IP Library Granted Patent US 11,351,231
Granted Patent B2
US 11,351,231 · App. 15/657,764 · Granted Jun 7, 2022

Lysosomal targeting peptides and uses thereof

Inventors: Jonathan LeBowitz (Novato, CA); John Maga (Novato, CA)
Assignee: BIOMARIN PHARMACEUTICAL INC.
A61K38/47C07K14/65C12N9/2408C12Y302/0102C07K2319/06C07K2319/33
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 11,351,231
App. No.
15/657,764
Granted
Jun 7, 2022
Kind
B2
Abstract

The present invention provides further improved compositions and methods for efficient lysosomal targeting based on the GILT technology. Among other things, the present invention provides methods and compositions for targeting lysosomal enzymes to lysosomes using furin-resistant lysosomal targeting peptides. The present invention also provides methods and compositions for targeting lysosomal enzymes to lysosomes using a lysosomal targeting peptide that has reduced or diminished binding affinity for the insulin receptor.

Claims (11)

1. A nucleic acid encoding a fusion protein comprising an amino acid sequence at least 70% identical to wild-type human acid alpha-glucosidase (GAA); a lysosomal targeting moiety, that is an IGF-II mutein comprising an amino acid sequence at least 70% identical to mature human IGF-II (SEQ ID NO:1), the IGF-II mutein having a mutation within a region corresponding to amino acids 30-40 of SEQ ID NO:1 such that said mutation abolishes at least one furin protease cleavage site, wherein the IGF-II mutein

comprises an amino acid substitution at a position corresponding to Arg37 of SEQ ID NO: 1, wherein the amino acid substitution is a Lys substitution and

(a) shows reduced or slowed susceptibility to furin cleavage compared to wild type human IGFII peptide,

(b) has diminished binding affinity for the insulin receptor relative to the affinity of naturally-occurring human IGF-II for the insulin receptor, and

(c) binds to the human cation-independent mannose-6-phosphate receptor in a mannose-6-phosphate-independent manner.

2. The nucleic acid of claim 1 , wherein the IGF- II mutein has diminished binding affinity for the IGF-I receptor relative to the affinity of naturally-occurring human IGF-II for the IGF-I receptor.

3. The nucleic acid of claim 1 , wherein the fusion protein comprises amino acids 70-952 of human GAA.

4. The nucleic acid of claim 3 , fusion protein further comprises a spacer between amino acids 70-952 of human GAA and the IGF-II mutein.

5. The nucleic acid of claim 4 , wherein the spacer comprises an amino acid sequence Gly-Ala-Pro.

6. An isolated cell containing the nucleic acid of claim 3 .

7. An isolated cell containing the nucleic acid of claim 1 .

Assignments (2)
SECURITY INTEREST Recorded Apr 27, 2026
From: BIOMARIN PHARMACEUTICAL INC.; AMICUS THERAPEUTICS, INC.
To: CITIBANK, N.A., AS COLLATERAL AGENT
Reel/Frame 075493/0968 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Sep 5, 2019
From: LEBOWITZ, JONATHAN H.; MAGA, JOHN
To: BIOMARIN PHARMACEUTICAL INC.
Reel/Frame 050286/0944 →
Continuity (6)
Continuation 15274115 · Sep 23, 2016
Continuation 14535505 · Nov 7, 2014
Continuation 12991104
Provisional Application 61144106 · Jan 12, 2009
Provisional Application 61051336 · May 7, 2008
Related Publication 20180125949A1 · May 10, 2018
Cited By (2)
US 12,329,801 US 12,358,963