Monoclonal antibodies with enhanced ADCC function

Details Monoclonal antibodies with enhanced ADCC function Monoclonal antibodies with enhanced ADCC function

2011-04-26

2011-04-26

Dahle, Chun (Department: 1644)

Drug, bio-affecting and body treating compositions

Immunoglobulin, antiserum, antibody, or antibody fragment,...

C424S141100, C424S143100, C424S152100

Reexamination Certificate

active

07931895

ABSTRACT:
The invention concerns a method for obtaining and selecting monoclonal antibodies by an ADDC-type test, said antibodies capable of activating type III Fcy receptors and having a particular glycan structure. The inventive anti-D antibodies can be used for preventing Rhesus isoimmunisation in Rh negative persons, in particular for haemolytic disease in a new-born baby of for uses such as idiopathic thrombocytopenic pupura 9ITP).

REFERENCES:
patent: 5830470 (1998-11-01), Nakamura et al.
patent: 5843708 (1998-12-01), Hardman et al.
patent: 7214775 (2007-05-01), Hanai et al.
patent: 0 249 557 (1987-12-01), None
patent: 0 251 440 (1988-01-01), None
patent: 0 576 093 (1993-12-01), None
patent: 1 176 195 (2002-01-01), None
patent: 1 229 125 (2002-08-01), None
patent: 2 653 561 (1991-04-01), None
patent: 2 094 462 (1997-10-01), None
patent: WO-85/02413 (1985-06-01), None
patent: WO-89/02442 (1989-03-01), None
patent: WO-89/02600 (1989-03-01), None
patent: WO 99/54342 (1999-10-01), None
patent: WO 00/61739 (2000-10-01), None
patent: WO 01/29246 (2001-04-01), None
patent: WO 02/30954 (2002-04-01), None
patent: WO 02/31140 (2002-04-01), None
patent: WO 03/055993 (2003-07-01), None
patent: WO 03/084569 (2003-10-01), None
patent: WO 03/084570 (2003-10-01), None
patent: WO 03/085102 (2003-10-01), None
patent: WO 03/085107 (2003-10-01), None
patent: WO 03/085118 (2003-10-01), None
patent: WO 03/085119 (2003-10-01), None
Kilmartin et al. The Journal of Cell Biology. 1982. 93:576-582.
Shinkawa et al. The Journal of Biological Chemistry. 2003. 278;5:3466-3473.
Vitetta et al. Science. 2006. 313:308-309.
Hutchins et al. PNAS. 1995. 92:11980-11984.
Bihoreau et al., “Combination of capillary electrophoresis and matrix-assisted laser description ionization mass spectrometry for glycosylation analysis fo a human monoclonal anti-Rhesus(D) antibody,” Journal of Chromatography B: Biomedical Sciences & Applications, Elsevier Science Publishers, vol. 697, No. 1-2, Sep. 12, 1997, pp. 123-133, XP0004090752, ISSN: 0378-4347.
Bredius et al., “Role of neutrophil Fc-gamma-RIIa (CD32) and Fc-gamma-RIIIb (CD16 polymorphic forms in phagocytosis of human IfG1- and IgG3-opsonized bacteria and erythrocytes,” Immunology, vol. 83, No. 4, 1994, pp. 624-630, XP000971450, ISSN: 0019-2805.
Hadley, et al., “The functional activity of Fc.gamma.RII and Fc.gamma.RIII on subsets of human lymphocytes,” Immunology, 1992, vol. 76, No. 3, pp. 446-451, XP001015733.
Klein et al., “Human recombinant anti-Rh(D) monoclonal antibodies: Improvement of biological properties by in vitro class-switch,” Human Antibodies, vol. 8, No. 1, 1997, pp. 17-25, XP001015726, ISSN: 1093-2607.
Paterson et al., “Variation in IfF1 heavy chain allotype does not contribute to differences in biological activity of two human anti-Rhesus (D) monoclonal antibodies,” Immunotechnology, Elsevier Science Publishers BV, vol. 4, No. 1, Jun. 1, 1998, pp. 37-47, XP004127385, ISSN: 1380-2933.
Ugen et al., “New recombinant multimer of two fusion proteins, each including part of C4 binding protein; recombinant complement-C4 binding protein and CD4, CD8, CD16, CD35, Rhesus-D, antigen, enzyme or single chain antibody fusion protein multimer for use as a recombinant vaccine or diagnostic,” Vaccine, Butterworth Scientific, Guildford, Great Britain, vol. 15, No. 8, Jun. 1, 1997, p. 935, XP004075692, ISSN: 0264-410X.
Keen, M.J., “The culture of rat myeloma and rat hybridoma cells in a protein-free medium,” Cytotechnology, 1995, 17:193-202.
Lifely et al., “Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions,” Glycobiology, 1995, 5(8):813-822.
