IP Library › Granted Patent US 12,202,909
Granted Patent B2
US 12,202,909 · App. 17/836,862 · Granted Jan 21, 2025

Antigen binding molecules specific for an anti-CD19 scFV

Inventors: Stuart Sievers (Van Nuys, CA); Jed Wiltzius (Winchester, MA)
Assignee: Kite Pharma, Inc.
C07K16/4258A61K35/17A61K39/0011A61K39/3955C07K16/2803C07K16/4208G01N33/56972G01N33/686A61K2039/5156A61K2039/5158C07K2317/20C07K2317/24C07K2317/51C07K2317/515C07K2317/565C07K2317/622C07K2319/03C07K2319/33C07K2319/74
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 12,202,909
App. No.
17/836,862
Granted
Jan 21, 2025
Kind
B2
Abstract

Isolated antigen binding molecules that specifically bind to an anti-CD19 scFv comprising SEQ ID NO: 1 are provided. The antigen binding molecules can be used in the methods provided herein.

Claims (15)

1. An isolated antigen binding molecule that specifically binds a molecule comprising SEQ ID NO: 1, wherein the antigen binding molecule comprises:

(a) a heavy chain variable region (VH) complementary determining region (CDR) 1 comprising the amino acid sequence of SEQ ID NO: 41;

(b) a VH CDR2 comprising the amino acid sequence of SEQ ID NO: 42;

(c) a VH CDR3 comprising the amino acid sequence of SEQ ID NO: 43;

(d) a light chain variable region (VL) CDR1 comprising the amino acid sequence of SEQ ID NO: 47;

(e) a VL CDR2 comprising the amino acid sequence of SEQ ID NO: 48; and

(f) a VL CDR3 comprising the amino acid sequence of SEQ ID NO: 49.

2. The antigen binding molecule of claim 1 , wherein the antigen binding molecule is selected from the group consisting of an antibody, an scFv, a Fab, a Fab′, a Fv, a F(ab′) 2, a rabbit antibody, a mouse antibody, a rat antibody, a non-human primate antibody, a humanized antibody, a chimeric antibody, a monoclonal antibody, a polyclonal antibody, a recombinant antibody, an IgE antibody, an IgD antibody, an IgM antibody, an IgG1 antibody, an IgG1 antibody having at least one mutation in the hinge region, an IgG2 antibody, an IgG2 antibody having at least one mutation in the hinge region, an IgG3 antibody, an IgG3 antibody having at least one mutation in the hinge region, an IgG4 antibody, an IgG4 antibody having at least one mutation in the hinge region, an antibody comprising at least one non-naturally occurring amino acid, and any combination thereof.

3. The antigen binding molecule of claim 1 , wherein the antigen binding molecule comprises a VH comprising the amino acid sequence of SEQ ID NO: 40.

4. The antigen binding molecule of claim 1 , wherein the antigen binding molecule comprises a VL comprising the amino acid sequence of SEQ ID NO: 46.

5. The antigen binding molecule of claim 1 , wherein the antigen binding molecule comprises a VH comprising the amino acid sequence of SEQ ID NO: 40 and a VL comprising the amino acid sequence of SEQ ID NO: 46.

6. The antigen binding molecule of claim 1 , wherein the antigen binding molecule further comprises a detectable label.

7. The antigen binding molecule of claim 6 , wherein the detectable label is selected from the group consisting of a fluorescent label, a photochromic compound, a proteinaceous fluorescent label, a magnetic label, a radiolabel, and a hapten.

