IP Library Granted Patent US 7,041,487
Granted Patent B2
US 7,041,487 · App. 10/206,443 · Granted May 9, 2006

Recombinant α-L-iduronidase, methods for producing and purifying the same and methods for treating diseases caused by deficiencies thereof

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Quick Facts
Patent No.
US 7,041,487
App. No.
10/206,443
Granted
May 9, 2006
Kind
B2
Abstract

The present invention provides a recombinant α-L-iduronidase and biologically active fragments and mutants thereof, methods to produce and purify this enzyme as well as methods to treat certain genetic disorders including-α-L-iduronidase deficiency and mucopolysaccharidosis I (MPS 1).

Claims (37)

1. A recombinant α-L-iduronidase enzyme with a purity of equal to or greater than 99%, wherein said recombinant α-L-iduronidase enzyme comprises:

(a) the amino acid sequence of residues 26 to 653 of SEQ ID NO:2, or a biologically active fragment of SEQ ID NO:2 which retains α-L-iduronidase enzyme biological activity; and

(b) one or more mannose-6-phosphate residues.

2. The recombinant α-L-iduronidase enzyme of claim 1 with a specific activity greater than 200,000 units per milligram protein.

3. The recombinant α-L-iduronidase enzyme of claim 2 with a specific activity greater than 240,000 units per milligram protein.

4. The recombinant α-L-iduronidase enzyme of claim 1 , wherein said recombinant α-L-iduronidase enzyme is a recombinant human α-L-iduronidase enzyme.

5. A recombinant α-L-iduronidase enzyme with a purity of equal to or greater than 99%, wherein said recombinant α-L-iduronidase enzyme comprises

(a) the amino acid sequence of residues 26 to 653 of SEQ ID NO:2, or a biologically active fragment of SEQ ID NO:2 which retains α-L-iduronidase enzyme biological activity; and

(b) has a specific activity greater than 200,000 units per milligram protein.

6. The recombinant α-L-iduronidase enzyme of claim 1 comprising a mannose-6-phosphate residue attached at position 3 and a mannose-6-phosphate residue attached at position 6.

7. The recombinant α-L-iduronidase enzyme of claim 1 , wherein said recombinant α-L-iduromdase enzyme has a half-life inside a cell of approximately 5 days.

8. A formulation of a pharmaceutical composition comprising said recombinant α-L-iduronidase enzyme of claim 1 alone or in combination with a pharmaceutically suitable carrier.

9. The formulation of claim 8 further comprising a sodium chloride solution, a buffer and human albumin.

10. The formulation of claim 9 wherein said α-L-iduronidase enzyme is present at a concentration of about 0.05 to 0.20 mg/mL or about 12,500 to about 50,000 units per mL.

11. The formulation of claim 10 wherein said human albumin is present at a concentration of at least about 1 mg/mL.

12. The formulation of claim 11 wherein said buffer is a sodium phosphate buffer at a concentration of about 10–50 mM.

13. The formulation of claim 12 wherein the pH of said sodium chloride solution is about 5.8.

14. The formulation of claim 8 wherein administration of said formulation to a human patient results in the human patient exhibiting a greater than 50% reduction in the excretion of undegraded GAG, wherein said human patient manifests a clinical phenotype of MPS-I prior to said administration.

15. The formulation of claim 14 wherein said reduction is greater than 65% following 8 weeks of treatment.

16. The formulation of claim 8 wherein administration of said formulation to a human patient results in the human patient exhibiting an increase of leukocyte iduronidase activity to 5.86 units per mg protein, wherein said human patient manifests a clinical phenotype of MPS-I prior to said administration.

17. The formulation of claim 8 wherein administration of said formulation to a human patient for 6 weeks results in a reduction in the size of the liver of the human patient, wherein said human patient manifests a clinical phenotype of MPS-I prior to said administration.

18. The formulation of claim 8 wherein administration of said formulation to a human patient for 6 weeks results in a reduction in the size of the spleen of the human patient, wherein said human patient manifests a clinical phenotype of MPS-I prior to said administration.

19. The recombinant α-L-iduronidase enzyme of claim 5 with a specific activity greater than 240,000 units per milligram protein.

20. The recombinant α-L-iduronidase enzyme of claim 5 , wherein said recombinant α-L-iduronidase enzyme is a recombinant human α-L-iduronidase enzyme.

21. The recombinant α-L-iduronidase enzyme of claim 5 comprising a mannose-6-phosphate residue attached at position 3 and a mannose-6-phosphate residue attached at position 6.

22. The recombinant α-L-iduronidase enzyme of claim 5 , wherein said recombinant α-L-iduronidase enzyme has a half-life inside a cell of approximately 5 days.

23. A formulation of a pharmaceutical composition comprising said recombinant α-L-iduronidase of claim 5 alone or in combination with a pharmaceutically suitable carrier.

