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US20040097703A1 - Wt1 modified peptide - Google Patents

Wt1 modified peptide Download PDF

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US20040097703A1
US20040097703A1 US10/471,835 US47183503A US2004097703A1 US 20040097703 A1 US20040097703 A1 US 20040097703A1 US 47183503 A US47183503 A US 47183503A US 2004097703 A1 US2004097703 A1 US 2004097703A1
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cells
peptide
cancer
antigen
ser
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Haruo Sugiyama
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International Institute of Cancer Immunology Inc
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Assigned to INTERNATIONAL INSTITUTE OF CANCER IMMUNOLOGY, INC. reassignment INTERNATIONAL INSTITUTE OF CANCER IMMUNOLOGY, INC. ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Assignors: SUGIYAMA, HARUO
Priority to US12/552,660 priority Critical patent/US8105604B2/en
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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/82—Translation products from oncogenes
    • 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
    • C07K14/4748—Tumour specific antigens; Tumour rejection antigen precursors [TRAP], e.g. MAGE
    • 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
    • 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
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
    • A61K2039/515—Animal cells
    • A61K2039/5154—Antigen presenting cells [APCs], e.g. dendritic cells or macrophages
    • 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
    • A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
    • A61K2039/515—Animal cells
    • A61K2039/5158—Antigen-pulsed cells, e.g. T-cells
    • 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
    • A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
    • A61K2039/53—DNA (RNA) vaccination
    • 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

Definitions

  • the present invention relates to a cancer antigen based on the product of Wilms' tumor suppresser gene WT1.
  • This cancer antigen is useful as an anticancer vaccine against cancers of the blood such as leukemia, myelodysplastic syndrome, multiple myeloma and malignant lymphoma, solid cancers such as gastric cancer, colon cancer, lung cancer, breast cancer, germinal cell cancer, liver cancer, skin cancer, bladder cancer, prostate cancer, uterine cancer, cervical carcinoma and ovarian cancer, as well as any cancer that expresses WT1.
  • the immune mechanism for eliminating foreign objects from the body generally consists of humoral immunity, in which is involved macrophages that function as antigen-presenting cells that recognize an antigen, helper T-cells that activate other T-cells by recognizing antigens presented by said macrophages and producing various lymphokines, and B lymphocytes that differentiate into antibody-producing cells due to the action of said lymphokines; and, cellular immunity, by which killer T-cells (cytotoxic T-cells (CTL)), which have differentiated as a result of being presented with an antigen, attack and destroy target cells.
  • CTL cytotoxic T-cells
  • cancer immunity is thought to mainly be the result of cellular immunity involving killer T-cells.
  • precursor T-cells which have recognized cancer antigen presented in the form of a complex of major histocompatibility complex (MHC) class I (MHC class I antigen, also referred to as HLA antigen in the case of humans) and cancer antigen, differentiate and proliferate, and the resulting killer T-cells that have formed attack and destroy the cancer cells.
  • MHC class I antigen major histocompatibility complex
  • HLA antigen also referred to as HLA antigen in the case of humans
  • cancer antigen differentiate and proliferate, and the resulting killer T-cells that have formed attack and destroy the cancer cells.
  • the cancer cells present a complex of MHC class I antigen and cancer antigen on their cell surface, and this is targeted by the killer T-cells (Cur. Opin. Immunol., 5, 709, 1993; Cur. Opin. Immunol., 5, 719, 1993; Cell, 82, 13, 1995; Immun
  • the aforementioned cancer antigen presented by MHC class I antigen on the cancer cells serving as the target cells is thought to be a peptide composed of about 8-12 amino acids formed as a result of antigen protein synthesized within cancer cells being processed by intracellular protease (Cur. Opin. Immunol., 5, 709, 1993; Cur. Opin. Immunol., 5, 719, 1993; Cell, 82, 13, 1995; Immunol. Rev., 146, 167, 1995).