8. The antigen binding molecule of claim 7 , wherein the fluorescent label is selected from the group consisting of an Atto dye, an Alexafluor dye, quantum dots, Hydroxycoumarin, Aminocouramin, Methoxycourmarin, Cascade Blue, Pacific Blue, Pacific Orange, Lucifer Yellow, NBD, R-Phycoerythrin (PE), PE-Cy5 conjugates, PE-Cy7 conjugates, Red 613, PerCP, TruRed, FluorX, Fluorescein, BODIPY-FL, Cy2, Cy3, Cy3B, Cy3.5, Cy5, Cy5.5, Cy7, TRITC, X-Rhodamine, Lissamine Rhocamine B, Texas Red, APC-Cy7 conjugates, Indo-1, Fluo-3, Fluo-4, DCFH, DHR, SNARF, GFP (Y66H mutation), GFP (Y66F mutation), EBFP, EBFP2, Azurite, GFPuv, T-Sapphire, Cerulean, mCFP, mTurquoise2, ECFP, CyPet, GFP (Y66W mutation), mKeima-Red, TagCFP, AmCyan1, mTFP1, GFP (S65A mutation), Midorishi Cyan, Wild Type GFP, GFP (S65C mutation), TurboGFP, TagGFP, GFP (S65L mutation), Emerald, GFP (S65T mutation), EGFP, Azami Green, ZsGreen1, TagYFP, EYFP, Topaz, Venus, mCitrine, YPet, Turbo YFP, ZsYellow1, Kusabira Orange, mOrange, mKO, TurboRFP, tdTomato, TagRFP, DsRed monomer, DsRed2 (“RFP”), mStrawberry, TurboFP602, AsRed2, mRFP1, J-Red, B-phycoeryhring (BPE), mCherry, HcRed1, Katusha, P3, Peridinin Chlorophyll (PerCP), mKate (TagFP635), TurboFP635, mPlum, and mRaspberry.