Shitara et al., “A new vector for the high level expression of chimeric antibodies in myeloma cells,” J. Immun. Methods, 1994, 167:271-278.
“WinRho,” (http://www.winrho.com/winrho.html), Sep. 19, 2009. pp. 1-3.
Boylston, A. W., et al.; “Production of Human IgM Anti-D in Tissue Culture by EB-Virus-transformed Lymphocytes”; Scand. J. Immunol., 12, 355-358, 1980.
Bron, D. et al.; “Production of human monoclonal IgG antibodies against Rhesus (D) antigen”; Proc. Nat. Acad. Sci., vol. 81, pp. 3214-3217, May 1984.
Chouchane, L., et al.; “Molecular characterization of a human anti-Rh(D) antibody with a DH segment encoded by a germ-line sequence”; Eur. J. Biochem; 207:1115-1121 (1992).
Crawford, D. et al.; “Production of Human Monoclonal Antibody to Rhesus D Antigen”; The Lancet; pp. 386-388; Feb. 19, 1983.
Debre, M.; “Feasibility of administering Tegeline at home Restrospective study of the data concerning efficacy, safety and tolerance”; Pressre Med., 33:682-688 (2004).
Doyle, A. et al.; “In vitro Development of Human Monoclonal Antibody-Secreting Plasmacytomas”; Human Immunology; 13:199-209 (1985).
Edelman, L., et al.; “Obtaining a functional recombinant anti-rhesus (D) antibody using the baculovirus-insect cell expression system”; Immunology 91:13-19 (1997).
Foung, S., et al.; “Human Monoclonal Antibodies to Rh0(D)”; Vox Sang; 53:44-47 (1987).
Goossen, D. et al.; “Human monoclonal antibodies against blood group antigens”; Journal of Immunological Methods, 101 (1987) 193-200.
Issitt, P.; “Genetics of the Rh blood group system: some current concepts”; Medical Laboratory Sciences; 45:395-404 (1988).
Jefferis, R. et al.; “A comparative study of the N-linked oligosaccharide structures of human IgC subclass proteins”; Biochem. J. (1990) 268. 529-537.
Jefferis, R. et al.; Molecular Definition of Interaction Sites on Human IgG for Fc Receptors (huFcyR); Molecular Immunology, vol. 27, No. 12, pp. 1237-1240 (1990).
Koskimies; “Human Lymphoblastoid Cell Line Producing Specific Antibody against Rh-Antigen D”; Scand. J. Immunol. 11, 73-77, 1980.
Kumpel, B. et al.; “Galactosylation of human IgG monoclonal anti-D produced by EBV-transformed B-lymphoblastoid cell lines is dependent on culture method and affects Fc receptor-mediated functional activity”; Hum. Antibod. Hybridomas, vol. 5, 3 and 4 (1994).
Kumpel, B. et al.; “Human Rh D Monoclonal Antibodies (BRAD-3 and BRAD-5) Cause Accelerated Clearance of RhD+ Red Blood Cells and Suppression of Rh D Immunization in Rh D− Volunteers”; Blood, vol. 86, No. 5, pp. 1701-1709; Sep. 1, 1995.
Kumpel, B. M. et al.; “Human monoclonal anti-D antibodies”; British Journal of Haematology; 1989, 71, 125-129.
Leatherbarrow, R. et al.; “Effector Functions of a Monoclonal Aglycosylated Mouse IgG2a: Binding and Activation of Complement Component C1 and Interaction with Human Monocyte Fc Receptor”; Molecular Immunology, vol. 22, No. 4, pp. 407-415, 1985.
Little, S. F., et al.; “Passive Protection by Polyclonal Antibodies againstBacillus anthracisInfection in Guinea Pigs”; Infection and Immunity, pp. 5171-5175; (1997).
Lomas, C., et al.; “Demonstration of Seven Epitopes on the Rh Antigen D Using Human Monoclonal Anti-D Antibodies and Red Cells from D Categories”; Vox Sang; 57:261-264 (1989).
Lund, J. et al.; “A Protein Structural Change in Aglycosylated IgG3 Correlates with Loss of huFcyR1 and huFcyR111 Binding and/or Activation”; Molecular Immunology, vol. 27, No. 11, pp. 1145-1153 (1990).
Lund, J. et al.; “Control of IgG/Fc Glycosylation: A Comparison of Oligosaccharides from Chimeric Human/Mouse and Mouse Subclass Immunoglobulin Gs”; Molecular Immunology, vol. 30, No. 8, pp. 741-748 (1993).
Ma, J. et al.; Immunotherapeutic potential of antibodies produced in plants; Tibtech, vol. 13, pp. 522-527 (Dec. 1995).
McCann-Carter, M. et al.; “The production and evaluation of two human monoclonal anti-D antibodies”; Transfusion Medicine; 3:187-194 (1993).
Melamed, M. et al.; Senescence of a human lymphoblastoid clone produci

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