  • the tumor suppresser gene WT1 of Wilms tumor has been isolated from chromosome 11p13 as one of the causative genes of Wilms tumor based on analysis of the WAGR syndrome that occurs as a complication of Wilms tumor, aniridia, urogenital abnormalities, mental retardation and so forth (Gessler, M., et al., Nature, Vol. 343, p. 774-778 (1990)).
  • Its genomic DNA is about 50 kb and is composed of 10 exons, while its cDNA is about 3 kb.
  • the amino acid sequence estimated from cDNA is as shown in Sequence ID No. 1 (Mol. Cell. Biol., 11, 1707, 1991).
  • the WT1 gene is expressed with high frequency in human leukemia, and when leukemia cells are treated with WT1 antisense oligomer, the growth of the cells is inhibited (Japanese Unexamined Patent Publication No. 9-104627). Thus, WT1 gene is thought to act to promote the growth of leukemia cells. Moreover, WT1 is also highly expressed in solid cancers such as gastric cancer, colon cancer, lung cancer, breast cancer, germinal cell cancer, liver cancer, skin cancer, bladder cancer, prostate cancer, uterine cancer, cervical carcinoma and ovarian cancer (Japanese Patent Application No. 9-191635), and the WT1 gene has been demonstrated to be a novel tumor marker in leukemia and solid cancers.
  • an object of the present invention is to provide a peptide that is promising as a cancer vaccine and which has higher activity than previously known cancer-specific antigen peptides.
  • WT1 modified peptide having an amino acid sequence in which the second amino acid Met of the aforementioned known amino acid sequence (Sequence ID No. 2) is changed to Tyr, namely Cys Tyr Thr Trp Asn Gln Met Asn Leu (Sequence ID No. 3), has higher activity, thereby leading to completion of the present invention.
  • the present invention provides a peptide (WT1 modified peptide) consisting of 9-30 amino acids and comprising the following amino acid sequence: Cys Tyr Thr Trp Asn Gln Met Asn Leu (Sequence ID No. 3).
  • This peptide is preferably a polypeptide consisting of 9-12 amino acids and comprising the amino acid sequence indicated in Sequence ID No. 3 and, more preferably, a peptide consisting of the amino acid sequence indicated in Sequence ID No. 3.
  • the present invention provides a cancer vaccine having for its active ingredient the aforementioned WT1 modified peptide.
  • the present invention also provides a DNA vaccine against cancer having for its active ingredient DNA coding for the aforementioned peptide.
  • the present invention provides antigen-presenting cells on which presented a complex of HLA antigen (MHC class I antigen) and the aforementioned peptide.
  • the present invention also provides cytotoxic T-cells that recognize a complex of HLA antigen and the aforementioned peptide.
  • FIG. 1 is a graph showing the cell killing effects (specific cytolytic activity) on C1R2402 target cells (T), either pulsed or not pulsed with peptide, by effecter cells (E) stimulated with WT1 wild peptide (Sequence ID No. 2) or the WT1 modified peptide of the present invention (Sequence ID No. 3).
  • the black circles indicate the cytolytic effect on C1R2402 target cells pulsed with wild peptide by effecter cells stimulated with WT1 modified peptide
  • the black squares indicate the cytolytic effect on C1R2404 target cells pulsed with wild peptide by effecter cells stimulated with WT1 wild peptide
  • the white circles indicate the cytolytic effect on C1R2402 target cells not pulsed with wild peptide by effecter cells stimulated with WT1 modified peptide
  • the white squares indicate the cytolytic effect on C1R2402 target cells not pulsed with wild peptide by effecter cells stimulated with WT1 wild peptide.
  • FIG. 2 is a graph showing the cytolytic activity on acute myelocytic leukemia cells endogenously expressing WT1 antigen or on acute myelocytic leukemia cells not expressing WT1 antigen by effecter cells stimulated with WT1 wild peptide or the WT1 modified peptide of the present invention.
  • FIG. 3 is a graph showing the cell killing effects (specific cytolytic activity) on C1R2402 target cells, either pulsed or not pulsed with peptide, by effecter cells stimulated with WT1 wild peptide or the WT1 modified peptide of the present invention.
