IP Library Granted Patent US 12685759
Granted Patent B2
US 12685759 · App. 18/157,385 · Granted Jul 21, 2026

Interleukin-18 variants and methods of use

Inventors: Aaron Ring (New Haven, CT); Ting Zhou (New Haven, CT); Suzanne Fischer (New Haven, CT)
A61K38/20C07K14/54A61K35/17A61K35/768A61K38/1774A61K47/642A61K2300/00A61P35/00C07K14/70596C07K2319/02C07K2319/21C07K2319/35C07K2319/50C12N15/85
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Quick Facts
Patent No.
US 12685759
App. No.
18/157,385
Granted
Jul 21, 2026
Kind
B2
Abstract

The present invention provides compositions and methods comprising an activator of interleukin-18 (IL-18) activity for use in therapeutic and non-therapeutic applications. The activator provides IL-18 signaling activity even in the presence of an inhibitory molecule 5 such as IL-18 binding protein (IL-18BP).

Claims (28)

1 . A method comprising administering to a subject a composition comprising a modified interleukin 18 (IL-18) polypeptide conjugated, with or without a linker, to an anti-PD-1 antibody, wherein the modified IL-18 polypeptide comprises an amino acid sequence having 93% or more sequence identity with the wild-type (WT) IL-18 sequence as set forth in SEQ ID NO: 30 and at least three mutations, relative to WT human IL-18 as set forth in SEQ ID NO:30, that reduce binding to IL-18 binding protein (IL-18BP) as compared to WT IL-18 as set forth in SEQ ID NO: 30, wherein the at least three mutations comprise at least one substitution at a position selected from: Methionine-51, Lysine-53, Serine-55, Glutamine-56, Proline-57, Glycine-59, and Methionine-60.

2 . The method of claim 1 , wherein the at least three mutations comprise a substitution at Tyrosine-1 and the at least one substitution at a position selected from: Methionine-51, Lysine-53, Serine-55, Glutamine-56, Proline-57, Glycine-59, and Methionine-60.

3 . The method of claim 1 , wherein the at least three mutations comprise at least two substitutions at positions selected from: Methionine-51, Lysine-53, Serine-55, Glutamine-56, Proline-57, Glycine-59, and Methionine-60.

4 . The method of claim 1 , wherein the modified IL-18 polypeptide further comprises a substitution at Glutamic acid-6.

5 . The method of claim 1 , wherein the at least three mutations comprise the at least one substitution at a position selected from: Methionie-51, Lysine-53, Serine-55, Glutamine-56, Proline-57, Glycine-59, and Methionin-60, and at least one substitution at a position selected from: Glutamine-103, Serine-105, Aspartic acid-110, Asparagine-111, and Methionine-113.

6 . The method of claim 1 , wherein the subject has cancer.

7 . The method of claim 6 , wherein the subject has leukemia.

8 . The method of claim 6 , wherein the subject has multiple myeloma.

9 . The method of claim 1 , wherein the modified IL-18 polypeptide has an EC 50 for IL-18BP that is at least 10-fold higher than the EC 50 of WT IL-18 for IL-18BP.

10 . The method of claim 1 , wherein the modified IL-18 polypeptide has an IL-18 BP to IL-18 Receptor (IL-18R) dissociation constant ratio that is at least 2-fold higher than the IL-18 to IL-18R dissociation constant ratio of WT IL-18.

11 . The method of claim 10 , wherein the modified IL-18 polypeptide has an IL-18 BP to IL-18R dissociation constant ratio that is at least 20-fold higher than the IL-18 to IL-18R dissociation constant ratio of WT IL-18.

12 . The method of claim 1 , wherein the modified IL-18 polypeptide comprises at least four mutations, relative to WT IL-18 as set forth in SEQ ID NO: 30, that reduce binding to IL-18BP as compared to WT IL-18 as set forth in SEQ ID NO: 30.

13 . The method of claim 1 , wherein the modified IL-18 polypeptide comprises at least five mutations, relative to WT IL-18 as set forth in SEQ ID NO: 30, that reduce binding to IL-18BP as compared to WT IL-18 as set forth in SEQ ID NO: 30.

14 . The method of claim 6 , wherein the subject has an MHC class I deficient cancer.

15 . The method of claim 6 , wherein the subject has a solid tumor.

16 . The method of claim 1 , wherein the modified IL-18 polypeptide has a K D for IL-18BP of 10 nM or greater.

17 . The method of claim 16 , wherein the modified IL-18 variant polypeptide binds human IL-18Ra with an affinity that is at least comparable to WT human IL-18.

18 . A method comprising administering to a subject a composition comprising a nucleic acid encoding a modified interleukin 18 (IL-18) polypeptide fused, with or without a linker, to an anti-PD-1 antibody, wherein the modified IL-18 polypeptide comprises an amino acid sequence having 93% or more sequence identity with the wild-type (WT) IL-18 sequence as set forth in SEQ ID NO: 30 and at least three mutations, relative to WT human IL-18 as set forth in SEQ ID NO:30, that reduce binding to IL-18 binding protein (IL-18BP) as compared to WT IL-18 as set forth in SEQ ID NO: 30, wherein the at least three mutations comprise at least one substitution at a position selected from: Methionine-51, Lysine-53, Serine-55, Glutamine-56, Proline-57, Glycine-59, and Methionine-60.

19 . The method of claim 18 , wherein the at least three mutations comprise a substitution at Tyrosine-1 and the at least one substitution at a position selected from: Methionine-51, Lysine-53, Serine-55, Glutamine-56, Proline-57, Glycine-59, and Methionine-60.

20 . The method of claim 18 , wherein the at least three mutations comprise at least two substitutions at positions selected from: Methionine-51, Lysine-53, Serine-55, Glutamine-56, Proline-57, Glycine-59, and Methionine-60.

21 . The method of claim 18 , wherein the modified IL-18 polypeptide further comprises a substitution at Glutamic acid-6.

22 . The method of claim 18 , wherein the at least three mutations comprise the at least one substitution at a position selected from: Methionine-51, Lysine-53, Serine-55, Glutamine-56, Proline-57, Glycine-59, and Methionine-60, and at least one substitution at Glutamine-103, Serine-105, Aspartic acid-110, Asparagine-111, or Methionine-113.

23 . The method of claim 18 , wherein the modified IL-18 polypeptide has an EC 50 for IL-18BP that is at least 10-fold higher than the EC 50 of WT IL-18 for IL-18BP.

24 . The method of claim 18 , wherein the modified IL-18 polypeptide has an IL-18 BP to IL-18 Receptor (IL-18R) dissociation constant ratio that is at least 2-fold higher than the IL-18 to IL-18R dissociation constant ratio of WT IL-18.

25 . The method of claim 24 , wherein the modified IL-18 polypeptide has an IL-18 BP to IL-18R dissociation constant ratio that is at least 20-fold higher than the IL-18 to IL-18R dissociation constant ratio of WT IL-18.

26 . The method of claim 18 , wherein the modified IL-18 polypeptide comprises at least four mutations, relative to WT IL-18 as set forth in SEQ ID NO: 30, that reduce binding to IL-18BP as compared to WT IL-18 as set forth in SEQ ID NO: 30.

27 . The method of claim 18 , wherein the modified IL-18 polypeptide comprises at least five mutations, relative to WT IL-18 as set forth in SEQ ID NO: 30, that reduce binding to IL-18BP as compared to WT IL-18 as set forth in SEQ ID NO: 30.

28 . The method of claim 18 , wherein the subject has cancer.