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Last Updated: January 23, 2020

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Claims for Patent: 9,663,581

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Summary for Patent: 9,663,581
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:14/396,420
Patent Claims:1. A preparation comprising a glycoprotein comprising a modified amino acid sequence of a reference glycoprotein, the reference glycoprotein comprising an immunoglobulin Fc region or Fc fragment; wherein the glycoprotein of the preparation comprises an Fc region comprising two amino acid substitutions relative to the Fc region or Fc fragment of the reference glycoprotein, and 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, and wherein the preparation of the glycoprotein 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 preparation of claim 1, wherein the 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 preparation of claim 2, wherein the effector function is antibody dependent cellular cytotoxicity, complement dependent cytotoxicity, programmed cell death, or cellular phagocytosis.

4. The preparation of claim 2, wherein the 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 preparation of claim 4, wherein the glycoprotein of the preparation binds to a macrophage, neutrophil, or eosinophil.

6. The preparation of claim 1, wherein the reference glycoprotein is an antibody.

7. The preparation 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 preparation of claim 1, wherein the preparation of the glycoprotein comprises an increased level of sialylated glycans relative to a preparation of the reference glycoprotein.

9. The preparation of claim 1, wherein the preparation of the glycoprotein comprises an increased level of fucosylated glycans relative to a preparation of the reference glycoprotein.

10. The preparation of claim 1, wherein the preparation of the glycoprotein comprises an increased level of N-acetylglucosamine glycans relative to a preparation of the reference glycoprotein.

11. The preparation 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 preparation 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 preparation 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 preparation of claim 1, wherein the glycoprotein of the preparation comprises two Fc regions, wherein one of the Fc regions comprises two amino acid substitutions 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 relative to the Fc region or Fc fragment of the reference glycoprotein, as numbered according to the EU numbering index of Kabat.

15. The preparation of claim 1, wherein the glycoprotein of the preparation comprises two Fc regions, wherein the two Fc regions comprise two amino acid substitutions 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 relative to the Fc region or Fc fragment of the reference glycoprotein, as numbered according to the EU numbering index of Kabat.

Summary for Patent:   Start Trial

PCT Information
PCT FiledApril 24, 2013PCT Application Number:PCT/US2013/037997
PCT Publication Date:October 31, 2013PCT Publication Number:WO2013/163297

Details for Patent 9,663,581

Applicant Tradename Biologic Ingredient Dosage Form BLA Number Approval Date Patent No. Assignee Estimated Patent Expiration Status Orphan Source
Centocor Inc REOPRO abciximab INJECTABLE; INJECTION 103575 001 1994-12-22   Start Trial Momenta Pharmaceuticals, Inc. (Cambridge, MA) 2032-04-25 RX search
Genentech RITUXAN rituximab VIAL 103705 001 1997-11-26   Start Trial Momenta Pharmaceuticals, Inc. (Cambridge, MA) 2032-04-25 RX Orphan search
Novartis SIMULECT basiliximab VIAL; SINGLE-USE 103764 001 1998-05-12   Start Trial Momenta Pharmaceuticals, Inc. (Cambridge, MA) 2032-04-25 RX search
>Applicant >Tradename >Biologic Ingredient >Dosage Form >BLA >Number >Approval Date >Patent No. >Assignee >Estimated Patent Expiration >Status >Orphan >Source

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