IP Library › Granted Patent US 12,679,887
Granted Patent B2
US 12,679,887 · App. 17/055,252 · Granted Jul 14, 2026

Anti-interleukin-17A antibody, pharmaceutical composition thereof and use thereof

Inventors: Baiyong Li (Zhongshan, CN); Yu Xia (Zhongshan, CN); Zhongmin Maxwell Wang (Zhongshan, CN); Peng Zhang (Zhongshan, CN)
Assignee: Akeso Biopharma, Inc.
C07K16/244A61K47/6801A61P17/06G01N33/577
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Quick Facts
Patent No.
US 12,679,887
App. No.
17/055,252
Filed
Nov 13, 2020
Granted
Jul 14, 2026
Kind
B2
Art Unit
1643
USPC
424/133.1
Abstract

The present invention relates to the fields of treating autoimmune diseases and molecular immunology, and specifically, to an anti-IL-17A antibody, a pharmaceutical composition thereof, and use thereof. The present invention relates to a monoclonal antibody or an antigen binding fragment thereof, wherein a heavy chain variable region of the monoclonal antibody comprises: HCDR1-HCDR3 with amino acid sequences set forth in SEQ ID NOs: 31-33 respectively, or HCDR1-HCDR3 with amino acid sequences set forth in SEQ ID NOs: 37-39 respectively, and a light chain variable region of the monoclonal antibody comprises: LCDR1-LCDR3 with amino acid sequences set forth in SEQ ID NOs: 34-36 respectively, or LCDR1-LCDR3 with amino acid sequences set forth in SEQ ID NOs: 40-42 respectively. Monoclonal antibodies of the present invention can specifically antagonize the binding of IL-17A to a ligand and inhibit activation of fibroblasts by IL-17A.

Claims (26)

1 . An anti-interleukin-17A (anti-IL-17A) monoclonal antibody or an antigen-binding fragment thereof comprising:

a) a heavy chain variable region (VH) comprising three complementarity determining regions (HCDRs):

HCDR1 having the amino acid sequence set forth in SEQ ID NO: 31,

HCDR2 having the amino acid sequence set forth in SEQ ID NO: 32, and

HCDR3 having the amino acid sequence set forth in SEQ ID NO: 33; and

b) a light chain variable region (VL) comprising three CDRs (LCDRs):

LCDR1 having the amino acid sequence set forth in SEQ ID NO: 34,

LCDR2 having the amino acid sequence set forth in SEQ ID NO: 35, and

LCDR3 having the amino acid sequence set forth in SEQ ID NO: 36.

2 . The anti-IL-17A monoclonal antibody or antigen-binding fragment thereof of claim 1 , wherein

the VH comprises the amino acid sequence set forth in SEQ ID NO: 2, and

the VL comprises the amino acid sequence set forth in SEQ ID NO: 4.

3 . The monoclonal antibody or antigen-binding fragment thereof of claim 1 , wherein

the VH comprises the amino acid sequence set forth in SEQ ID NO: 6, and

the VL comprises the amino acid sequence set forth in SEQ ID NO: 8.

4 . The monoclonal antibody or antigen-binding fragment thereof of claim 1 , wherein

the VH comprises the amino acid sequence set forth in SEQ ID NO: 10, and

the VL comprises the amino acid sequence set forth in SEQ ID NO: 12.

5 . The monoclonal antibody or antigen-binding fragment thereof of claim 1 , wherein

the VH comprises the amino acid sequence set forth in SEQ ID NO: 14, and

the VL comprises the amino acid sequence set forth in SEQ ID NO: 12.

6 . The anti-IL-17A monoclonal antibody or antigen-binding fragment thereof of claim 1 , wherein the anti-IL-17A monoclonal antibody or antigen-binding fragment thereof is selected from an Fab, an Fab′, an F(ab′)2, an Fv, a single chain antibody, a humanized antibody, a chimeric antibody, and a diabody.

7 . The anti-IL-17A monoclonal antibody or antigen-binding fragment thereof of claim 1 , wherein the anti-IL-17A monoclonal antibody or antigen-binding fragment thereof comprises non-CDR regions derived from a species other than a mouse.

8 . A conjugate comprising the anti-IL-17A monoclonal antibody or antigen-binding fragment thereof of claim 1 and a conjugated portion comprising a detectable label.

9 . A reagent kit comprising the anti-IL-17A monoclonal antibody or antigen-binding fragment thereof of claim 1 .

