur. J. Immunol.(1994) 24(10):2542-7.
Burmeister et al. Crystal structure of the complex of rat neonatal Fc receptor with FcNature(1994) 372:379-383.
Canfield “The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region”,J. Exp. Med.(1991) 173(6):1483-91.
Caron et al. Engineered humanized dimeric forms of IgG are more effective antibodies,J. Exp. Med.(1992) 176(4): 1191-5.
Chapman et al. “Characterization of the Interaction Between the Herpes Simplex Virus Type 1 Fc Receptor and Immunoglobulin G”,J. Biol. Chem.(1999) 274(11):6911-9.
Chappel et al. “Identification of a secondary Fc gamma R1 binding site within a genetically engineered human IgG antibody”,J. Biol. Chem.(1993) 268(33): 25124-31.
Chaudhury et al. “The Major Histocompatibility Complex-related Fc Receptor for IgG (FcRn) Binds Albumin and Prolongs Its Lifespan”,J. Exp. Med.(2003) 197(3):315-322.
Chintalacharuvu et al. “Hybrid IgA2/IgG1 Antibodies with Tailor-Made Effector Functions”,Clin. Imm.(2001) 101(1):21-31.
Cole et al. “HuM291, A Humanized Anti-CD3 Antibody, is Immunosuppressive to T cells While Exhibiting Reduced Mitogenicity in Vitro”,Transplanation(1999) 68(4):563-71.
Cole et al. “Human IgG2 variants of chimeric anti-CD3 are nonmitogenic to T cells”,J. Immunol.(1997) 159(7): 3613-21.
Dall'Acqua William F., et al. “Properties of Human IgG1s Engineered for Enhanced Binding to the Neonatal Fc Receptor (FcRn)”,Journal of Biological Chemistry(2006) 281(33):23514-23524.
Dall'Acqua et al. “Increasing the Affinity of a Human IgG1 for the Neonatal Fc Receptor: Biological Consequences”,J. Immunol.(2002) 169(9):5171-80.
Datta-Mannan A., et al. “Humanized IgG1Variants With Differential Binding Properties to the Neonatal Fc Receptor: Relationship to Pharmacokinetics in Mice and Primates”,Drug Metabolism and Disposition, [published on Oct. 18, 2006 as doi:10.1124/dmd.106.011734—DMD#11734, pp. 1-47].
Datta-Mannan, A. et al. “Monoclonal Antibody Clearance: Impact of modulating the interaction of IgG with FcRn”,Journal of Biological Chemistry[in press—published on Nov. 29, 2006 as Ms. M607161200, pp. 1-24].
Deisenhofer “Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A fromStaphylococcus aureusat 2.9- and 2.8-A resolution”,Biochemistry(1981) 20:2361-2370.
Delano et al. “Convergent Solutions to Binding at a Protein-Protein Interface”,Science(2000) 287(5456):1279-83.
Dorai et al. “Role of inter-heavy and light chain disulfide bonds in the effector functions of human immunoglobulin IgG1”,Mol. Immunol.(1992) 29(12):1487-91.
Duncan et al. “The binding site for C1q on IgG”,Nature(1988) 332(6166):738-40.
Ehrlich et al. “Characterization of human monoclonal antibodies directed against hepatitis B surface antigen”,Hum. Antibodies Hybridomas(1992) 3:2-7.
El-Amine et al. “In Vivo Induction of Tolerance by an Ig Peptide is not Affected by the Deletion of FcR or a Mutated IgG Fc Fragment”,Int. Immunol.(2002) 14(7):761-6.
Ellison et al. “Linkage and sequence homology of two human immunoglobulin gamma heavy chain constant region genes”,Proc. Natl. Acad. Sci. USA.(1982) 79:1984-1988.
Firan et al. “The MHC Class I-Related Receptor FcRn, Plays an Essential Role in the Matermofetal Transfer of Gamma-Globulin in Humans”,Int. Immunol.(2001) 13(8):993-1002.
Ghetie and Ward “Multiple roles for the major histocompatibility complex class I-related receptor FcRn”,Annu. Rev. Immunol.(2000) 18:739-766.
Ghetie, Victor et al. “Increasing the serum persistence of an IgG fragment by random mutagenesis”,Nature Biotechnology(1997) 15(7):637-640.
He X-y, et al. “Humanization and Pharmacokinetics of a Monoclonal Antibody with Specificity for Both E- and P-selectin”,The American Association of Immunologists(1998).
Helm et al. “Identification of the high affinity receptor binding region in human immunoglobulin E”,J. Biol. Chem.(1996) 271(13): 7494-500.
Hezareh et al. “Effector Function Activities of a Panel of Mutants of a Broadly Neutralizing Antibody Against Human Immunodeficiency Virus
Hinton Paul R.
Tsurushita Naoya
Dahle Chun
Facet Biotech Corporation
Haddad Maher M
Townsend and Townsend / and Crew LLP
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