IP Library Granted Patent US 12,329,816
Granted Patent B2
US 12,329,816 · App. 17/270,323 · Granted Jun 17, 2025

Immunotherapy with metabolic enzyme expression

Inventors: Joshua D. Rabinowitz (Princeton, NJ); Roderick O'Connor (Philadelphia, PA)
Assignees: The Trustees of Princeton University; The Trustees of the University of Pennsylvania
A61K45/06A61K38/50A61K40/11A61K40/31A61K40/4255A61P35/00C12N5/0636
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,329,816
App. No.
17/270,323
Granted
Jun 17, 2025
Kind
B2
Abstract

The present invention provides, in some embodiments, methods of promoting an immune response in a subject in need thereof, comprising administering to the subject a population of immune cells that express an enzyme that facilitates immune cell function in a nutrient-poor environment. The invention also provides, in other embodiments, compositions comprising an ex vivo population of immune cells expressing an enzyme that enhances immune cell function in a nutrient-poor environment.

Claims (20)

1. A composition comprising an ex vivo population of immune cells that express an enzyme that catalyzes the formation of aspartate from asparagine or the formation of alanine from pyruvate and glutamate.

2. The composition of claim 1 , wherein the immune cells are T cells.

3. The composition of claim 2 , wherein the immune cells are chimeric antigen receptor (CAR)-T cells.

4. The composition of claim 1 , wherein the enzyme is asparaginase.

5. The composition of claim 4 , wherein the asparaginase is a naturally-occurring asparaginase or a variant of a naturally-occurring asparaginase having at least about 80% amino acid sequence identity to a naturally-occurring asparaginase.

6. The composition of claim 4 , wherein the asparaginase comprises, consists essentially of or consists of the sequence of SEQ ID NO:1.

7. A method of promoting an immune response in a subject in need thereof, comprising administering to the subject an effective amount of a population of immune cells that express an enzyme that catalyzes the formation of aspartate from asparagine or the formation of alanine from pyruvate and glutamate.

8. A method for treating a cancer in a subject in need thereof, comprising administering to the subject an effective amount of a population of anti-cancer immune cells that express an enzyme that catalyzes the formation of aspartate from asparagine or the formation of alanine from pyruvate and glutamate.

9. The method of claim 7 , wherein the immune cells are T cells.

10. The method of claim 9 , wherein the immune cells are CAR-T cells.

11. The method of claim 7 , wherein the immune cells express asparaginase.

12. The method of claim 11 , wherein the asparaginase is a naturally-occurring asparaginase or a variant of a naturally-occurring asparaginase having at least about 80% amino acid sequence identity to a naturally-occurring asparaginase.

13. The method of claim 11 , wherein the asparaginase comprises, consists essentially of or consists of the sequence of SEQ ID NO:1.

14. The method of claim 7 , further comprising administering one or more additional therapeutic agents to the subject.

15. The method of claim 14 , wherein the one or more additional therapeutic agents comprises a checkpoint inhibitor.

16. The method of claim 15 , wherein the checkpoint inhibitor is a PD-1, PD-L1 or CTLA-4 checkpoint inhibitor.

17. A method of enhancing an immunotherapy in a subject receiving the immunotherapy, comprising administering to the subject an effective amount of a population of immune cells that express an enzyme that catalyzes the formation of aspartate from asparagine or the formation of alanine from pyruvate and glutamate.

18. The method of claim 17 , wherein the immunotherapy comprises a checkpoint inhibitor.

19. The method of claim 18 , wherein the checkpoint inhibitor is a PD-1, PD-L1 or CTLA-4 checkpoint inhibitor.

20. The method of claim 17 , wherein the immunotherapy is a CAR-T therapy.

Assignments (3)
CONFIRMATORY LICENSE Recorded Nov 22, 2023
From: PRINCETON UNIVERSITY
To: NATIONAL INSTITUTES OF HEALTH (NIH), U.S. DEPT. OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT
Reel/Frame 065664/0726 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 12, 2022
From: RABINOWITZ, JOSHUA D.
To: THE TRUSTEES OF PRINCETON UNIVERSITY
Reel/Frame 062054/0640 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 12, 2022
From: O'CONNOR, RODERICK
To: THE TRUSTEES OF THE UNIVERSITY OF PENNSYLVANIA
Reel/Frame 062054/0718 →
Continuity (2)
Provisional Application 62722518 · Aug 24, 2018
Related Publication 20210379109A1 · Dec 9, 2021
References Cited (13)
US 20160361360A1 · Chang · 2016 [cited by examiner]
WO 2020041662A1 · 2020 [cited by applicant]
Ron-Harel et al., Mitochondrial biogenesis and proteome remodeling promote one-carbon metabolism for T cell activation; 2016, Cell Metabolism, 24: 104-117. (Year: 2016). [cited by examiner]
Ron-Harel et al., T cell activation depends on extracellular alanine; 2019, Cell Reports, 28: 3011-3021. (Year: 2019). [cited by examiner]
Mackenzie et al., Functional properties and cellular distribution of the system A glutamine transporter SNAT1 support specialized roles in central neurons; 2003, 278(26): 23720-23730. (Year: 2003). [cited by examiner]
Notification of International Preliminary Report on Patentability of International Application No. PCT/US2019/047830, entitled: “Immunotherapy With Metabolic Enzyme Expression,” mailed Mar. 2, 2021. [cited by applicant]
Belviso, S. et al., “The human asparaginase enzyme (ASPG) inhibits growth in leukemic cells,” PLOS, vol. 12; No. 5; 14 pages (2017). [cited by applicant]
Caruana, I. ct al., “Heparanasc promotes tumor infiltration and antitumor activity of CAR-redirected T lymphocytes,” Nature Medicine, vol. 21; No. 5; 524-529 (2015). [cited by applicant]
Pavlova, N.N. et al., “As Extracellular Clutamine Levels Decline, Asparagine Decomes an Essential Amino Acid,” Cell Metabolism, vol. 27; 428-438 (2018). [cited by applicant]
Rigouin, C. et al., “Discovery of human-like L-asparaginases with potential clinical use by directed evolution,” Scientific Reports, vol. 7; No. 1; 10224; 13 pages (2017). [cited by applicant]
Sullivan, L.B. et al., “Aspartate is an endogenous metabolic limitation for tumor growth,” Nature Cell Biology, vol. 20; No. 7; 782-788 (2018). [cited by applicant]
Zhang, J. et al., “Asparagine Plays a Critical Role in Regulating Cellular Adaptation to Glutamine Depletion,” Molecular Cell, vol. 56; 205-218 (2014). [cited by applicant]
Notification of Transmittal of the International Search Report and the Written Opinion of International Application No. PCT/US2019/047830, entitled: “Immunotherapy With Metabolic Enzyme Expression,” mailed Dec. 10, 2019. [cited by applicant]