WO2009149021A2 - Xbp1, cd138, and cs1 peptides - Google Patents

Xbp1, cd138, and cs1 peptides Download PDF

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Publication number
WO2009149021A2
WO2009149021A2 PCT/US2009/045866 US2009045866W WO2009149021A2 WO 2009149021 A2 WO2009149021 A2 WO 2009149021A2 US 2009045866 W US2009045866 W US 2009045866W WO 2009149021 A2 WO2009149021 A2 WO 2009149021A2
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WO
WIPO (PCT)
Prior art keywords
amino acid
acid sequence
cell
peptide
peptides
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
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PCT/US2009/045866
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English (en)
French (fr)
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WO2009149021A3 (en
Inventor
Nikhil C. Munshi
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Dana Farber Cancer Institute Inc
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Dana Farber Cancer Institute 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
Priority to CN200980130349.4A priority Critical patent/CN102112147B/zh
Priority to EP09759182.0A priority patent/EP2300034B1/en
Priority to US12/995,661 priority patent/US9096681B2/en
Priority to CA2726804A priority patent/CA2726804C/en
Priority to JP2011512566A priority patent/JP2011523560A/ja
Priority to EP18162674.8A priority patent/EP3384919A1/en
Application filed by Dana Farber Cancer Institute Inc filed Critical Dana Farber Cancer Institute Inc
Publication of WO2009149021A2 publication Critical patent/WO2009149021A2/en
Publication of WO2009149021A3 publication Critical patent/WO2009149021A3/en
Anticipated expiration legal-status Critical
Priority to US14/754,456 priority patent/US11083783B2/en
Priority to US17/370,412 priority patent/US20220031821A1/en
Ceased legal-status Critical Current

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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P35/00—Antineoplastic agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K40/00—Cellular immunotherapy
    • A61K40/10—Cellular immunotherapy characterised by the cell type used
    • A61K40/11—T-cells, e.g. tumour infiltrating lymphocytes [TIL] or regulatory T [Treg] cells; Lymphokine-activated killer [LAK] cells
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K40/00—Cellular immunotherapy
    • A61K40/40—Cellular immunotherapy characterised by antigens that are targeted or presented by cells of the immune system
    • A61K40/41—Vertebrate antigens
    • A61K40/42—Cancer antigens
    • A61K40/4261—Proteoglycans, e.g. glypican, brevican or CSPG4
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P35/00—Antineoplastic agents
    • A61P35/02—Antineoplastic agents specific for leukemia
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P37/00—Drugs for immunological or allergic disorders
    • A61P37/02—Immunomodulators
    • A61P37/04—Immunostimulants
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C07K14/4702—Regulators; Modulating activity
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
    • C07K14/70503—Immunoglobulin superfamily
    • C07K14/70507—CD2
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
    • A61K2039/55511—Organic adjuvants
    • A61K2039/55516—Proteins; Peptides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
    • A61K2039/55511—Organic adjuvants
    • A61K2039/55566—Emulsions, e.g. Freund's adjuvant, MF59
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K2039/80—Vaccine for a specifically defined cancer
    • A61K2039/804—Blood cells [leukemia, lymphoma]
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
    • Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
    • Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change