24. The formulation of claim 23 further comprising a sodium chloride solution, a buffer and human albumin.

25. The formulation of claim 24 wherein said α-L-iduronidase enzyme is present at a concentration of about 0.05 to 0.20 mg/mL or about 12,500 to about 50,000 units per mL.

26. The formulation of claim 25 wherein said human albumin is present at a concentration of at least about 1 mg/mL.

27. The formulation of claim 26 wherein said buffer is a sodium phosphate buffer at a concentration of about 10–50 mM.

28. The formulation of claim 27 wherein the pH of said sodium chloride solution is about 5.8.

29. The formulation of claim 23 wherein administration of said formulation to a human patient results in the human patient exhibiting a greater than 50% reduction in the excretion of undegraded GAG, wherein said human patient manifests a clinical phenotype of MPS-I prior to said administration.

30. The formulation of claim 29 wherein said reduction is greater than 65% following 8 weeks of treatment.

31. The formulation of claim 23 wherein administration of said formulation to a human patient results in the human patient exhibiting an increase of leukocyte iduronidase activity to 5.86 units per mg protein, wherein said human patient manifests a clinical phenotype of MPS-I prior to said administration.

32. The formulation of claim 23 wherein administration of said formulation to a human patient for 6 weeks results in a reduction in the size of the liver of the human patient, wherein said human patient manifests a clinical phenotype of MPS-I prior to said administration.

33. The formulation of claim 23 wherein administration of said formulation to a human patient for 6 weeks results in a reduction in the size of the spleen of the human patient, wherein said human patient manifests a clinical phenotype of MPS-I prior to said administration.

Assignments (11)
ASSIGNMENT OF SECURITY INTEREST IN PATENTS TO ROYALTY SECURITIZATION TRUST I Recorded Oct 20, 2014
From: DEUTSCHE BANK TRUST COMPANY AMERICAS
To: ROYALTY SECURITIZATION TRUST I
Reel/Frame 034018/0628 →
ASSIGNMENT OF SECURITY INTEREST Recorded Oct 20, 2014
From: ROYALTY SECURITIZATION TRUST I
To: VALEANT HOLDINGS IRELAND
Reel/Frame 034018/0682 →
ASSIGNMENT OF SECURITY INTEREST Recorded Oct 20, 2014
From: PAUL ROYALTY FUND HOLDINGS II
To: VALEANT HOLDINGS IRELAND
Reel/Frame 034018/0812 →
ASSIGNMENT OF SECURITY INTEREST Recorded Oct 16, 2014
From: PAUL ROYALTY FUND II, L.P.
To: PAUL ROYALTY FUND HOLDINGS II
Reel/Frame 034012/0685 →
TRANSFER OF GRANTEE'S (DEBTOR'S) RIGHTS UNDER CERTAIN SECURITY INTEREST AGREEMENTS TO NEW GRANTEE (SECURED PARTY) Recorded Jan 12, 2005
From: ROYALTY SECURITIZATION TRUST I
To: DEUTSCHE BANK TRUST COMPANY AMERICAS (AS INDENTURE TRUSTEE)
Reel/Frame 015584/0474 →
TRANSFER FOR GRANTEE'S (DEBTOR'S) RIGHTS UNDER CERTAIN SECURITY INTEREST AGREEMENTS TO NEW GRANTEE (SECURED PARTY) Recorded Jan 11, 2005
From: ROYALTY FINANCIAL COMPANY LLC
To: ROYALTY SECURITIZATION TRUST I
Reel/Frame 015577/0341 →
TRANSFER OF GRANTEE'S (DEBTOR'S) RIGHTS UNDER CERTAIN SECURITY INTEREST AGREEMENTS TO NEW GRANTEE (SECURED PARTY) Recorded Jan 10, 2005
From: PAUL ROYALTY FUND, L.P.
To: ROYALTY FINANCIAL COMPANY LLC
Reel/Frame 015580/0887 →
CHANGE OF NAME Recorded Nov 22, 2004
From: HARBOR-UCLA RESEARCH AND EDUCATION INSTITUTE
To: LOS ANGELES BIOMEDICAL RESEARCH INSTITUTE AT HARBOR-UCLA MEDICAL CENTER
Reel/Frame 015398/0139 →
SECURITY INTEREST Recorded Jun 23, 2004
From: HARBOR-UCLA RESEARCH AND EDUCATION INSTITUTE
To: PAUL ROYALTY FUND, L.P.
Reel/Frame 014767/0890 →
SECURITY INTEREST Recorded Dec 8, 2003
From: HARBOR-UCLA RESEARCH AND EDUCATION INSTITUTE
To: PAUL ROYALTY FUND II, L.P.
Reel/Frame 014770/0262 →
SECURITY INTEREST Recorded Dec 8, 2003
From: HARBOR-UCLA RESEARCH AND EDUCATION INSTITUTE
To: PAUL ROYALTY FUND, L.P.
Reel/Frame 014772/0426 →