IP Library › Granted Patent US 12,551,531
Granted Patent B2
US 12,551,531 · App. 17/059,539 · Granted Feb 17, 2026

Interleukin-2 and use thereof

Inventors: Lishan Kang (Jiangsu, CN); Fenggen Fu (Jiangsu, CN); Shuaixiang Zhou (Jiangsu, CN); Xinzhen Shi (Jiangsu, CN); Junjian Liu (Jiangsu, CN)
Assignee: INNOVENT BIOLOGICS (SUZHOU) CO., LTD.
A61K38/2013A61K47/6851A61K47/6853A61K47/6865C07K14/55C07K16/18C07K16/2803C07K16/3053C07K16/40C12N15/62C07K2317/55C07K2317/622C07K2319/30
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 12,551,531
App. No.
17/059,539
Granted
Feb 17, 2026
Kind
B2
Abstract

The present invention relates to a novel interleukin-2 (IL-2) mutant protein. The present invention further provides a fusion protein and an immunoconjugate comprising the IL-2 mutant protein, a nucleic acid encoding the IL-2 mutant protein, and a vector and a host cell comprising the nucleic acid. The present invention further provides a method for preparing the IL-2 mutant protein, a pharmaceutical composition comprising the IL-2 mutant protein, and therapeutic use of the mutant protein.

Claims (36)

1 . An IL-2 mutant protein, comprising, as compared to a wild-type IL-2,

(i) a shortened B′C′ loop region, or

(ii) a shortened B′C′ loop region and a mutated glycosylation motif,

wherein the shortened B′C′ loop region has the sequence of A(Q/G)S(K/A) N(F/I)H or SGDASIH positioned between amino acid residues aa72 and aa84;

wherein the mutated glycosylation motif is a glycosylation motif N-X-S/T introduced by a mutation at amino acid positions selected from the group consisting of: 38N-39X-40T/S, 41N-42X-43T/S, 43N-44X-45T/S, 45N-46X-47T/S, 62N-63X-64T/S, 68N-69X-70T/S, 72N-73X-74T/S, and 74N-75X-76T/S, wherein X is any amino acid other than proline, or X is an amino acid same as the amino acid at the corresponding position in the wild-type IL-2 or a conservatively substituted residue thereof;

wherein the wild-type IL-2 is a human IL-2 comprising the sequence of SEQ ID NO: 26;

and wherein the amino acid positions are numbered according to SEQ ID NO: 26.

2 . The mutant protein of claim 1 , wherein, compared to the wild-type IL-2, the mutant protein comprises a mutated glycosylation motif, selected from the group consisting of:

(i) R38N-M39-L40S, and

(ii) Q74N-S75-K76T,

wherein, compared to the wild-type IL-2, the mutant protein has improved expression and/or purity, when expressed in the form of an Fc fusion protein in a mammalian cell.

3 . The mutant protein of claim 1 , wherein, compared to the wild-type IL-2, the mutant protein comprises a mutated glycosylation motif, selected from the group consisting of:

(i) T41N-F42-K43S,

(ii) K43N-F44-Y45T,

(iii) Y45N-M46-P47S,

(iv) E68N-V69-L70S, and

(v) L72N-A73-Q74T,

optionally, further comprising:

(i) a mutated glycosylation motif selected from the group consisting of 35N-36X-37T/S, 38N-39X-40T/S, and 74N-75X-76T/S; and/or

(ii) a K35Q mutation,

further optionally wherein, compared to the wild-type IL-2, the mutant protein has reduced or eliminated binding to IL-2Rα, and/or has improved expression and purity when expressed in a mammalian cell in the form of an Fc fusion protein.

4 . The mutant protein of claim 1 , wherein, compared to the wild-type IL-2, the mutant protein comprises:

a loop region having a sequence of A(Q/G)S(K/A) N(F/I)H positioned between amino acid residues aa72 and aa84.

5 . The mutant protein of claim 1 , wherein compared to the wild-type IL-2, the mutant protein comprises:

(i) a B′C′ loop region having the sequence SGDASIH positioned between amino acid residues aa72 and aa84; or

(ii) a B′C′ loop region having the sequence AQSKNFH or AGSKNFH positioned between amino acid residues aa72 and aa84.

6 . The mutant protein of claim 1 , wherein, as compared to the wild-type IL-2, the mutant protein has an enhanced binding to IL-2Rβ, and/or an improved expression yield and/or purity.

