Methods and vectors for generating asialylated immunoglobulins
| Title: | Methods and vectors for generating asialylated immunoglobulins |
|---|---|
| Patent Number: | 8,540,992 |
| Publication Date: | September 24, 2013 |
| Appl. No: | 12/521417 |
| Application Filed: | December 26, 2007 |
| Abstract: | The properties of an Fc-containing protein, for example, an antibody, are controlled by altering the sialylation of the oligosaccharides in the Fc region by transfecting the cell line expressing the Fc-containing protein with a vector sequence encoding a sialidase. The modified Fc-containing proteins have therapeutic utility in diseases or conditions in which it is desirable to control the affinity for one or more of the FcγRI, FcγRIIA, and FcγRIIIA receptors, ADCC activity, macrophage or monocyte activation, serum half-life, and avidity. |
| Inventors: | Naso, Michael (Radnor, PA, US); Raju, T. Shantha (Radnor, PA, US); Scallon, Bernard (Radnor, PA, US) |
| Claim: | 1. A method for providing a sialidase enzymatic activity in a culture comprising a mammalian cell engineered to express an antibody, comprising transfecting the mammalian engineered cell with a vector encoding a catalytic domain of Arthrobacter ureafaciens sialidase enzyme A, wherein the polypeptide is secreted into the culture along with the antibody, whereby the antibody glycans can be acted upon by the polypeptide sialidase enzymatic activity, and wherein one or more of the avidity for multiply localized target proteins, the macrophage or monocyte activation, and serum half-life of the antibody are altered. |
| Claim: | 2. The method of claim 1 , wherein the mammalian cell line is selected from the group consisting of COS-1, COS-7, HEK293, BHK21, CHO, BSC-1, Hep G2, 653, SP2/0, 293, HeLa, YB2/0 or Y3, myeloma, or lymphoma cells, or any derivative, immortalized or transformed cell thereof. |
| Claim: | 3. The method of claim 2 , wherein the antibody is an anti-TNFα antibody and the cell line is C168M. |
| Current U.S. Class: | 4241/411 |
| Patent References Cited: | 5275939 January 1994 Sugimori et al. 7026152 April 2006 Ingram et al. WO 99/54342 October 1999 WO 2004/003176 January 2004 WO 2004/047735 June 2004 WO 2005/016455 February 2005 |
| Other References: | Christensen et al. Biotechnol Appl Biochem. Jun. 2005;41(Pt 3):225-31 (abstract). cited by examiner Chica et al. Curr Opin Biotechnol. Aug. 2005;16(4):378-84. cited by examiner Sen et al. Appl Biochem Biotechnol. Dec. 2007;143(3):212-23. cited by examiner Hanauer. Aliment Pharmacol Ther. Sep. 1999;13 Suppl 4:16-22; discussion 38. cited by examiner PCT International Search Report dated Sep. 12, 2008. cited by applicant Dalziel, et al., “Lectin analysis of human immunoglobulin G N-glycan sialylation,” Glycoconjugage Journal, 16: 801-807 (1999). cited by applicant Scallon, et al., “Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality,” Molecular Immunology, 44: 1524-1534 (2007). cited by applicant Supplementary European Search Report dated Dec. 17, 2010. cited by applicant Bäckström, et al., “Recombinant MUC1 mucin with a breast cancer-like O-glycosylation produced in large amounts in Chinese-hamster ovary cells,” Biochemical Journal, 376: 677-686 (2003). cited by applicant Christensen, et al., “Cloning, expression and characterization of a sialidase gene from Arthrobacter ureafaciens,” Biotechnology and Applied Biochemistry, 41, 225-231 (2005). cited by applicant Davis, et al., “Active influence virus neuraminidase is expressed in monkey cells from cDNA cloned in simian virus 40 vectors,” Proceedings of the National Academy of Science USA, 80(13): 3976-3980 (1983). cited by applicant Eisenberg, et al., “The therapeutic potential of anti-CD20. What do B-cells do?,” Clinical Immunology, 117: 207-213 (2005). cited by applicant Ferrari, et al., “Cloning and expression of a soluble sialidase from Chinese hamster ovary cells: sequence alignment similarities to bacterial sialidases,” Glycobiology, 4(3): 367-373 (1994). cited by applicant GenBank Accession No. AAQ03260, Aug. 13, 1990. cited by applicant Geletka, et al., “Infliximab for the treatment of early rheumatoid arthritis,” Expert Opinions in Biological Therapy, 5: 405-417 (2005). cited by applicant He, et al., “Purification and Characterization of Recombinant, Human Acid Ceramidase,” The Journal of Biological Chemistry, 278(35): 32978-32986 (2003). cited by applicant Idusogie, et al., “Mapping of the C1q Binding Site on Rituxan, a