9. A composition comprising the antigen binding molecule of claim 1 .

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Aug 8, 2024
From: WILTZIUS, JED; SIEVERS, STUART
To: KITE PHARMA, INC.
Reel/Frame 068520/0611 →
Continuity (4)
Division 16814661 · Mar 10, 2020
Division 15717691 · Sep 27, 2017
Provisional Application 62401007 · Sep 28, 2016
Related Publication 20220403050A1 · Dec 22, 2022
References Cited (86)
US 5223409A · Ladner · 1993 [cited by applicant]
US 7709226B2 · Foote · 2010 [cited by applicant]
US 10501775B2 · Wiltzius et al. · 2019 [cited by applicant]
US 10626187B2 · Wiltzius et al. · 2020 [cited by applicant]
US 11384155B2 · Wiltzius et al. · 2022 [cited by applicant]
US 20160096902A1 · Cooper et al. · 2016 [cited by applicant]
TW 201811828A · 2018 [cited by applicant]
WO WO2008133722A2 · 2008 [cited by applicant]
WO WO2012149356A2 · 2012 [cited by applicant]
WO WO2014190273A1 · 2014 [cited by applicant]
WO WO2016019300A1 · 2016 [cited by applicant]
WO WO2018023100A2 · 2018 [cited by applicant]
Al-Lazikani et al., “Standard conformations for the canonical structures of immunoglobulins” J Mol Biol, 1997, 273: 927-948. [cited by applicant]
Alting-Mees et al., “Monoclonal Antibody Expression Libraries: A Rapid Alternative To Hybridomas”, (1990) Strategies in Molecular Biology 3:1-9. [cited by applicant]
Baines, et al., “Purification of Immunoglobulin G (IgG)”, Methods in Molecular Biology, 1992, vol. 10: Immunochemical Protocols, 10:79-104 (The Humana Press). [cited by applicant]
Berzofsky, et al. “Antigen-Antibody interaction and Monoclonal Antibodies”, Fundamental immunology, editor, William E. Paul.—7th ed., (2013), Ch 7, Lippincott Williams & Wilkins. [cited by applicant]
Bird et al., “Single-chain antigen-binding proteins”, 1988, Science 242:423-26. [cited by applicant]
Bricogne, “[23] Bayesian statistical viewpoint on structure determination: Basic concepts and examples”, Meth Enzymol, 1997, 276A: 361-423. [cited by applicant]
Bricogne, “Direct phase determination by entropy maximization and likelihood ranking: status report and perspectives”, Acta Crystallogr D Biol Crystallogr, 1993, 49(Pt 1): 37-60. [cited by applicant]
Bruggenmann et al. “Production of human antibody repertoires in transgenic mice”, 1Curr. Opin. Biotechnol. 1997, 8:455-58. [cited by applicant]
Burton et al., “Human Antibodies from Combinatorial libraries”, Advances in immunology, 1994, vol. 57, 191-280. [cited by applicant]
Champe et al., “Monoclonal Antibodies That Block the Activity of Leukocyte Function-associated Antigen 1 Recognize Three Discrete Epitopes in the Inserted Domain of CD11a”, J Biol Chem, 1995, 270(3): 1388-94. [cited by applicant]
Chayen, “The role of oil in macromolecular crystallization”, Structure, 1997, 5(10): 1269-1274. [cited by applicant]
Chothia et al., “Canonical structures for the hypervariable regions of immunoglobulins”, J Mol Biol, 1987, 196: 901-917. [cited by applicant]
Chothia et al., “Conformations of immunoglobulin hypervariable regions”, Nature, , 1989, 342(6252):877-883. [cited by applicant]
Chothia et al., “Structural repertoire of the human VH segments” J Mol Biol, 1992, 227: 799-817. [cited by applicant]
Cunningham et al., “High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis”, Science 244(4908): 1081-85 (1989). [cited by applicant]
Dayhoff et al. A model of evolutionary change in proteins, in Dayhoff, M.O. Edition, Atlas of Protein Sequence and Structure, 1978, Natl. Biomed. Res. Found., Washington DC, 5(3), 345-352. [cited by applicant]
De Oliveira et al., “A CD19/Fc fusion protein for detection of anti-CD19 chimeric antigen receptors,” Journal of Translational Medicine, Jan. 29, 2013 (Jan. 29, 2013), vol. 11, pp. 1-9. [cited by applicant]
Evans et al. “Design of nonpeptidal ligands for a peptide receptor: cholecystokinin antagonists” J. Med. Chem, 1987 30:1229-39. [cited by applicant]
Fauchere, “Elements for the Rational Design of Peptide Drugs”, Advances in Drug Research, vol. 15, 1986, 41 pages. [cited by applicant]
Gautier et al. “Site-Specific Protein Labeling, Methods and Protocols”, Springer 2015, pp. 1-267. [cited by applicant]
Giege et al., “Crystallogenesis of biological macromolecules: facts and perspectives”, Acta Crystallogr D Biol Crystallogr, 1994, 50(Pt 4): 339-350. [cited by applicant]