7 . The mutant protein of claim 1 , wherein the mutant protein comprises an amino acid sequence selected from the group consisting of SEQ ID NOs: 40-44, or a sequence having at least 90%, 92%, 93%, 94%, 95%, 96%, 97%, or 98% identity thereto.

8 . An IL-2 mutant protein according to claim 1 , comprising, as compared to a wild-type IL-2, a combinatorial mutation of: (i) a mutated glycosylation motif selected from the group consisting of 41N-42X-43T/S, 43N-44X-45T/S, 45N-46X-47T/S, 68N-69X-70T/S, and 72N-73X-74T/S; and (ii) a shortened B′C′ loop region sequence positioned between amino acid positions aa72 and aa84, selected from the group consisting of SGDASIH and A(Q/G)S(K/A)N(F/I)H, wherein the amino acid positions are numbered according to SEQ ID NO:26.

9 . The IL-2 mutant protein of claim 8 , having, as compared to the wild-type IL-2, a reduced preference for preferentially stimulating p-STATA5 signaling in CD25 + T cells and an enhanced ability to stimulate signaling in CD25 − T cells.

10 . The IL-2 mutant protein of claim 8 , wherein the mutant protein comprises combinatorial mutation:

(i) a mutated glycosylation motif of K43N-F44-Y45T and a shortened B′C′ loop region having the sequence SGDASIH between amino acid positions aa72 and aa84; or

(ii) a mutated glycosylation motif K43N-F44-Y45T and a shortened B′C′ loop region having the sequence AQSKNFH between amino acid positions aa72 and aa84.

11 . The mutant protein of claim 10 , wherein the mutant protein comprises an amino acid sequence selected from the group consisting of SEQ ID NOs: 48, 49, and 50 or a sequence having at least 90%, 92%, 93%, 94%, 95%, 96%, 97%, or 98% identity thereto.

12 . The IL-2 mutant protein of claim 1 , wherein the wild-type IL-2 comprises a sequence of SEQ ID NO: 26, and wherein the IL-2 mutant protein has at least 85%, 86%, 87%, 88%, 89%, 90% or 95% identity to the wild-type human IL-2.