10 . A pharmaceutical composition comprising the anti-IL-17A monoclonal antibody or antigen-binding fragment thereof of claim 1 and at least one pharmaceutically acceptable carrier.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 21, 2020
From: LI, BAIYONG; WANG, ZHONGMIN; XIA, YU; ZHANG, PENG
To: AKESO BIOPHARMA, INC.
Reel/Frame 054706/0521 →
Priority Claims (1)
CN 201810539405.0 · May 30, 2018 · national
Continuity (1)
Related Publication 20210122815A1 · Apr 29, 2021
References Cited (70)
US 4816567A · Cabilly et al. · 1989 [cited by applicant]
US 10442857B2 · Ulitin et al. · 2019 [cited by applicant]
US 10738112B2 · Zhang et al. · 2020 [cited by applicant]
US 20110293629A1 · Bastid · 2011 [cited by examiner]
US 20170327571A1 · Liu et al. · 2017 [cited by applicant]
CN 105315371A · 2016 [cited by applicant]
CN 106795219A · 2017 [cited by applicant]
CN 107488227A · 2017 [cited by applicant]
WO WO2006013107A1 · 2006 [cited by applicant]
WO WO2007070750A1 · 2007 [cited by applicant]
WO WO2009147362A1 · 2009 [cited by applicant]
WO WO2012059598A2 · 2012 [cited by applicant]
WO WO2014001368A1 · 2014 [cited by applicant]
WO WO2014122613A1 · 2014 [cited by applicant]
WO WO2014161570A1 · 2014 [cited by applicant]
WO WO2016082193A1 · 2016 [cited by applicant]
WO WO2016113555A1 · 2016 [cited by applicant]
WO WO2017221174A1 · 2017 [cited by applicant]
Paul, Fundamental Immunology, 3rd Edition, 1993, pp. 292-295 (Year: 1993). [cited by examiner]
Bendig M. M. (Methods: A Companion to Methods in Enzymology, 1995; 8:83-93) (Year: 1995). [cited by examiner]
Rudikoff et al. (Proceedings of the National Academy of Sciences USA, vol. 79, p. 1979-1983, 1982) (Year: 1982). [cited by examiner]
Dubel (Handbook of Therapeutic Antibodies, 2007, p. 100-101) (Year: 2007). [cited by examiner]
Johnson and Wu (Methods in Molecular Biology, Antibody Engineering: Methods and Protocols, vol. 248, p. 11-25, 2004) (Year: 2004). [cited by examiner]
Rothstein et al., “Secukinumab for treating plaque psoriasis,” Expert Opinion on Biology Therapy 16(1):119-128 (2015). [cited by applicant]
Strober et al, “Secukinumab improves patient-reported psoriasis symptoms of itching, pain, and scaling: results of two phase 3, randomized, placebo-controlled clinical trials,” International Journal of Dermatology, Wile… [cited by applicant]
Alfthan et al., “Properties of a single-chain antibody containing different linker peptides,” Protein Eng. 8(7):725-731 (1995). [cited by applicant]
Baeten et al., “Secukinumab, an Interleukin-17A Inhibitor, in Ankylosing Spondylitis,” N Engl J Med, 373:253425-48 (2015). [cited by applicant]
Bird et al., “Single-chain antigen-binding proteins,” Science 242:423 426 (1988). [cited by applicant]
Chao et al., “Anti-IL-17A therapy protects against bone erosion in experimental models of rheumatoid arthritis,” Autoimmunity. 44(3):243-52 (2011). [cited by applicant]
Chen et al., Plasma IL-17A is increased in new-onset SLE patients and associated with disease activity. J Clin Immunol, 30:221-225 (2010). [cited by applicant]
Choi et al. “Recombinant chimeric OKT3 scFv IgM antibodies mediate immune suppression while reducing T cell activation in vitro,” Eur. J. Immunol. 31: 94-106 (2001). [cited by applicant]
Clark, “Antibody humanization: a case of the Emperor's new clothes?” Immunol. Today 21:397-402 (2000). [cited by applicant]
Dong et al., “IL-17 induces autoantibody overproduction and peripheral blood mononuclear cell overexpression of IL-6 in lupus nephritis patients,” Chin Med J (Engl), 116(4):543-548 (2003). [cited by applicant]
Dubin et al., “Interleukin-17A and interleukin-17F: a tale of two cytokines,” Immunity 30(1): 9-11 (2009). [cited by applicant]
Ely et al., Structural basis of receptor sharing by interleukin 17 cytokines, Nat Immunol 10(12): 1245-1251 (2009). [cited by applicant]
Gaffen, “The role of interleukin-17 in the pathogenesis of rheumatoid arthritis,” Curr Rheumatol Rep 11:365-370 (2009). [cited by applicant]
Gaffen et al., “Structure and signalling in the IL-17 receptor superfamily,” Nat Rev Immunol 9:556-567 (2009). [cited by applicant]
Genbank Accession No. p01834, dated Apr. 7, 2021, 6 pages. [cited by applicant]
Genbank Accession No. P01857, dated Apr. 7, 2021, 9 pages. [cited by applicant]
GenBank ID: Q16552, dated Apr. 7, 2021, 9 pages. [cited by applicant]
Genbank No. NP_055154.3, dated May 6, 2021, 4 pages. [cited by applicant]