Definitions

  • the second amino acid sequence can comprise, or be, a targeting polypeptide, an immune stimulatory molecule, an
  • the one or more chemotherapeutic agents can be selected from the group consisting of cisplatin, carboplatin, procarbazine, mechlorethamine, cyclophosphamide, camptothecin, adriamycin, ifosfamide, melphalan, chlorambucil, bisulfan, nitrosurea, dactinomycin, daunorubicin, doxorubicin, bleomycin, plicomycin, mitomycin, etoposide, verampil, podophyllotoxin, taxol, transplatinum, 5-flurouracil, vincristin, vinblastin, methotrexate, and an analog of any of the aforementioned.
  • the method can also include administering to the subject one or more immune stimulating agents.
  • Fig. 8 is a series of two-dimensional FFC histograms depicting the proliferation of XBPl-CTL (XBPl 2M- CTL and XBPl-SP 3M CTL) following co-culture with MM or AML cells.
  • the Y-axis represents the number of each cell in the population and the x-axis represents the amount of carboxyfluoroscein succinimidyl ester (CFSE) in the cells.
  • CFSE carboxyfluoroscein succinimidyl ester
  • Fig. 11 is a bar graph depicting the affinity of fluorophore-labeled CD138 peptides for HLA- A2 molecules on the surface of human T2 cells.
  • Fig. 20 is a bar graph depicting the affinity of fluorophore-labeled CSl peptides for HLA- A2 molecules on the surface of human T2 cells.
  • the X-axis represents the mean fluorescence intensity and the Y-axis indicates the various peptides screened in the assay: CSl- Pl: CSl 2 36-245 (LLLSLFVLGL (SEQ ID NO: 15)); CS1-P2: CSl239-247 (SLFVLGLFL (SEQ ID NO: 16)); CS 1 -P3 : CS 1232-240 (LLVPLLLSL (SEQ ID NO: 17)); and CS 1-P4: CS I 9- I?
  • One suitable chemical cross-linker 4-succinimidyloxycarbonyl- ⁇ -methyl- ⁇ (2- pyridyldithio)toluene (SMPT), forms such a linkage between the two amino acid sequences utilizing a terminal lysine on one of the amino acid sequences and a terminal cysteine on the other.
  • SMPT 4-succinimidyloxycarbonyl- ⁇ -methyl- ⁇ (2- pyridyldithio)toluene
  • Heterobifunctional reagents which cross-link by a different coupling moiety on each amino acid sequence.
  • the resulting "dimers” will be heterodimers (peptides containing the first and second amino acid sequences) rather than either homodimers (e.g., two first amino acid sequences or two second amino acid sequences) or a mixture of homodimers and heterodimers.
  • a suitable in vivo method involves immunizating HLA transgenic mice, wherein peptides in adjuvant are administered subcutaneously to HLA transgenic mice and several weeks following immunization, splenocytes are removed and cultured in vitro in the presence of test peptide for approximately one week, peptide-specific T cells are detected using, e.g., a 51 Cr- release assay (see, e.g., Wentworth, P.
  • the activation of a T cell by a peptide can be determined by a CD 107 toxicity assay or calcein release assays (see, e.g., Examples 13 and 14).
  • compositions can also be associated with a detectable label.
  • a detectable label e.g., one or more of the MHC molecules of the multimer can be covalently or non-covalently bound to a detectable label.
  • Suitable detectable labels e.g., enzymes, fluorescent materials, luminescent materials, bioluminescent materials, or radionuclides
  • methods for joining detectable labels to a peptide or an MHC molecule are described above.
  • the disclosure also features a variety of methods for inducing an immune response in a subject.
  • the methods for inducing an immune response in a subject can include the step of administering to a subject one or more of any of peptides (or expression vectors containing nucleic acid sequences encoding the peptides) described herein (or any of the pharmaceutical compositions containing one or more peptides (or vectors) described herein). Any of the peptides described herein can be used to stimulate an immune response by use of a nucleic acid expression system that encodes one or more of the peptides described herein.
  • the VH or VL chain of the antibody can further include all or part of a heavy or light chain constant region, to thereby form a heavy or light immunoglobulin chain, respectively.
  • the antibody is a tetramer of two heavy immunoglobulin chains and two light immunoglobulin chains.
  • the heavy and light immunoglobulin chains can be connected by disulfide bonds.
  • the heavy chain constant region typically includes three constant domains, CHl, CH2 and CH3 and a hinge region.
  • the light chain constant region typically includes a CL domain.
  • the variable region of the heavy and light chains contains a binding domain that interacts with an antigen.
  • the constant regions of the antibodies typically mediate the binding of the antibody to host tissues or factors, including various cells of the immune system (e.g., effector cells) and the first component (CIq) of the classical complement system.
  • the cells were washed, and then contacted with a FITC-conjugated (or in the case of determining the binding of CSl peptides to HLA- A2, a PE-conjugated) mouse anti-human HLA- A2 monoclonal antibody for 15 minutes at 4 0 C.
  • the cells were again washed and then analyzed by fluorescence flow cytometry (FFC) using a FACSortTM flow cytometer with CellQuestTM v2.1 software (Becton Dickinson, San Jose, CA).
  • IFN-Y ELISA IFN-Y ELISA.
  • IFN- ⁇ release by XBPl-CTL, CD138-CTL, or CSl-CTL following co- culture with multiple myeloma (MM) cells (McCAR, MMlS), acute myelogenous leukemia (AML) cells (ML-2), or T2 cells (above) was measured using a human IFN- ⁇ ELISA kit from BD Biosciences (San Diego, CA). Briefly, dilutions of purified IFN- ⁇ as standards or CTL supernates were transferred into wells of a 96-well plate pre-coated with a monoclonal anti- human IFN- ⁇ capture antibody and incubated for 2 hours at room temperature.
  • XBPl-CTL were exposed to carboxyfluoroscein succinimidyl ester (CFSE) as described above. Proliferation of the XBPl-CTL in response to stimulation with various tumor lines was determined by measuring the amount of CFSE in the cells.
  • CFSE is a membrane permeable dye, which is taken up by cells. Upon cell division, one half of the CFSE is distributed to each daughter cell. In turn, when each of the daughter cells divide, a total of one quarter of the original CFSE concentration is distributed to the third generation cells. Thus, the number of cell divisions can be determined as the inverse of the concentration of dye in each cell of a population.