  • the black circles indicate the cytolytic effect on C1R2402 cells pulsed with wild peptide by effecter cells stimulated with WT1 modified peptide
  • the black squares indicate the cytolytic effect on C1R2402 target cells pulsed with wild peptide by effecter cells stimulated with WT1 wild peptide
  • the white circles indicate the cytolytic effect on C1R2402 target cells not pulsed with wild peptide by effecter cells stimulated with WT1 modified peptide
  • the white squares indicate the cytolytic effect on C1R2402 target cells not pulsed with wild peptide by effecter cells stimulated with WT1 wild peptide.
  • FIG. 4 is a graph showing the cytolytic activity on lung cancer cell lines endogenously expressing WT1 or not expressing WT1 by effecter cells stimulated with WT1 wild peptide or the WT1 modified peptide of the present invention.
  • FIG. 5 is a graph showing the inhibitory effects of anti-HLA class I antibody, anti-HLA class II antibody and anti-CD8 antibody on the cell killing effects (specific cytolytic activity) on C1R2402 target cells pulsed with wild peptide by effecter cells stimulated by WT1 wild peptide or the WT1 modified peptide of the present invention.
  • the peptide of the present invention is a peptide consisting of 9-30 amino acids that comprises the amino acid sequence consisting of the 9 amino acids shown in Sequence ID No. 3.
  • the peptide is preferably a peptide consisting of 9-12 amino acids that comprises the amino acid sequence shown in Sequence ID No. 3 and, more preferably, is a peptide having rules (motifs) in the sequence of antigen peptide presented by binding to HLA antigen at that time (J. Immunol., 152, p. 3913, 1994; Immunogenetics, 41, p. 178, 1995; J. Immunol., 155, p. 4307, 1994; J. Immunol., 155, p. 4749, 1995).
  • the peptide is most preferably a peptide consisting of an amino acid sequence of the 9 amino acids shown in Sequence ID No. 3.
  • the aforementioned “peptide comprising the amino acid sequence shown in Sequence ID No. 3” is specifically, for example, a peptide comprising the amino acid sequence shown in Sequence ID No. 3 and extending in the direction of the N-terminal and/or the direction of the C-terminal from the applicable position on WT1 (Sequence ID No. 1) (position nos. 235-243) or from the corresponding position on human WT1 (NCBI Database Accession No. XP012009), that has activity as a cancer antigen peptide.
  • An example of a method for measuring the activity of the cancer antigen peptide of the present invention is the method described in J. Immunol., 154, p. 2257, 1995. The following provides an explanation of an outline of this method using the case of the type of HLA being HLA-A24 as an example.
  • peripheral blood lymphocytes are isolated from a person positive for HLA-A24 antigen.
  • CTL cytotoxic T-cells
  • This induction of CTL can be investigated by, for example, measuring the amounts of various cytokines (e.g., IFN- ⁇ ) produced by the CTL by reacting with the complex of antigen peptide and HLA-A24.
  • induction of CTL can also be investigated by a method in which the cytotoxicity of the CTL is measured with respect to antigen peptide-presenting cells labeled with 51 Cr or Europium ( 51 Cr Release Assay, Int. J. Cancer, 58, p. 317, 1994; Europium Release Assay, J. Immunol., 154, p. 3991, 1995).
  • induction of CTL can also be investigated by referring to the examples described later.
  • the present invention also relates to a cancer vaccine that has the aforementioned antigen as its active ingredient.
  • This vaccine can be used for the prevention or treatment of cancers of the blood such as leukemia, myelodysplastic syndrome, multiple myeloma and malignant lymphoma, as well as solid cancers such as gastric cancer, colon cancer, lung cancer, breast cancer, germinal cell cancer, liver cancer, skin cancer, bladder cancer, prostate cancer, uterine cancer, cervical carcinoma and ovarian cancer.
  • this vaccine can be applied to patients positive for HLA-A24.
