IP Library Granted Patent US 12,091,695
Granted Patent B2
US 12,091,695 · App. 18/501,967 · Granted Sep 17, 2024

Compositions and methods for using engineered deubiquitinases for probing ubiquitin-dependent cellular processes

Inventors: Henry M. Colecraft (Robbinsville, NJ); Scott Kanner (New York, NY)
Assignee: The Trustees of Columbia University in the City of New York
C12N9/6472C12N15/85C12Q1/6883C12Y304/22A61K38/00C12Q2600/156
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 12,091,695
App. No.
18/501,967
Granted
Sep 17, 2024
Kind
B2
Abstract

The present disclosure provides, inter alia, a recombinant engineered deubiquitinase (DUB) and methods for treating or ameliorating an inherited ion channelopathy, such as long QT syndrome, Brugada syndrome, or cystic fibrosis, in a subject. Further provided are methods for screening mutations causing such inherited ion channelopathies for a trafficking-deficient mutation that is treatable by the recombinant engineered DUB disclosed herein.

Claims (33)

1. A vector comprising a nucleic acid molecule encoding a recombinant engineered deubiquitinase (DUB) comprising:

a) a catalytic unit comprising the catalytic domain of a deubiquitinase;

b) a protein binder comprising an antibody, or antigen binding fragment thereof, that specifically binds a target substrate protein for deubiquitination by the engineered DUB; and

c) a variable linker between the catalytic unit and the protein binder.

2. The vector of claim 1 , wherein the vector is a plasmid vector.

3. The vector of claim 1 , wherein the vector is a viral vector.

4. The vector of claim 3 , wherein the viral vector is an adenoviral vector.

5. The vector of claim 1 , wherein the nucleic acid molecule is an RNA molecule.

6. The vector of claim 1 , wherein the nucleic acid molecule is an mRNA molecule.

7. The vector of claim 1 , wherein the nucleic acid molecule is an DNA molecule.

8. The vector of claim 1 , wherein the nucleic acid molecule is a cDNA molecule.

9. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of a deubiquitinase, wherein the deubiquitinase is from the ubiquitin specific proteases (USP) family, the ovarian tumor proteases (OTU) family, the ubiquitin C-terminal hydrolases (UCH) family, the Josephin domain (Josephin) family, the motif interacting with ubiquitin-containing novel DUB (MINDY) family, or the JAB1/MPN/Mov34 metalloenzyme domain (JAMM) family.

10. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of a deubiquitinase from the USP family.

11. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of USP21.

12. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of a deubiquitinase from the OTU family.

13. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of OTUD1 or OTUD4.

14. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of Cezanne.

15. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of TRABID.

16. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of OTULIN.

17. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of USP21 and is capable of non-selectively eliminating all ubiquitin linkage types.

18. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of OTUD1 and is capable of selectively eliminating K63 ubiquitin linkages.

19. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of OTUD4 and is capable of selectively eliminating K48 ubiquitin linkages.

20. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of Cezanne and is capable of selectively eliminating K11 ubiquitin linkages.

21. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of TRABID and is capable of selectively eliminating K29 ubiquitin linkages, K33 ubiquitin linkages, or K29 and K33 ubiquitin linkages.

22. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of OTULIN and is capable of selectively eliminating Met1 ubiquitin linkages.

23. The vector of claim 1 , wherein the antibody is a nanobody, scFv, (scFv)2, Fab, Fab′, F(ab′)2, Fv, diabody, or a DARPin.

24. The vector of claim 1 , wherein the antibody is a scFv, (scFv)2, Fab, Fab′, F(ab′)2, Fv, antibody mimetic, or diabody.

25. The vector of claim 1 , wherein the antibody is a single domain antibody (dAb).

26. The vector of claim 1 , wherein the antibody is a nanobody.

27. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of Cezanne and the antibody is a nanobody.

28. The vector of claim 1 , wherein the catalytic unit comprises the catalytic domain of Cezanne and the antibody is a single domain antibody (dAb).

29. The vector of claim 1 , wherein the protein binder specifically binds an ion channel.

30. The vector of claim 29 , wherein the ion channel is KCNQ1, HERG, or CFTR.

Assignments (2)
CONFIRMATORY LICENSE Recorded Jan 22, 2024
From: COLUMBIA UNIV NEW YORK MORNINGSIDE
To: NATIONAL INSTITUTES OF HEALTH (NIH), U.S. DEPT. OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT
Reel/Frame 066360/0699 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Nov 10, 2023
From: COLECRAFT, HENRY M.; KANNER, SCOTT
To: THE TRUSTEES OF COLUMBIA UNIVERSITY IN THE CITY OF NEW YORK
Reel/Frame 065530/0010 →
Continuity (4)
Division 16867923 · May 6, 2020
Continuation In Part PCTUS2018059229 · Nov 5, 2018
Provisional Application 62582108 · Nov 6, 2017
Related Publication 20240067946A1 · Feb 29, 2024
Cited By (1)
US 12,312,618