WO2020135201A1 - 一种抗体及其用途 - Google Patents

一种抗体及其用途 Download PDF

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Publication number
WO2020135201A1
WO2020135201A1 PCT/CN2019/126495 CN2019126495W WO2020135201A1 WO 2020135201 A1 WO2020135201 A1 WO 2020135201A1 CN 2019126495 W CN2019126495 W CN 2019126495W WO 2020135201 A1 WO2020135201 A1 WO 2020135201A1
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WIPO (PCT)
Prior art keywords
seq
sequence
antibody
cdr
light chain
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/CN2019/126495
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English (en)
French (fr)
Chinese (zh)
Inventor
田海军
邓俗俊
赵春霞
李虹
刘登念
龙虎
王成
肖亮
薛彤彤
王晶翼
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Sichuan Kelun Biotech Biopharmaceutical Co Ltd
Klus Pharma Inc
Original Assignee
Sichuan Kelun Biotech Biopharmaceutical Co Ltd
Klus Pharma Inc
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Sichuan Kelun Biotech Biopharmaceutical Co Ltd, Klus Pharma Inc filed Critical Sichuan Kelun Biotech Biopharmaceutical Co Ltd
Priority to US17/295,603 priority Critical patent/US12297265B2/en
Priority to CN202411323934.9A priority patent/CN119350498A/zh
Priority to EP19903546.0A priority patent/EP3904386A4/en
Priority to KR1020217015188A priority patent/KR20210109520A/ko
Priority to CN201980076474.5A priority patent/CN113166246B/zh
Priority to JP2021528872A priority patent/JP7562528B2/ja
Publication of WO2020135201A1 publication Critical patent/WO2020135201A1/zh
Anticipated expiration legal-status Critical
Priority to US19/097,908 priority patent/US20250340630A1/en
Ceased legal-status Critical Current

