Alteration of FcRn binding affinities or serum half-lives of...

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C530S388100, C435S069100, C435S069600, C435S326000, C435S440000, C435S455000

Reexamination Certificate

active

10687118

ABSTRACT:
The present invention provides for a modified antibody of class IgG, 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 antibody, thereby altering the binding affinity for FcRn and/or the serum half-life in comparison to the unmodified antibody.

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: 6277375 (2001-08-01), Ward
patent: 6329511 (2001-12-01), Landolfi et al.
patent: 6528624 (2003-03-01), Idusogie et al.
patent: 6797493 (2004-09-01), Sun et al.
patent: 7083784 (2006-08-01), Dall'Acqua et al.
patent: 2001/0033842 (2001-10-01), Jardieu et al.
patent: 2002/0098193 (2002-07-01), Ward
patent: 2003/0003088 (2003-01-01), Strom
patent: 2003/0003098 (2003-01-01), Strom
patent: 2003/0044858 (2003-03-01), Jardieu et al.
patent: 2005/0014934 (2005-01-01), Hinton et al.
patent: 2005/0032114 (2005-02-01), Hinton et al.
patent: 2005/0226864 (2005-10-01), Hinton et al.
patent: 2005/0276799 (2005-12-01), Hinton et al.
patent: 2006/0198840 (2006-09-01), Dall'Acqua et al.
patent: 1260521 (1991-08-01), None
patent: WO9304173 (1993-03-01), None
patent: WO9631229 (1996-10-01), None
patent: WO9728267 (1997-08-01), None
patent: WO9734621 (1997-09-01), None
patent: WO9734631 (1997-09-01), None
patent: WO9805787 (1998-02-01), None
patent: WO9823289 (1998-06-01), None
patent: WO9847531 (1998-10-01), None
patent: WO9902709 (1999-01-01), None
patent: WO9951642 (1999-10-01), None
patent: WO9958572 (1999-11-01), None
patent: WO0042072 (2000-07-01), None
patent: WO0047625 (2000-08-01), None
patent: WO00/668381 (2000-11-01), None
patent: WO0158957 (2001-08-01), None
patent: WO02/060919 (2002-08-01), None
patent: WO0260919 (2002-08-01), None
patent: WO2004/092219 (2004-10-01), None
Martin et al. Molecular Cell, 2001, 7:867-877.
Reff et al. Critical Review in Oncology/Hematology, 2001, 40:25-35.
Ogata et al PNAS, 1993, 90:3014-3018.
He X-y, et al.; “Humanization and Pharmacokinetics of a Monoclonal Antibody with Specificity for Both E- and P-selectin” The Americal Association of Immunologists; 1998.
Chintalacharuvu, et al., “Hybrid IgA2/IgG1 Antibodies with Tailor-Made Effector Functions”,Clin. Imm. 101(1):21-31 (2001).
Achatz, et al., “The IgE Antigen Receptor: a Key Regulator for the Production of IgE Antibodies,”Int. Arch. Allergy Immunol, 124(1-3): 31-4 (2001).
Alegre, et al., “Effect of a single amino acid mutation on the activating and immunosuppressive properties of a humanized OKT3 monoclonal antibody,”J. Immunol.148(11):3461-8 (1992).
Angal, et al., “A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody,”Mol Immunol30(1): 105-8 (1993).
Armour, et al., “Recombinant human IgG molecules lacking Fcgamma receptor 1 binding and monocyte triggering activities,”Eur J Immunol, 29(8): 2613-24 (1999).
Armour, et al., “The Contrasting IgG-Binding Interactions of Human and Herpes Simplex Virus Fc Receptors,”Biochem Soc. Trans., 30(4): 495-500 (2002).
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 Immunol152(3): 1206-12 (1994).
Batra, et al., “Insertion of Constant Region Domains of Human IgG1 into CD4-PE40 Increases Its Plasma Half-Life,”Molec. Immunol.30(4), 379-386 (1993).
Brekke, et al., “Human IgG isotype-specific amino acid residues affecting complement-mediated cell lysis and phagocytosis,”Eur J Immunol24(10): 2542-7 (1994).
Burmeister et al., “Crystal structure of the complex of rat neonatal Fc receptor with Fc,”Nature372:379-383 (1994).
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 Med173(6): 1483-91 (1991).