Golub, et al., “Immunology—A Synthesis (2nd Edition)”, Sinauer Assoc., Sunderland, Mass. (1991), table of contents only, 13 pages. [cited by applicant]
Hartl et al., “Genetics: Principles and Analysis”, 1997, Jones and Bartlett Publishers. [cited by applicant]
Heim et al. “Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer”, 1996, Current Biology vol. 6, No. 2:178-182. [cited by applicant]
Henilkoff et al. “Amino acid substitution matrices from protein blocks”, Proc Natl Acad Sci US A., 89(22): 10915-10919, Nov. 15, 1992. [cited by applicant]
Holliger et al., “Diabodies: Small Bivalen and Bispecific Antibody Fagments” Proc Natl Acad Sci U.S.A., 1993, 90:6444-48 Biophysics. [cited by applicant]
Honegger et al. “Yet Another Numbering Scheme for Immunoglobulin Variable Domains: An Automatic Modeling and Analysis Tool” J. Mol. Biol., 2001, 309, 657-670. [cited by applicant]
Hoogenboom et al., “By-passing immunisation”, Journal of Molecular Biology, 1992, 227(2):381-388. [cited by applicant]
Huse, et al., “Generation of a Large Combinatorial Library of the Immunoglobulin Repertoire in Phage Lambda”, Science, 1989, 246(4935):1275-1281. [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]
Intl. Search Report—Written Opinion dated Mar. 5, 2018 for PCT/US2017/053790. [cited by applicant]
Jena, B. et al.; Chimeric Antigen Receptor {CAR)-Specific Monoclonal Antibody to Detect CD19-Specific T Cells in Clinical Trials; (2013) PLoS One 8(3): e57838. doi:10.1371/journal.pone.0057838. [cited by applicant]
Johnson et al. “Molecular Probe Handbook A Guide to Fluorescent Probes and Labeling Technologies” 11th Edition, Life Technologies (2010). [cited by applicant]
Kabat et al. “Sequences of Proteins of Immunological Interest”, 1991, 5th Ed., NIH Publication 91-3242, Bethesda MD title page, publication page, and table of contents only, 10 pages. [cited by applicant]
Kang et al., “Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces”, Proc Natl Acad Sci US A., May 15, 1991, 88(10):4363-6. [cited by applicant]
Kawalekar, et al. “Distinct Signaling of Coreceptors Regulates Specific Metabolism Pathways and Impacts Memory Development in CART Cells,” Immunity, Feb. 16, 2016 (Feb. 16, 2016), vol. 44, pp. 380-390. [cited by applicant]
Kiebak, et el. “A safeguard eliminates T cell receptor gene-modified autoreactive T cells after adoptive transfer,” Proceedings of the National Academy of Sciences, Jan. 15, 2008 (Jan. 15, 2008), vol. 105, No. 2, pp. 62… [cited by applicant]
Kochenderfer, J.N., et al.; Construction and Pre-clinical Evaluation of an Anti-CD19 Chimeric Antigen Receptor; J Immunolher. Sep. 2009; pp. 689-702.; 32(7): doi:10.1097/CJI.0b013e3181ac6138. [cited by applicant]
Korndorfer et al., “Crystallographic Analysis of an “Anticalin” With Tailored Specificity for Fluorescein Reveals High Structural Plasticity of the Lipocalin Loop Region” Proteins: Structure, Function, and Bioinformatic… [cited by applicant]
Ichiki et al., “Regulation of the expression of human C epsilon germline transcript. Identification of a novel IL-4 responsive element”, http://www.jimmunol.org/content/150/12/5408 J Immunol 1993; 150:5408-5417. [cited by applicant]
McPherson, “Crystallization of Proteins from Polyethylene Glycol”, J Biol Chem, 1976, 251(20): 6300-6303. [cited by applicant]
McPherson, “Current approaches to macromolecular crystallization”, Eur J Biochem, 1990, 189: 1-23. [cited by applicant]
Nicholson et al., Construction and Characterisation of A Functional CD19 Specific Single Chain Fv Fragment for Immunotherapy of B Lineage Leukaemia and Lymphoma Mol Immunol, 1997, vol. 34, No. 16-17:1157-65, Elsavier. [cited by applicant]
Obermaier et al. “Principles of Protein Labeling Techniques. In: Posch A. (eds) Proteomic Profiling. Methods in Molecular Biology”, 2015, vol. 1295. , Humana Press, New York, NY. [cited by applicant]
Pan, Y. et al.; Anti-idiotypic Antibodies: Biological Function and Structural Studies; The FASEB Journal, Jan. 1995 p. 43-49; vol. 9, No. 1. [cited by applicant]
Perisic et al., “Crystal structure of a diabody, a bivalent antibody fragment” Structure, 1994, 2(12): 1217-26. [cited by applicant]
Poljak et al., “Production and structure of diabodies” Structure, 1994, vol. 2, No. 12: 1121-23. [cited by applicant]