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Definitions

  • VL Light chain variable region containing the following 3 CDRs: CDR-L1 with sequence SEQ ID NO: 14, CDR-L2 with sequence SEQ ID NO: 15, CDR-L3 with sequence SEQ ID NO: 16 ;
  • the VH of the antibody or antigen-binding fragment of the invention comprises a heavy chain variable region (VH) framework region (FR) derived from murine immunoglobulin, and/or the antibody or
  • the VL of the antigen-binding fragment contains a light chain variable region (VL) framework region (FR) derived from murine immunoglobulin. Therefore, in certain preferred embodiments, the antibodies or antigen-binding fragments thereof of the invention are of murine origin.
  • the antibody or antigen-binding fragment of the invention has a degree of humanization of at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93 %, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.
  • the anti-CLDN 18.2 antibody molecule has a heavy chain constant region (Fc) selected from heavy chain constant regions of, for example, IgG1, IgG2, IgG3, IgG4, IgM, IgA1, IgA2, IgD, and IgE; in particular It is selected, for example, from the heavy chain constant region of IgG1, IgG2, IgG3, and IgG4, and more particularly from the heavy chain constant region of IgG1 or IgG4 (eg, human IgG1 or IgG4).
  • the anti-CLDN 18.2 antibody molecule has a light chain constant region selected from light chain constant regions such as ⁇ or ⁇ , preferably a ⁇ light chain constant region (eg, human ⁇ light chain).
  • the antibodies of the invention include the VH of the sequence shown in SEQ ID NO: 39 and the heavy chain of the heavy chain constant region (CH) shown in SEQ ID NO: 42, and, including SEQ ID NO : VL of the sequence shown in 41 and the light chain of the light chain constant region (CL) shown in SEQ ID NO: 43.
  • the antibodies of the invention are chimeric antibodies or humanized antibodies.
  • the antibody or antigen-binding fragment of the present invention is selected from ScFv, Fab, Fab', (Fab') 2 , Fv fragment, disulfide-linked Fv (dsFv), diabody ), bispecific antibodies, and multispecific antibodies.
  • the pharmaceutical composition of the invention comprises the vector or host cell of the invention, and a pharmaceutically acceptable carrier and/or excipient.
  • the isolated nucleic acid molecule contained in the vector comprises a nucleotide sequence encoding a chimeric antigen receptor, and the nucleotide sequence encoding the chimeric antigen receptor further comprises an antibody encoding the invention Or the nucleotide sequence of its antigen-binding fragment (eg ScFv); the host cell contains the isolated nucleic acid molecule or vector as described above.
  • the isolated nucleic acid molecule encodes a chimeric antigen receptor comprising an antigen-binding fragment (eg, ScFv) of the antibody of the invention.
  • the host cell is a T cell.
  • the host cell is a chimeric antigen receptor T cell (CAR-T).
  • the present invention provides a method of preventing and/or treating tumors in a subject. In another aspect, the present invention provides a method of delaying tumor progression in a subject. In another aspect, the invention provides a method of reducing or inhibiting tumor recurrence in a subject. The method described above includes administering an effective amount of the antibody or antigen-binding fragment thereof, carrier, host cell, conjugate, chimeric antigen receptor, or multispecific antibody of the present invention to a subject in need thereof, Pharmaceutical composition.
  • the isolated nucleic acid molecule encodes a chimeric antigen receptor comprising an antigen-binding fragment (eg, ScFv) of the antibody of the invention.
  • the host cell is a T cell.
  • the host cell is a chimeric antigen receptor T cell (CAR-T).
  • the tumors involved in the antibodies or antigen-binding fragments thereof of the present invention are HER2 negative.
  • the pharmaceutical composition of the present invention may include a "therapeutically effective amount” or “prophylactically effective amount” of the antibody or antigen-binding fragment thereof of the present invention.
  • “Prophylactically effective amount” refers to an amount sufficient to prevent, prevent, or delay the occurrence of disease.
  • “Therapeutically effective amount” refers to an amount sufficient to cure or at least partially prevent the disease and its complications in patients already suffering from the disease.
  • the therapeutically effective amount of the antibody or antigen-binding fragment thereof of the present invention may vary according to the following factors: the severity of the disease to be treated, the overall state of the patient's own immune system, the general condition of the patient such as age, weight and gender, the drug's Mode of administration, and other treatments administered simultaneously.
  • the “germline antibody gene” is an immunoglobulin sequence encoded by non-lymphocytes, and it has not undergone the maturation process leading to genetic rearrangement and maturation of the expression of specific immunoglobulins.
  • One advantage provided by the various embodiments of the present invention stems from the recognition that germline antibody genes retain more of the important amino acid sequence structures characteristic of individuals of animal species than mature antibody genes. Therefore, when applied therapeutically to this species, it is less recognized as a foreign substance by this species.
  • bispecific antibody refers to a conjugate formed by a first antibody (fragment) and a second antibody (fragment) or antibody analog through a coupling arm, and the manner of coupling includes but It is not limited to chemical reaction, gene fusion, protein fusion, polypeptide fusion and enzymatic.
  • Multispecific antibodies include, for example, trispecific antibodies and tetraspecific antibodies, the former are antibodies with three different antigen binding specificities, and the latter are antibodies with four different antigen binding specificities.
  • the monoclonal antibodies of the present invention can be prepared by a variety of techniques, such as hybridoma technology (see, for example, Kohler et al. Nature, 256:495,1975), recombinant DNA technology (see, for example, US Patent Application 4,816,567), or bacteriophage Antibody library technology (see, for example, Clackson et al. Nature 352:624-628, 1991, or Marks et al. J. Mol. Biol. 222:581-597, 1991).
  • Figure 5B 1E9.2-hz11, IMAB362 antibody ADCC activity detection (KATOIII-Claudin 18.2 cells)
  • V T beginning mean tumor volume at the beginning of treatment in the treatment group

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US12297265B2 (en) 2025-05-13
JP7562528B2 (ja) 2024-10-07
KR20210109520A (ko) 2021-09-06
CN113166246B (zh) 2024-10-18
CN119350498A (zh) 2025-01-24
US20250340630A1 (en) 2025-11-06
CN113166246A (zh) 2021-07-23
JP2022515318A (ja) 2022-02-18

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