Gottlieb et al., “Secukinumab Improves Physical Function in Subjects With Plaque Psoriasis and Psoriatic Arthritis: Results from Two Randomized, Phase 3 Trials,” J Drugs Dermatol, 14821-14833 (2015). [cited by applicant]
Gracey et al., “Sexual Dimorphism in the Th17 Signature of Ankylosing Spondylitis,” Arthritis R.heumatoL 68(3): 679-689. (2016). [cited by applicant]
Holliger et al., “‘Diabodie’: small bivalent and bispecific antibody fragments,” Proc. Natl. Acad. Sci. USA 90(14): 6444-6448 (1993). [cited by applicant]
Hu et al., “Minibody: A novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts,” Cancer Res. 56:3055-3061 (1996). [cited by applicant]
Huston et al., “Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in [cited by applicant]
Hymowitz et al., “IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding,” EMBO J. 20(19):5332-5341 (2001). [cited by applicant]
Johansen et al., “Characterization of the interleukin-17 isoforms and receptors in lesional psoriatic skin,” Brit J Dermatol, 160(2):319-324 (2009). [cited by applicant]
Jones et al., “Replacing the complementarity-determining regions in a human antibody with those from a mouse,” Nature, 321:522-525 (1986). [cited by applicant]
Kipriyanov et al., “Bispecific tandem diabody for tumor therapy with improved antigen binding and pharmacokinetics,” J. Mol. Biol. 293(1):41-56 (1999). [cited by applicant]
Kitami et al., “IL-17A suppresses the expression of bone resorption-related proteinases and osteoclast differentiation via IL-17RA or IL-17RC receptors in RAW264.7 cells,” Biochimie. 92(4): 398-404 (2010). [cited by applicant]
Kohler et al., Continuous cultures of fused cells secreting antibody of predefined specificity Nature, 256(5517):495-497(1975). [cited by applicant]
Langley et al., “Secukinumab in plaque psoriasis—results of two phase 3 trials,Lowes et al., Psoriasis vulgaris lesions contain discrete populations of Th1 and Th 17 T cells,” N Engl J Med, 371:326-338 (2014). [cited by applicant]
Lowes et al., “Psoriasis vulgaris lesions contain discrete populations of Th1 and Th 17 T cells,” J Invest Dermatol 128(5):1207-1211 (2008). [cited by applicant]
Lubberts et al., “Overexpression of IL-17 in the knee joint of collagen type II immunized mice promotes collagen arthritis and aggravates joint destruction,” Inflamm Res 51. 102-104 (2002). [cited by applicant]
Nakae et al., “Suppression of immune induction of collagen-induced arthritis in IL-17-deficient mice,” J Immunol, 171(11): 6173-6177 (2003). [cited by applicant]
Nestle et al., “Psoriasis,” N Engl J Med, 361. 496-509 (2009). [cited by applicant]
Ogura et al., “Interleukin-17 Promotes Autoimmunity by Triggering a Positive-Feedback Loop via Interleukin-6 Induction,” Immunity 29: 628-636 (2008). [cited by applicant]
Onishi et al., “nterleukin-17 and its target genes: mechanisms of interleukin-17 function in disease,” Immunology 129(3): 311-321 (2010). [cited by applicant]
Poljak RJ et al., “Production and structure of diabodies,” Structure 2:1121 1123 (1994). [cited by applicant]
Presta, “Antibody engineering,” Current Opinion in Structural Biology 2(4):593-596 (1992). [cited by applicant]
Reichmann et al., “Reshaping human antibodies for therapy,” Nature, 332(6162):323-329 (1988). [cited by applicant]
Roovers, et al., “In vitro characterisation of a monovalent and bivalent form of a fully human anti Ep-CAM phage antibody,” Cancer Immunol Immunotherapy 50(1):51-59 (2001). [cited by applicant]
Sarkar et al., “Interleukin (IL)-17A, F and AF in inflammation: a study in collagen-induced arthritis and rheumatoid arthritis,” Clin Exp Immunol. 177(3): 652-661 (2014). [cited by applicant]
Shi et aL, IL-17 Signaling and Function, Chinese Journal of Cell Biology 33(4):345-357 (2011). [cited by applicant]
Toy et al., “Cutting edge: interleukin 17 signals through a heteromeric receptor complex,” J Immunol 177: 36-39 (2006). [cited by applicant]
Ward et al., “Binding activities of a repertoire of single immunoglobulin variable domains secreted from [cited by applicant]
Wright et al, “The human IL-17F/IL-17A heterodimeric cytokine signals through the IL-17RA/IL-17RC receptor complex,” J Immunol 181: 2799-2805 (2008). [cited by applicant]
Mirsky, A, et al., “Antibody-Specific Model of Amino Acid Substitution for Immunological Inferences from Alignments of Antibody Sequences” Mol. Biol. Evol. 32(3): 806-819 Mar. 2015. [cited by applicant]
IN Application No. 202017056968, Office Action mailed Mar. 24, 2026; Applicant AKESO Biopharma, INC., 9 total pages including English translation. [cited by applicant]