Roque et al., “Antibodies and Genetically Engineered Related Molecules: Production and Purification”, Biotechnol. Prog. 20:639-654 (2004). [cited by applicant]
Roversi et al., “Modeling prior distributions of atoms for macromolecular refinement and completion”, Acta Crystallogr D Biol Crystallogr, 2000, 56 (Pt 10): 1316-1323. [cited by applicant]
Sastry et al. “Cloning of the immunological repertoire in [cited by applicant]
Schlebusch et al., “Production of a Single-Chain Fragment of the Murine Anti-Idiotypic Antibody ACA125 as Phage-Displayed and Soluble Antibody by Recombinant Phage Antibody Technique”, 1997, Hybridoma 16:47-52. [cited by applicant]
Stauber et al. “Development and Applications of Enhanced Green Fluorescent Protein Mutants”, BioTechniques, Mar. 1998, vol. 24, No. 3:462-471. [cited by applicant]
Stocks, “Intrabodies: production and promise” Drug Discovery Today, 2004, 9(22):960-66. [cited by applicant]
Strack, “Protein labeling in cells”, Nature Methods, Jan. 2016, vol. 13, No. 1, p. 33. [cited by applicant]
Torikai et al.; “A foundation for universal T-cell based immunotherapy: T cells engineered to express a CD19-specific chimeric-antigen-receptor and eliminate expression of endogenous TCR,” Blood, Jun. 14, 2012 (Jun. 14,… [cited by applicant]
Tramontano et al., “Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins” J Mol Biol, 1990, 215(1): 175-82. [cited by applicant]
Verber, et al., “The design of metabolically-stable peptide analogs,”. Trends in Neurosciences, Sep. 1985, pp. 392-396. [cited by applicant]
Winter, et al., “Making Antibodies by Phage Display Technology”, Annual Review of Immunology, Publication Annual Review of Immunology, 1994, 12(1):433-455. [cited by applicant]
Wyckoff et al., eds., Methods in Enzymology vol. 114—Diffraction Methods for Biological Macromolecules, Academic Press, Orlando, FL; title page, publication page, and table of contents only, 5 pages (1985). [cited by applicant]
Wyckoff et al., eds., Methods in Enzymology vol. 115. Diffraction Methods for Biological Macromolecules, Academic Press, Orlando, FL; title page, publication page, and table of contents only, 4 pages (1985). [cited by applicant]
Zheng, el al., “Protein L: a novel reagent for the detection of Chimeric Antigen Receptor (CAR) expression by flow cytometry,” Journal of Translational Medicine, Feb. 13, 2012(Feb. 13, 2012), vol. 10, pp. 1-6. [cited by applicant]
Zola, Y. et al.; Preparation and Characterization of a Chimeric CD19 Monoclonal Antibody:Immunology and Cell Biology; Dec. 1991; pp. 411-422; 69 { PI 6). [cited by applicant]
Wu et al., “From Therapeutic Antibodies to Chimeric Antigen Receptors (CARs): Making Better CARs Based on Antigen-Binding Domain,” Expert Opinion on Biological Therapy, vol. 16, No. 12, (2016), pp. 1469-1478. [cited by applicant]
Park et al., “CD19-Targeted CAR T-Cell Therapeutics for Hematologic Malignancies: Interpreting Clinical Outcomes to Date,” Blood, vol. 127, No. 26, (2016), pp. 3312-3320. [cited by applicant]
Kochenderfer et al., “B-Cell Depletion and Remissions of Malignancy along with Cytokine-Associated Toxicity in a Clinical Trial of Anti-CD19 Chimeric-Antigen-Receptor-Transduced T Cells,” Bood, vol. 119, No. 12, (2011),… [cited by applicant]
Extended European Search Report, issued in EP Application No. 17857353, dated Jun. 18, 2020. [cited by applicant]
Office Action dated Jul. 27, 2020 in Taiwanese Appl. No. 109114726. [cited by applicant]
Office Action dated Feb. 27, 2019 in Taiwanese Appl. No. 106133121. [cited by applicant]
Non-Final Office Action dated Aug. 7, 2019 in U.S. Appl. No. 15/717,691. [cited by applicant]
Notice of Allowance dated Dec. 11, 2019 in U.S. Appl. No. 15/717,691. [cited by applicant]
Decision of Rejection dated Jul. 17, 2019 in Taiwanese Appl. No. 106133121. [cited by applicant]
Baines, et al., “Purification ofImmunoglobu1in G (IgG)”, Methods in Molecular Biology, 1992, vol. 10: Immunochemical Protocols, 10:79-104 (The Humana Press). [cited by applicant]
Communication pursuant to Article 94(3) EPC dated May 12, 2021 for European Appl. No. 17857353.1. [cited by applicant]
Office Action dated Dec. 12, 2022 for European Appl. No. 17857353.1. [cited by applicant]