  • This vaccine can be administered orally or parenterally by for example, intraperitoneal, subcutaneous, intracutaneous, intramuscular, intravenous or intranasal administration.
  • administration of the vaccine of the present invention can also be carried out by a method in which monocytes are collected from the peripheral blood of a patient, dendritic cells are extracted from the monocytes, the dendritic cells are pulsed with the peptide of the present invention and then returned to the patient by subcutaneous administration and so forth.
  • cytotherapy cytotherapy or dendritic cell (DC) therapy
  • DC dendritic cell
  • the vaccine in addition to the peptide administered as the aforementioned active ingredient, may also contain pharmaceutically allowable carriers such as a suitable adjuvant (Clin-Microbiol. Rev., 7, 277-289, 1994), examples of which include a mineral gel like aluminum hydroxide, a surfactant like phosphorous lecithin and a pluronic polyole, a polyanion, a peptide and an oily emulsion.
  • the vaccine may contain other aggregates mixed into liposomes or blended into polysaccharide or the vaccine.
  • the dosage is typically 0.1 ⁇ g/kg to 1 mg/kg per day.
  • DNA that codes the aforementioned polypeptide vaccine can also be used as a vaccine (DNA vaccine). Namely, after inserting nucleic acids, and preferably DNA, that contain nucleic acids that encode the WT1 modified peptide of the present invention into a suitable vector, and preferably an expression vector, cancer immunity can be imparted by administering the vector to an animal.
  • a suitable vector and preferably an expression vector
  • cancer immunity can be imparted by administering the vector to an animal.
  • WO 00/6602 or J. Immunol., 160, p. 1717, 1998 and so forth should be referred to for the specific technique used for this DNA vaccine.
  • the present invention relates to antigen-presenting cells on which a complex of HLA antigen and the aforementioned peptide is presented.
  • antigen-presenting cells on which a complex of HLA antigen and the aforementioned peptide is presented.
  • HLA-A24 antigen HLA antigen
  • CTL cytotoxic T-cells
  • the antigen-presenting cells used in cytotherapy are produced by isolating cells having the ability to present antigen from tumor patients, pulsing these cells with peptide of the present invention outside the body, and causing a complex of HLA antigen and the peptide of the present invention to be presented on the surface of the cells.
  • the “cells having the ability to present antigen” are cells that express HLA antigen capable of presenting the peptide of the present invention on the surface of the cells, dendritic cells are preferable since they are considered to have high antigen-presenting ability.
  • the peptide of the present invention that is used to pulse the aforementioned cells having the ability to present antigen may not only be in the form of a peptide, but rather may also be in the form of DNA or RNA that encodes said peptide.
  • a specific method for preparing the antigen-presenting cells of the present invention can be referred to in, for example, Cancer Immunol. Immunother., 46, 82, 1998, J. Immunol., 158, p. 1796, 1997, and Cancer Res., 59, p. 1184, 1999.
  • dendritic cells lymphocytes are isolated from the peripheral blood of a tumor patients using the Fycoll method, and after subsequently removing the non-adhered cells, dendritic cells are derived from the adhered cells by culturing in the presence of GM-CSF and IL-4, after which the antigen-presenting cells of the present invention can be prepared by pulsing the dendritic cells by culturing with the peptide of the present invention.
  • insertion can be carried out by referring to, for example, Cancer Res., 56, p. 5672, 1996 or J. Immunol., 161, p. 5607, 1998 in the case of DNA, or by referring to J. Exp. Med., 184, p. 465, 1996 in the case of RNA.
  • these antigen-presenting cells can be used as the active ingredient of a tumor therapeutic agent.
  • the treatment agent preferably comprises physiological saline, phosphate-buffered saline (PBS) or medium and so forth.
  • administration methods include intravenous administration, subcutaneous administration and intracutaneous administration.
  • the present invention also relates to cytotoxic T-cells (CTL) that recognize a complex of HLA antigen and the aforementioned peptide.
  • CTL cytotoxic T-cells
  • the CTL of the present invention can be effectively used in the adoptive immunotherapy described below.