Chimeric Antibody with a Human IgG1 Fc,” Journal of Immunology, 164: 4178-4184 (2000). cited by applicant Jefferis, et al., “IgF-Fc-mediated effector functions: molecular definition of interaction sites for effector ligans and the role of glycosylation,” Immunological Reviews, 163: 59-76 (1998). cited by applicant Lifely, et al., “Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions,” Glycobiology, 5(8): 813-822 (1995). cited by applicant Leonard Presta, “Antibody Engineering for Therapeutics,” Current Opinion in Structural Biology, 13(4): 519-525 (2003). cited by applicant Raju, et al., “Species-Specific Variation in Glycosylation of IgG: Evidence for the Species-Specific Sialylation and Branch-Specific Galactosylation and Importance for Engineering Recombinant Glycoprotein Therapeutics,” Glycobiology, 10(5):477-486 (2000). cited by applicant Richard J. Stockert, “The Asialoglycoprotein Receptor: Relationships Between Structure, Function, and Expression,” Physiological Reviews, 75(3): 591-609 (1995). cited by applicant Wright, et al., “Effect of Glycosylation on Antibody Function: Implications for Genetic Engineering,” Trends in Biotechnology, 15(1):26-32 (1997). cited by applicant |
| Primary Examiner: | Fronda, Christian |
| Attorney, Agent or Firm: | Dichter, Eric |
| Accession Number: | edspgr.08540992 |
| Database: | USPTO Patent Grants |
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| Items | – Name: Title Label: Title Group: Ti Data: Methods and vectors for generating asialylated immunoglobulins – Name: DocumentID Label: Patent Number Group: Patent Data: 8,540,992 – Name: DateEntry Label: Publication Date Group: Patent Data: September 24, 2013 – Name: DocumentID Label: Appl. No Group: Patent Data: 12/521417 – Name: DateFiled Label: Application Filed Group: Patent Data: December 26, 2007 – Name: Abstract Label: Abstract Group: Ab Data: The properties of an Fc-containing protein, for example, an antibody, are controlled by altering the sialylation of the oligosaccharides in the Fc region by transfecting the cell line expressing the Fc-containing protein with a vector sequence encoding a sialidase. The modified Fc-containing proteins have therapeutic utility in diseases or conditions in which it is desirable to control the affinity for one or more of the FcγRI, FcγRIIA, and FcγRIIIA receptors, ADCC activity, macrophage or monocyte activation, serum half-life, and avidity. – Name: Author Label: Inventors Group: Patent Data: <searchLink fieldCode="ZA" term="%22Naso%2C+Michael%22">Naso, Michael</searchLink> (Radnor, PA, US); <searchLink fieldCode="ZA" term="%22Raju%2C+T%2E+Shantha%22">Raju, T. Shantha</searchLink> (Radnor, PA, US); <searchLink fieldCode="ZA" term="%22Scallon%2C+Bernard%22">Scallon, Bernard</searchLink> (Radnor, PA, US) – Name: Comment Label: Claim Group: Patent Data: 1. A method for providing a sialidase enzymatic activity in a culture comprising a mammalian cell engineered to express an antibody, comprising transfecting the mammalian engineered cell with a vector encoding a catalytic domain of Arthrobacter ureafaciens sialidase enzyme A, wherein the polypeptide is secreted into the culture along with the antibody, whereby the antibody glycans can be acted upon by the polypeptide sialidase enzymatic activity, and wherein one or more of the avidity for multiply localized target proteins, the macrophage or monocyte activation, and serum half-life of the antibody are altered. – Name: Comment Label: Claim Group: Patent Data: 2. The method of claim 1 , wherein the mammalian cell line is selected from the group consisting of COS-1, COS-7, HEK293, BHK21, CHO, BSC-1, Hep G2, 653, SP2/0, 293, HeLa, YB2/0 or Y3, myeloma, or lymphoma cells, or any derivative, immortalized or transformed cell thereof. – Name: Comment Label: Claim Group: Patent Data: 3. The method of claim 2 , wherein the antibody is an anti-TNFα antibody and the cell line is C168M. – Name: CodeClass Label: Current U.S. Class Group: Patent Data: 4241/411 – Name: Ref Label: Patent References Cited Group: Patent Data: <searchLink fieldCode="RF" term="%225275939%22">5275939</searchLink> January 1994 Sugimori et al.<br /><searchLink fieldCode="RF" term="%227026152%22">7026152</searchLink> April 2006 Ingram et al.