Claims for Patent: 10,377,832

Summary for Patent: 10,377,832

Title:	Modified glycoproteins
Abstract:	Modified glycoproteins, and methods of making and using such modified glycoproteins, are described.
Inventor(s):	Washburn; Nathaniel (Littleton, MA), Meador, III; James (Framingham, MA), Bosques; Carlos J. (Arlington, MA), Bulik; Dorota A. (Malden, MA), Bhatnagar; Naveen (Framingham, MA), Brown; Julia (Somerville, MA), Markowitz; Lynn (Waltham, MA), Prabbhakar; Sathya (Boxborough, MA)
Assignee:	Momenta Pharmaceuticals, Inc. (Cambridge, MA)
Application Number:	15/497,057
Patent Claims:	1. A method of producing a preparation of recombinant glycoprotein, the method comprising: expressing in a cell a recombinant glycoprotein comprising a modified amino acid sequence of a reference glycoprotein, the reference glycoprotein comprising an immunoglobulin Fc region or Fc fragment, wherein the recombinant glycoprotein comprises an Fc region or Fc fragment comprising two amino acid substitutions relative to the Fc region or Fc fragment of the reference glycoprotein, wherein the two amino acid substitutions are F241A/F243A, F241A/K246A, F241A/T260A, F241A/R301A, F243A/K246A, F243A/T260A, F243A/R301A, K246A/T260A, K246A/R301A, or T260A/R301A, as numbered according to the EU numbering index of Kabat; and isolating the recombinant glycoprotein, thereby producing the preparation of recombinant glycoprotein, wherein the preparation has an increased level of one or more of sialylated glycans, fucosylated glycans, and N-acetylglucosamine glycans, relative to a preparation of the reference glycoprotein. 2. The method of claim 1, wherein the recombinant glycoprotein of the preparation has a different Fc receptor affinity, Fc receptor specificity, complement activation activity, signaling activity, targeting activity, effector function, half-life, clearance, anti-inflammatory activity, or transcytosis activity than the reference glycoprotein. 3. The method of claim 2, wherein the effector function is antibody dependent cellular cytotoxicity, complement dependent cytotoxicity, programmed cell death, or cellular phagocytosis. 4. The method of claim 2, wherein the recombinant glycoprotein of the preparation has a different Fc receptor affinity or Fc receptor specificity than the reference glycoprotein, wherein the Fc receptor is an Fc.gamma.RT, Fc.gamma.RIIA, Fc.gamma.RIIB, Fc.gamma.RIIIA, Fc.gamma.RIIIB, Fc.gamma.RIV, or FcRn receptor. 5. The method of claim 4, wherein the recombinant glycoprotein of the preparation binds to a macrophage, neutrophil, or eosinophil. 6. The method of claim 1, wherein the reference glycoprotein is an antibody. 7. The method of claim 6, wherein the antibody is abciximab, adalimumab, alemtuzumab, basiliximab, bevacizumab, cetuximab, certolizumab, daclizumab, eculizumab, efalizumab, gemtuzumab, ibritumomab, infliximab, muromonab, natalizumab, omalizumab, palivizumab, panitumumab, ranibizumab, rituximab, tositumomab, or trastuzumab. 8. The method of claim 1, wherein the preparation of the recombinant glycoprotein comprises an increased level of sialylated glycans relative to a preparation of the reference glycoprotein. 9. The method of claim 1, wherein the preparation of the recombinant glycoprotein comprises an increased level of fucosylated glycans relative to a preparation of the reference glycoprotein. 10. The method of claim 1, wherein the preparation of the recombinant glycoprotein comprises an increased level of N-acetylglucosamine glycans relative to a preparation of the reference glycoprotein. 11. The method of claim 8, wherein the level of sialylated glycans is increased by 10% to 500% relative to a preparation of the reference glycoprotein. 12. The method of claim 9, wherein the level of fucosylated glycans is increased by 10% to 500% relative to a preparation of the reference glycoprotein. 13. The method of claim 10, wherein the level of N-acetylglucosamine glycans is increased by 10% to 500% relative to a preparation of the reference glycoprotein. 14. The method of claim 1, wherein the recombinant glycoprotein of the preparation comprises two Fc regions, wherein one of the two Fc regions comprises two amino acid substitutions relative to the Fc region of the reference glycoprotein, wherein the two amino acid substitutions are selected from the group consisting of F241A/F243A, F241A/K246A, F241A/T260A, F241A/R301A, F243A/K246A, F243A/T260A, F243A/R301A, K246A/T260A, K246A/R301A, and T260A/R301A, as numbered according to the EU numbering index of Kabat. 15. The method of claim 1, wherein the glycoprotein of the preparation comprises two Fc regions, wherein the two Fc regions each comprises two amino acid substitutions relative to the Fc region of the reference glycoprotein, wherein the two amino acid substitutions are selected from the group consisting of F241A/F243A, F241A/K246A, F241A/T260A, F241A/R301A, F243A/K246A, F243A/T260A, F243A/R301A, K246A/T260A, K246A/R301A, and T260A/R301A, as numbered according to the EU numbering index of Kabat.

Details for Patent 10,377,832

Applicant	Tradename	Biologic Ingredient	Dosage Form	BLA	Approval Date	Patent No.	Expiredate
Janssen Biotech, Inc.	REOPRO	abciximab	Injection	103575	December 22, 1994		2032-04-25
Genentech, Inc.	RITUXAN	rituximab	Injection	103705	November 26, 1997		2032-04-25
Hoffmann-la Roche Inc.	ZENAPAX	daclizumab	Injection	103749	December 10, 1997		2032-04-25