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Animal Behavior & Ethology (AREA)
  • Immunology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Molecular Biology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Genetics & Genomics (AREA)
  • Biophysics (AREA)
  • Biochemistry (AREA)
  • Zoology (AREA)
  • Toxicology (AREA)
  • Epidemiology (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Cell Biology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Engineering & Computer Science (AREA)
  • Oncology (AREA)
  • Hematology (AREA)
  • Peptides Or Proteins (AREA)
  • Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Microbiology (AREA)
  • Mycology (AREA)
  • Medicinal Preparation (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
  • Investigating Or Analysing Biological Materials (AREA)
  • Medicines Containing Material From Animals Or Micro-Organisms (AREA)
PCT/US2009/045866 2008-06-02 2009-06-01 Xbp1, cd138, and cs1 peptides Ceased WO2009149021A2 (en)

Priority Applications (8)

Application Number Priority Date Filing Date Title
EP09759182.0A EP2300034B1 (en) 2008-06-02 2009-06-01 Pharmaceutical composition for use in treating or preventing multiple myeloma or waldenstrom's macroglobulinemia
US12/995,661 US9096681B2 (en) 2008-06-02 2009-06-01 XBP1, CD138, and CS1 peptides
CA2726804A CA2726804C (en) 2008-06-02 2009-06-01 Xbp1, cd138, and cs1 peptides
JP2011512566A JP2011523560A (ja) 2008-06-02 2009-06-01 Ｘｂｐ１ペプチド、ｃｄ１３８ペプチドおよびｃｓ１ペプチド
EP18162674.8A EP3384919A1 (en) 2008-06-02 2009-06-01 Cs1 peptides
CN200980130349.4A CN102112147B (zh) 2008-06-02 2009-06-01 Xbp1、cd138、和cs1肽
US14/754,456 US11083783B2 (en) 2008-06-02 2015-06-29 XBP1, CD138, and CS1 peptides
US17/370,412 US20220031821A1 (en) 2008-06-02 2021-07-08 Xbp1, cd138, and cs1 peptides

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US5818008P 2008-06-02 2008-06-02
US61/058,180 2008-06-02

Related Child Applications (3)

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US12/995,661 A-371-Of-International US9096681B2 (en) 2008-06-02 2009-06-01 XBP1, CD138, and CS1 peptides
US14/754,456 Division US11083783B2 (en) 2008-06-02 2015-06-29 XBP1, CD138, and CS1 peptides
US14/754,456 Continuation US11083783B2 (en) 2008-06-02 2015-06-29 XBP1, CD138, and CS1 peptides

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WO2009149021A2 true WO2009149021A2 (en) 2009-12-10
WO2009149021A3 WO2009149021A3 (en) 2010-07-15

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US (3) US9096681B2 (enExample)
EP (2) EP2300034B1 (enExample)
JP (7) JP2011523560A (enExample)
CN (1) CN102112147B (enExample)
CA (2) CA2726804C (enExample)
WO (1) WO2009149021A2 (enExample)

Cited By (2)

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WO2014071402A1 (en) * 2012-11-05 2014-05-08 Dana-Farber Cancer Institute, Inc. Xbp1, cd138, and cs1, pharmaceutical compositions that include the peptides, and methods of using such petides and compositions
US9096681B2 (en) 2008-06-02 2015-08-04 Dana-Farber Cancer Institute, Inc. XBP1, CD138, and CS1 peptides

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WO2016049022A1 (en) * 2014-09-23 2016-03-31 Board Of Trustees Of Michigan State University Compositions and methods for modulating an immune response
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CN106093393A (zh) * 2016-06-02 2016-11-09 滨州医学院 一种基于XBP1和XBP1s表达水平的检测胃癌组织的试剂盒
CA3079422A1 (en) 2017-10-24 2019-05-02 Oncopep, Inc. Peptide vaccines and pembrolizumab for treating breast cancer
CN115040663B (zh) * 2022-06-15 2023-12-12 上海交通大学医学院附属仁济医院 溶质载体家族38成员2在制备多发性骨髓瘤治疗药物中的应用

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US5328470A (en) 1989-03-31 1994-07-12 The Regents Of The University Of Michigan Treatment of diseases by site-specific instillation of cells or site-specific transformation of cells and kits therefor
US5798113A (en) 1991-04-25 1998-08-25 Brown University Research Foundation Implantable biocompatible immunoisolatory vehicle for delivery of selected therapeutic products
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US6407213B1 (en) 1991-06-14 2002-06-18 Genentech, Inc. Method for making humanized antibodies
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US6602503B1 (en) 1993-01-12 2003-08-05 Biogen, Inc. Recombinant anti-VLA-4 antibody molecules
US5798230A (en) 1995-11-09 1998-08-25 Gsf-Forschungszentrum Fur Umwelt Und Gesundheit Gmbh Process for the preparation of human monoclonal antibodies and their use
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