13 . A pharmaceutical composition, comprising the IL-2 mutant protein of claim 1 , or a fusion comprising the IL-2 mutant protein fused to an Fc antibody fragment, and a pharmaceutically acceptable carrier.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Nov 30, 2020
From: KANG, LISHAN; FU, FENGGEN; ZHOU, SHUAIXIANG; SHI, XINZHEN; LIU, JUNJIAN
To: INNOVENT BIOLOGICS (SUZHOU) CO., LTD.
Reel/Frame 054486/0774 →
Priority Claims (1)
CN 201811108663.X · Sep 21, 2018 · national
Continuity (1)
Related Publication 20210213102A1 · Jul 15, 2021
References Cited (99)
US 4518584A · Mark et al. · 1985 [cited by applicant]
US 5153310A · Mitchell et al. · 1992 [cited by applicant]
US 6171586B1 · Lam et al. · 2001 [cited by applicant]
US 6207156B1 · Kuchroo et al. · 2001 [cited by applicant]
US 6267958B1 · Andya et al. · 2001 [cited by applicant]
US 9244059B2 · Triebel et al. · 2016 [cited by applicant]
US 20040175357A1 · Shanafelt et al. · 2004 [cited by applicant]
US 20110070238A1 · Triebel et al. · 2011 [cited by applicant]
US 20110150892A1 · Thudium et al. · 2011 [cited by applicant]
US 20120244112A1 · Ast et al. · 2012 [cited by applicant]
US 20180142037A1 · Ast et al. · 2018 [cited by applicant]
US 20210221863A1 · Kang et al. · 2021 [cited by applicant]
US 20230145766A1 · He et al. · 2023 [cited by applicant]
US 20230174604A1 · Fu et al. · 2023 [cited by applicant]
CA 3040313A1 · 2018 [cited by applicant]
CN 1309705A · 2001 [cited by applicant]
CN 102101885A1 · 2011 [cited by applicant]
CN 103492411A · 2014 [cited by applicant]
CN 104231068A · 2014 [cited by applicant]
CN 105980410A · 2016 [cited by applicant]
CN 116370641A · 2023 [cited by applicant]
EP 4273161A1 · 2023 [cited by applicant]
JP H04503604A · 1992 [cited by applicant]
JP 2007527242A · 2007 [cited by applicant]
JP 2007528728A · 2007 [cited by applicant]
JP 2007535919A · 2007 [cited by applicant]
JP 2008509651A · 2008 [cited by applicant]
JP 2014506793A · 2014 [cited by applicant]
JP 2017500040A · 2017 [cited by applicant]
JP 2017518361A · 2017 [cited by applicant]
JP 2020529977A · 2020 [cited by applicant]
JP 2021531013A · 2021 [cited by applicant]
TW 201237165A1 · 2012 [cited by applicant]
TW 201831688A · 2018 [cited by applicant]
TW 202144391A · 2021 [cited by applicant]
WO 1990010070A1 · 1990 [cited by applicant]
WO 9102000A1 · 1991 [cited by applicant]
WO 9842752A1 · 1998 [cited by applicant]
WO 0037504A2 · 2000 [cited by applicant]
WO 0114424A2 · 2001 [cited by applicant]
WO 2005086751A2 · 2005 [cited by applicant]
WO 2005086798A2 · 2005 [cited by applicant]
WO 2005100395A2 · 2005 [cited by applicant]
WO 2006044908A2 · 2006 [cited by applicant]
WO 2010021961A2 · 2010 [cited by applicant]
WO 2010087994A2 · 2010 [cited by applicant]
WO 2012119093A1 · 2012 [cited by applicant]
WO 2014008218A1 · 2014 [cited by applicant]
WO 2014153111A2 · 2014 [cited by applicant]
WO 2017025016A1 · 2017 [cited by applicant]
WO 2018223923A1 · 2018 [cited by applicant]
WO 2019028419A1 · 2019 [cited by applicant]
WO 2019096194A1 · 2019 [cited by applicant]
WO 2019173832A2 · 2019 [cited by applicant]
WO 2019246404A1 · 2019 [cited by applicant]
WO 2020020783A1 · 2020 [cited by applicant]
WO 2020057646A1 · 2020 [cited by applicant]
WO 2021185361A1 · 2021 [cited by applicant]
WO 2023023070A2 · 2023 [cited by applicant]
WO 2023045977A1 · 2023 [cited by applicant]
Lopes et al: “ALKS 4230: a novel engineered IL-2 fusion protein with an improved cellular selectivity profile for cancer immunotherapy”, Journal for Immunotherapy of Cancer, vol. 8, No. 1, 2020:e000673. 13 pages. [cited by applicant]
Wu et al: “IL-2R[alpha]-biased agonist enhances antitumor immunity by invigorating tumor-infiltrating CD25+CD8+ T cells”, Nature Cancer, vol. 4, No. 9, 2023:1309-1325. 35 pages. [cited by applicant]
Zhang et al.: “Comparative analysis of bat genomes provides insight into the evolution of flight and immunity”, Science, 2013, 339(6118): 456-460. 10 pages. [cited by applicant]
Smith, Interleukin-2, Inception, Impact and Implications, Science 240, 1169-76 (1988). [cited by applicant]
Bazan et al., Unraveling the structure of IL-2, Science 257, 410-413 (1992). [cited by applicant]
Krieg et al, Improved IL-2 immunotherapy by selective stimulation of IL-2 receptors on lymphocytes and endothelial cells, Proc Natl Acad Sci 107, 11906-11 (2010). [cited by applicant]
Boyman et al., The role of interleukin-2 during homeostasis and activation of the immune system, J. Nat. Rev. Immunol. 12, 180-190 (2012). [cited by applicant]
Fontenot et al, A function for interleukin 2 in Foxp3-expressing regulatory T cells, Nature Immunol. 6,1142-51 (2005). [cited by applicant]
D'Cruz et al., Development and function of agonist-induced CD25+Foxp3+ regulatory T cells in the absence of interleukin 2 signaling, Nature Immunol. 6,1152-59 (2005). [cited by applicant]