<br />WO 99/54342 October 1999<br />WO 2004/003176 January 2004<br />WO 2004/047735 June 2004<br />WO 2005/016455 February 2005<br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /><br /> – Name: Ref Label: Other References Group: Patent Data: Christensen et al. Biotechnol Appl Biochem. Jun. 2005;41(Pt 3):225-31 (abstract). cited by examiner<br />Chica et al. Curr Opin Biotechnol. Aug. 2005;16(4):378-84. cited by examiner<br />Sen et al. Appl Biochem Biotechnol. Dec. 2007;143(3):212-23. cited by examiner<br />Hanauer. Aliment Pharmacol Ther. Sep. 1999;13 Suppl 4:16-22; discussion 38. cited by examiner<br />PCT International Search Report dated Sep. 12, 2008. cited by applicant<br />Dalziel, et al., “Lectin analysis of human immunoglobulin G N-glycan sialylation,” Glycoconjugage Journal, 16: 801-807 (1999). cited by applicant<br />Scallon, et al., “Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality,” Molecular Immunology, 44: 1524-1534 (2007). cited by applicant<br />Supplementary European Search Report dated Dec. 17, 2010. cited by applicant<br />Bäckström, et al., “Recombinant MUC1 mucin with a breast cancer-like O-glycosylation produced in large amounts in Chinese-hamster ovary cells,” Biochemical Journal, 376: 677-686 (2003). cited by applicant<br />Christensen, et al., “Cloning, expression and characterization of a sialidase gene from Arthrobacter ureafaciens,” Biotechnology and Applied Biochemistry, 41, 225-231 (2005). cited by applicant<br />Davis, et al., “Active influence virus neuraminidase is expressed in monkey cells from cDNA cloned in simian virus 40 vectors,” Proceedings of the National Academy of Science USA, 80(13): 3976-3980 (1983). cited by applicant<br />Eisenberg, et al., “The therapeutic potential of anti-CD20. What do B-cells do?,” Clinical Immunology, 117: 207-213 (2005). cited by applicant<br />Ferrari, et al., “Cloning and expression of a soluble sialidase from Chinese hamster ovary cells: sequence alignment similarities to bacterial sialidases,” Glycobiology, 4(3): 367-373 (1994). cited by applicant<br />GenBank Accession No. AAQ03260, Aug. 13, 1990. cited by applicant<br />Geletka, et al., “Infliximab for the treatment of early rheumatoid arthritis,” Expert Opinions in Biological Therapy, 5: 405-417 (2005). cited by applicant<br />He, et al., “Purification and Characterization of Recombinant, Human Acid Ceramidase,” The Journal of Biological Chemistry, 278(35): 32978-32986 (2003). cited by applicant<br />Idusogie, et al., “Mapping of the C1q Binding Site on Rituxan, a Chimeric Antibody with a Human IgG1 Fc,” Journal of Immunology, 164: 4178-4184 (2000). cited by applicant<br />Jefferis, et al., “IgF-Fc-mediated effector functions: molecular definition of interaction sites for effector ligans and the role of glycosylation,” Immunological Reviews, 163: 59-76 (1998). cited by applicant<br />Lifely, et al., “Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions,” Glycobiology, 5(8): 813-822 (1995). cited by applicant<br />Leonard Presta, “Antibody Engineering for Therapeutics,” Current Opinion in Structural Biology, 13(4): 519-525 (2003). cited by applicant<br />Raju, et al., “Species-Specific Variation in Glycosylation of IgG: Evidence for the Species-Specific Sialylation and Branch-Specific Galactosylation and Importance for Engineering Recombinant Glycoprotein Therapeutics,” Glycobiology, 10(5):477-486 (2000). cited by applicant<br />Richard J. Stockert, “The Asialoglycoprotein Receptor: Relationships Between Structure, Function, and Expression,” Physiological Reviews, 75(3): 591-609 (1995). cited by applicant<br />Wright, et al., “Effect of Glycosylation on Antibody Function: Implications for Genetic Engineering,” Trends in Biotechnology, 15(1):26-32 (1997). cited by applicant – Name: AuthorEditor Label: Primary Examiner Group: Patent Data: <searchLink fieldCode="ZE" term="%22Fronda%2C+Christian%22">Fronda, Christian</searchLink> – Name: AuthorCorporate Label: Attorney, Agent or Firm Group: Patent Data: <searchLink fieldCode="ZG" term="%22Dichter%2C+Eric%22">Dichter, Eric</searchLink> – Name: AN Label: Accession Number Group: ID Data: edspgr.08540992 |
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| RecordInfo | BibRecord: BibEntity: Languages: – Text: English Titles: – TitleFull: Methods and vectors for generating asialylated immunoglobulins Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Naso, Michael – PersonEntity: Name: NameFull: Raju, T. Shantha – PersonEntity: Name: NameFull: Scallon, Bernard IsPartOfRelationships: – BibEntity: Dates: – D: 24 M: 09 Text: September 24, 2013 Type: published Y: 2013 |
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