  • the CTL of the present invention can be used as the active ingredient of a tumor therapeutic agent.
  • the therapeutic agent preferably comprises physiological saline, phosphate-buffered saline (PBS) or medium and so forth.
  • administration methods include intravenous administration, subcutaneous administration and intracutaneous administration.
  • Peripheral blood mononuclear cells were isolated from HLA-A*2402-positive donors and distributed among the wells of a 24-well plate at 2 ⁇ 10 6 cells/well followed by the addition of WT1 wild peptide or WT1 modified peptide to a concentration of 20 ⁇ M and culturing for 1 week.
  • the medium used at this time consisted of 45% RPMI, 45% AIV, 10% FCS 1 ⁇ non-essential amino acids and SM/PCG. Following the aforementioned culturing, the cells were adjusted to 2 ⁇ 10 6 cells/well and used as responder cells.
  • peripheral blood mononuclear cells were similarly isolated from the same HLA-A*2402-positive donors and then peptide-pulsed by culturing for 4 days with one of the aforementioned peptides at 20 ⁇ M. After then irradiating at 30 Gy, the cells were adjusted to 4 ⁇ 10 6 cells/well and used as stimulator cells.
  • WT1+/A*2402+ cells leukemia cells from AML patient #1
  • WT1 ⁇ /A*2402+ cells leukemia cells from AML patient #2
  • WT1+/A*2402 ⁇ cells leukemia cells from AML patient #3
  • WT1 ⁇ /A*2402 ⁇ cells leukemia cells from AML patient #4
  • Example 2 The same experiment as Example 1 was carried out using effector cells prepared from peripheral blood mononuclear cells of different healthy donors positive for HLA-A*2402. Those results are shown in FIG. 3.
  • the cytotoxic activity of effector cells stimulated with WT1 wild peptide or WT1 modified peptide was tested on a cancer cell line associated with lung cancer that endogenously expresses WT1 antigen (target cells) using the 51 Cr release method.
  • RERF-LCAI WT1+/A*2402+
  • LC1sq WT1+/A*2402+
  • 11-18 WT1 ⁇ /A*2402+
  • LK87 WT1+/A*2402 ⁇
  • Effector cells stimulated with WT1 wild peptide or WT1 modified peptide were confirmed to be CD8-positive killer cells that bind to HLA class I by a blocking assay using antibody.
  • the antibodies used consisted of anti-HLA class I antibody, anti-HLA class II antibody and anti-CD8 antibody.
  • Effector cells (E) prepared in the same manner as Example 1 and target cells (T) in the form of C1R2402 cells or C1R2402 cells pulsed with WT1 wild peptide, both labeled with 51 Cr, were mixed with antibody at an E:T ratio of 20:1 and then cultured for 4 hours followed by measurement of the degree of cell lysis according to the 51 Cr release method. Those results are shown in FIG. 5.
  • WT1 modified peptide demonstrated stronger binding affinity for HLA-A*2402 than the WT1 wild peptide.
  • the peptide of the present invention was proven to unquestionably function as a cancer antigen, and cause the induction and proliferation of killer T-cells (cancer cell cytotoxic T-cells) against cancer cells.
  • the cancer antigen peptide of the present invention is useful as a cancer vaccine against leukemia and solid cancers accompanying an increased expression of the WT1 gene.