Maloy et al., Fueling regulation: IL-2 keeps CD4+ Treg cells fit, Nature Immunol. 6,1071-72 (2005). [cited by applicant]
Boyman et al., Selective Stimulation of T Cell Subsets with Antibody-Cytokine Immune Complexes, Science 311, 1924-1927 (2006). [cited by applicant]
Levin et al., Exploiting a natural conformational switch to engineer an interleukin-2 ‘superkine’, Nature, vol. 484, p. 529-533, 2012. [cited by applicant]
Vazquez-Lombardi, et al., Potent antitumour activity of interleukin-2-Fc fusion proteins requires Fc-mediated depletion of regulatory T-cells, Nature Communications, 8:15373, 2017. [cited by applicant]
Gerngross, Advances in the production of human therapeutic proteins in yeasts and filamentous fungi, Nat Biotech 22, 1409-1414 (2004). [cited by applicant]
Li et al., Optimization of humanized IgGs in glycoengineered Pichia pastoris, Nat Biotech 24, 210-215 (2006). [cited by applicant]
Graham et al., Characteristics of a human cell line transformed by DNA from human adenovirus type 5, J Gen Virol 36,59-72 (1977). [cited by applicant]
Mather, Establishment and Charaterization of Two Distinct Mouse Testicular Epithelial Cell Lines, Biol Reprod 23, 243-252 (1980). [cited by applicant]
Mather et al., Culture of Testicular Cells in Hormone-supplemented serum-free medium, Annals N. Y. Acad Sci. 383, 44-68 (1982). [cited by applicant]
Urlaub et al., Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity, Proc Natl Acad Sci USA 77, 4216 (1980). [cited by applicant]
Hurwitz et al. (1998) CTLA-4 blockade synergizes with tumor-derived granulocyte-macrophage colony-stimulating factor for treatment of an experimental mammary carcinoma, Proc. Natl. Acad. Sci. USA 95(17):10067-10071. [cited by applicant]
Camacho et al. (2004) Phase 1 clinical trial of anti-CTLA4 human monoclonal antibody CP-675,206 in patients (pts) with advanced solid malignancies, J. Clin. Oncology 22(145): Abstract No. 2505. [cited by applicant]
Mokyr et al. Realization of the Therapeutic Potential of CTLA-4 Blockade in Low-Dose Chemotherapy-treated Tumor-bearing Mice, (1998) Cancer Res. 58:5301-5304. [cited by applicant]
Lenardo et al., Interleukin-2 programs mouse αβ T lymphocytes for apoptosis, Nature 353: 858 (1991). [cited by applicant]
Estep et al., High throughput solution based measurement of antibody-antigen affinity and epitope binning. MAbs, 2013, 5(2): pp. 270-278. [cited by applicant]
Denesyuk et al., Molecular models of two competitive inhibitors, IL-2δ2 and IL-2δ3, generated by alternative splicing of human interleukin-2, Immunology Letters, 60 (1998) 61-66. [cited by applicant]
Xu et al., Structure-Function Studies of the C-terminal α-Helix of Human Iterleukin-2 by site-directed mutagenesis, Chinese Journal of Biotechnology, 9(4):298-302, 1993. [cited by applicant]
International Search Report and Written Opinion of PCT/CN2019/107054, mailed on Dec. 20, 2019. [cited by applicant]
Lorenzo Benatuil et al.: “An improved yeast transformation method for the generation of very large human antibody libraries”, Protein Engineering, Design & Selection, vol. 23 No. 4 pp. 155-159, 2010. [cited by applicant]
International Search Report and Written Opinion of PCT/CN2019/107055, mailed on Dec. 12, 2019. [cited by applicant]
Vidarsson et al., IgG subclasses and allotypes: from structure to effector functions , 2014, vol. 5, Article 520:1-17. [cited by applicant]
Carmenate et al., “Human IL-2 mutein with higher antitumor efficacy than wild type IL-2”. The Journal of Immunology. 2013, 190(12): 6230-6238. [cited by applicant]
Smith et al.: “A novel, native-format bispecific antibody triggering T-cell killing of B-cells is robustly active in mouse tumor models and cynomolgus monkeys”, Scientific Reports, 2015-5:17943—DOI: 10.1038/srep17943. [cited by applicant]
International Search Report and Written Opinion of PCT/CN2021/081840, mailed Jul. 1, 2021. [cited by applicant]
International Search Report and Written Opinion of PCT/CN2021/081841, mailed Jun. 18, 2021. [cited by applicant]
Chen et. al. “A novel human IL 2 mutein with minimal systemic toxicity exerts greater antitumor efficacy than wild-type IL 2”, Cell Death and Disease, 2018, 9:989, pp. 1-12. [cited by applicant]
Hadash-Bengad et al., “Immunotherapy Potentiates the Effect of Chemotherapy in Metastatic Melanonma—A Retrospective Study”, Frontiers in Oncology, 2020, vol. 10, Article 70, 8 pages. [cited by applicant]
International Search Report and Written Opinion of PCT/CN2024/143132, mailed Mar. 25, 2025. 13 pages. [cited by applicant]
U.S. Appl. No. 19/376,374, filed Oct. 31, 2025. [110 pages]. [cited by applicant]
Chirifu et al., “Crystal structure of the IL-15-IL-15Ra complex, a cytokine-receptor unit presented in trans”, Nature Immunology, vol. 8, No. 9, 2007, pp. 1001-1007. [cited by applicant]