IP Library Granted Patent US 8,920,801
Granted Patent B2
US 8,920,801 · App. 14/194,463 · Granted Dec 30, 2014

Methods and compositions for increasing arylsulfatase A activity in the CNS

Inventors: William M. Pardridge (Pacific Palisades, CA); Ruben J. Boado (Agoura Hills, CA)
Assignee: ArmaGen Technologies, Inc.
C12N9/16C07K16/2869
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Quick Facts
Patent No.
US 8,920,801
App. No.
14/194,463
Granted
Dec 30, 2014
Kind
B2
Abstract

Provided herein are methods and compositions for treating a subject suffering from a deficiency in arylsulfatase A in the CNS. The methods include systemic administration of a bifunctional fusion antibody comprising an antibody to a human insulin receptor and an arylsulfatase A.

Claims (20)

1. A fusion antibody comprising: (a) an arylsulfatase A (ASA) monomer, and (b) a single-chain antibody; wherein the fusion antibody crosses the blood brain barrier (BBB).

2. The fusion antibody of claim 1 , wherein the ASA monomer is covalently linked to the carboxy terminus of the single-chain antibody.

3. The fusion antibody of claim 1 , wherein the ASA monomer is covalently linked to the amino terminus of the single-chain antibody.

4. The fusion antibody of claim 1 , wherein the fusion antibody is post-translationally modified by a sulfatase modifying factor type 1 (SUMF1).

5. The fusion antibody of claim 1 , wherein the fusion antibody comprises a formylglycine.

6. The fusion antibody of claim 1 , wherein the fusion antibody further comprises a linker between the ASA monomer and the single-chain antibody.

7. The fusion antibody of claim 1 , wherein the ASA specific activity of the fusion antibody is at least about 10 units/mg of protein.

8. The fusion antibody of claim 1 , wherein the ASA retains at least 20% of its activity compared to its activity as a separate entity.

9. The fusion antibody of claim 1 , wherein the ASA and the single-chain antibody each retains at least 20% of its activity, on a molar basis, compared to its activity as a separate entity.

10. The fusion antibody of claim 1 , wherein the single-chain antibody comprises a CDR1 corresponding to the amino acid sequence of SEQ ID NO:1, a CDR2 corresponding to the amino acid sequence of SEQ ID NO:2, or a CDR3 corresponding to the amino acid sequence of SEQ ID NO:3.

11. The fusion antibody of claim 1 , wherein the single-chain antibody comprises a CDR1 corresponding to the amino acid sequence of SEQ ID NO:4, a CDR2 corresponding to the amino acid sequence of SEQ ID NO:5, or a CDR3 corresponding to the amino acid sequence of SEQ ID NO:6.

12. The fusion antibody of claim 1 , wherein the fusion antibody crosses the BBB by binding an endogenous BBB receptor-mediated transport system.

13. The fusion antibody of claim 1 , wherein the fusion antibody crosses the BBB by binding an endogenous BBB receptor selected from the group consisting of the insulin receptor, transferrin receptor, leptin receptor, lipoprotein receptor, and the IGF receptor.

14. The fusion antibody of claim 1 , wherein the fusion antibody crosses the BBB by binding an insulin receptor.

15. A pharmaceutical composition comprising a therapeutically effective amount of the fusion antibody of claim 1 , and a pharmaceutically acceptable excipient.

16. The fusion antibody of claim 1 , wherein the fusion antibody catalyzes hydrolysis of 2-sulfate groups of cerebroside sulfate esters and sulfatide sphingolipids.

17. The fusion antibody of claim 1 , wherein the single-chain antibody comprises a VH region and a VL region.

18. The fusion antibody of claim 1 , wherein the single-chain antibody is a single-chain Fab, Fab′, F(ab)2, or Fv antibody.

19. The fusion antibody of claim 18 , wherein the single-chain antibody is a single-chain Fv (ScFv) antibody.

20. A fusion antibody comprising: (a) a fusion protein comprising the amino acid sequences of an immunoglobulin light chain and an arylsulfatase A monomer, and (b) an immunoglobulin heavy chain; wherein the fusion antibody crosses the blood brain barrier (BBB), wherein the amino acid sequence of the arylsulfatase A is covalently linked to the carboxy terminus of the amino acid sequence of the immunoglobulin light chain.

Assignments (4)
RELEASE OF SECURITY INTEREST Recorded Apr 11, 2020
From: JCR PHARMACEUTICALS CO., LTD.
To: ARMAGEN, INC.
Reel/Frame 052373/0585 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Nov 18, 2019
From: OXFORD FINANCE LLC
To: JCR PHARMACEUTICALS CO., LTD.
Reel/Frame 051042/0528 →
SECURITY INTEREST Recorded Feb 2, 2018
From: ARMAGEN, INC.
To: OXFORD FINANCE LLC, AS COLLATERAL AGENT AND LENDER
Reel/Frame 044815/0135 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded May 16, 2014
From: PARDRIDGE, WILLIAM M.; BOADO, RUBEN J.
To: ARMAGEN TECHNOLOGIES, INC.
Reel/Frame 032916/0978 →
Continuity (4)
Continuation 13862250 · Apr 12, 2013
Continuation 13609099 · Sep 10, 2012
Provisional Application 61566497 · Dec 2, 2011
Related Publication 20140294822A1 · Oct 2, 2014