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US6815291B2 (en) 2002-02-20 2004-11-09 Seiko Epson Corporation Method of manufacturing semiconductor device
US20040247609A1 (en) * 2001-09-28 2004-12-09 Haruo Sugiyama Novel method of inducing antigen-specific t cells
US20050002951A1 (en) * 2001-09-28 2005-01-06 Haruo Sugiyama Novel method of inducing antigen-specific t cells
US20050266014A1 (en) * 1998-07-31 2005-12-01 Haruo Sugiyama Tumor antigen based on products of the tumor suppressor gene WT1
US20060205667A1 (en) * 2002-09-20 2006-09-14 Haruo Sugiyama Wt1 substitution pepides
US20060217297A1 (en) * 2003-01-15 2006-09-28 Haruo Sugiyama Dimerized peptide
US20070036808A1 (en) * 2002-09-12 2007-02-15 Haruo Sugiyama Cancer antigen peptide formulations
US7420034B2 (en) 2002-06-12 2008-09-02 Dainippon Sumitomo Pharma Co., Ltd. HLA-A24-restricted cancer antigen peptides
US20090325886A1 (en) * 2001-03-22 2009-12-31 International Institute Of Cancer Immunology, Inc Wt1 modified peptide
US20100062010A1 (en) * 2005-11-30 2010-03-11 International Institute Of Cancer Immunology, Inc. Novel peptide compound
US20100062013A1 (en) * 2004-03-31 2010-03-11 International Institute Of Cancer Immunology, Inc. Cancer antigen peptides derived from wt1
US20160009781A1 (en) 2012-09-12 2016-01-14 International Institute Of Cancer Immunology, Inc. Antigen-specific helper t-cell receptor genes
US9663563B2 (en) 2013-03-12 2017-05-30 Sumitomo Dainippon Pharma Co., Ltd. Aqueous liquid composition
US9803246B2 (en) 2011-06-28 2017-10-31 International Institute Of Cancer Immunology, Inc. Receptor gene for peptide cancer antigen-specific T cell
US9833493B2 (en) 2012-12-17 2017-12-05 International Institute Of Cancer Immunology, Inc. Method for activating helper T cell
US10093977B2 (en) 2007-03-05 2018-10-09 International Institute Of Cancer Immunology, Inc. Cancer antigen-specific T-cell receptor gene, peptide encoded by the gene, and use of them
US10124046B2 (en) 2003-11-05 2018-11-13 International Institute Of Cancer Immunology, Inc. HLA-DR-binding antigen peptide derived from WT1
US10139395B2 (en) 2007-02-27 2018-11-27 International Institute Of Cancer Immunology, Inc. Method for activation of helper T cell and composition for use in the method
US10253075B2 (en) 2014-02-26 2019-04-09 tella, Inc. WT1 antigenic polypeptide, and anti-tumor agent containing said polypeptide
US10426822B2 (en) 2007-12-05 2019-10-01 International Institute Of Cancer Immunology, Inc. Cancer vaccine composition
US10471136B2 (en) 2014-09-27 2019-11-12 Sumitomo Dainippon Pharma Co., Ltd. Pharmaceutical composition for injection
US10500257B2 (en) 2003-06-27 2019-12-10 International Institute Of Cancer Immunology, Inc. Method of selecting WT1 vaccine adaptive patient
US10588952B2 (en) 2013-03-29 2020-03-17 Sumitomo Dainippon Pharma Co., Ltd. Conjugate vaccine using trimming function of ERAP1
US10654892B2 (en) 2010-10-05 2020-05-19 International Institute Of Cancer Immunology, Inc. Method for activating helper T cell
US11759509B2 (en) 2013-03-29 2023-09-19 Sumitomo Pharma Co., Ltd. WT1 antigen peptide conjugate vaccine
US12383608B2 (en) 2016-11-30 2025-08-12 Sumitomo Pharma Co., Ltd. WT1 helper peptides and combinations of WT1 helper peptide and conjugate of cancer antigen peptides

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EP2518149B1 (en) * 2006-02-22 2015-12-16 International Institute of Cancer Immunology, Inc. HLA-A*3303-restricted WT1 peptide and pharmaceutical composition comprising the same
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CA2440303A1 (en) 2002-10-10
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US20090325886A1 (en) 2009-12-31
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ES2298353T3 (es) 2008-05-16
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BR0208183A (pt) 2004-03-02
KR100863853B1 (ko) 2008-10-15
KR20030084970A (ko) 2003-11-01
WO2002079253A1 (en) 2002-10-10
JP2006034296A (ja) 2006-02-09
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BRPI0208183B8 (pt) 2021-05-25
ATE383375T1 (de) 2008-01-15

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