Caron, et al., “Engineered humanized dimeric forms of IgG are more effective antibodies,”J Exp Med176(4): 1191-5 (1992).
Chapman, et al., “Characterization of the Interaction Between the Herpes Simplex Virus Type 1 Fc Receptor and Immunoglobulin G.,”J. Biol. Chem.274(11): 6911-9 (1999).
Chappel, et al., “Identification of a secondary Fc gamma RI binding site within a genetically engineered human IgG antibody,”J Biol Chem268(33): 25124-31 (1993).
Chaudhury et al., “The Major Histocompatibility Complex-related Fc Receptor for IgG (FcRn) Binds Albumin and Prolongs Its Lifespan,”J. Exp. Med.197(3), 315-322 (Feb. 3, 2003).
Cole, et al., “Human IgG2 variants of chimeric anti-CD3 are nonmitogenic to T cells,”J Immunol159(7): 3613-21 (1997).
Cole, et at., “HuM291, A Humanized Anti-CD3 Antibody, is Immunosuppressive to T Cells While Exhibiting Reduced Mitogenicity in Vitro,”Transplantation, 68(4): 563-71 (1999).
Dall'Acqua, et al., “Increasing the Affinity of a Human IgG1 for the Neonatal Fc Receptor: Biological Consequences,”J. Immunol.169(9): 5171-80 (2002).
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,”Biochemistry20:2361-2370 (1981).
Delano, et al., “Convergent Solutions to Binding at a Protein-Protein Interface,”Science, 287(5456): 1279-83 (2000).
Dorai, et al., “Role of inter-heavy and light chain disulfide bonds in the effector functions of human immunoglobulin IgG1,”Mol Immunol29(12): 1487-91 (1992).
Duncan, et al., “The binding site for C1q on IgG,”Nature332(6166): 738-40 (1988).
Ehrlich et al., “Characterization of human monoclonal antibodies directed against hepatitis B surface antigen,”Hum. Antibodies Hybridomas3:2-7 (1992).
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, 14(7): 761-6 (2002).
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., 13(8): 993-1002 (2001).
Ghetie and Ward, “Multiple roles for the major histocompatibility complex class I- related receptor FcRn,”Annu. Rev. Immunol.18:739-766 (2000).
Ghetie et al., “Increasing the serum persistence of an IgG fragment by random mutagenesis,”Nat. Biotechnol.15:637-640 (1997).
Helm, et al., “Identification of the high affinity receptor binding region in human immunoglobulin E,”J Biol Chem271(13): 7494-500 (1996).
Hezareh, et al., “Effector Function Activities of a Panel of Mutants of a Broadly Neutralizing Antibody Against Human Immunodeficiency Virus Type,”J. Virol., 75(24): 12161-8 (2001).
Hinton et al., “Engineered Human IgG Antibodies with Longer Serum Half-lives in Primate,” J. Biol. Chem. 279(8) 6213-6216 (2004).
Homick, et al., “Single Amino Acid Substitution in the Fc Region of Chimeric TNT-3 Antibody Accelerates Clearance and Improves Immunoscintigraphy of Solid Tumors,”J. Nucl. Med.41(2): 355-62 (2000).
Isaacs, et al., “Therapy with monoclonal antibodies. II. The contribution of Fc gamma receptor binding and the influence of C(H)1 and C(H)3 domains on in vivo effector function,”J Immunol161(8): 3862-9 (1998).
Ito, et al., “[An amino acid substitution determining G1m(x) allotypic marker],”Nippon Hoigaku Zasshi43(2): 155-60 (1989).
Jendeberg, et al., “Engineering of Fc(1) and Fc(3) from human immunoglobulin G to analyse subclass specificity for staphylococcal protein A,”J Immunol Methods201(1): 25-34 (1997).
Jol

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

Alteration of FcRn binding affinities or serum half-lives of... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Alteration of FcRn binding affinities or serum half-lives of..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Alteration of FcRn binding affinities or serum half-lives of... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3735776

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