IP Library › Granted Patent US 10,118,953
Granted Patent B2
US 10,118,953 · App. 15/643,787 · Granted Nov 6, 2018

Glucocorticoid-induced tumor necrosis factor receptor ligand (GITRL) single-chain fusion polypeptides

Inventors: Oliver Hill (Neckarsteinach, DE); Christian Gieffers (Dossenheim, DE); Meinolf Thiemann (Schriesheim, DE)
Assignee: APOGENIX AG
C07K14/525C07K14/70575C07K14/70578C07K16/00C12N15/62C12N15/79A61K38/00C07K2317/41C07K2317/52C07K2317/55C07K2319/00C07K2319/22C07K2319/30C07K2319/32C07K2319/35C07K2319/74
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 10,118,953
App. No.
15/643,787
Granted
Nov 6, 2018
Kind
B2
Abstract

The present invention refers to single-chain fusion proteins comprising three soluble TNF superfamily (TNFSF) cytokine domains and nucleic acid molecules encoding these fusion proteins. The fusion proteins are substantially non-aggregating and suitable for therapeutic, diagnostic and/or research applications.

Claims (19)

1. A single-chain fusion polypeptide comprising:

(i) a first soluble glucocorticoid-induced tumor necrosis factor receptor ligand ligand (GITRL) cytokine domain,

(ii) a first peptide linker,

(iii) a second soluble GITRL cytokine domain,

(iv) a second peptide linker, and

(v) a third soluble GITRL cytokine domain,

wherein each of the soluble GITRL cytokine domains lacks a stalk region and the first and the second peptide linkers independently have a length of 3-8 amino acids.

2. The polypeptide of claim 1 , wherein the first, the second, and the third soluble GITRL cytokine domains are independently an N-terminally shortened domain of SEQ ID NO:18, and optionally consists of an amino acid mutation.

3. The polypeptide of claim 1 , wherein the first, the second, and the third soluble GITRL cytokine domains independently have the amino sequence of 52-177 of SEQ ID NO: 18.

4. The polypeptide of claim 1 , wherein the first and second peptide linkers are, independently, glycine/serine linkers.

5. The polypeptide of claim 4 , wherein the glycine/serine linkers comprise substituted asparagine residues.

6. The polypeptide of claim 1 , wherein the first and second peptide linkers are independently selected from the group consisting of SEQ ID NO: 52-53 and SEQ ID NO: 1-26.

7. The polypeptide of claim 1 , which additionally comprises an N-terminal signal peptide domain.

8. The polypeptide of claim 7 , wherein the N-terminal signal peptide domain comprises a protease cleavage site.

9. The polypeptide of claim 1 , which additionally comprises a further domain at the N-terminal and/or C-terminal end.

10. The polypeptide of claim 1 , which additionally comprises a further domain and a third peptide linker at the C-terminal end.

11. A dimer comprising two polypeptides of claim 10 , wherein the two polypeptides are dimerized via disulfide bridges of the third peptide linkers.

12. An isolated nucleic acid molecule encoding the fusion polypeptide of claim 1 .

13. An isolated host cell or a non-human organism transformed or transfected with the nucleic acid molecule of claim 12 .

Priority Claims (1)
EP 08013112 · Jul 21, 2008 · regional
Continuity (5)
Continuation 15172393 · Jun 3, 2016
Continuation 14320261 · Jun 30, 2014
Continuation 13902328 · May 24, 2013
Continuation 13055109
Related Publication 20170313752A1 · Nov 2, 2017