METHOD FOR SELECTING SUBJECTS LIKELY TO BENEFIT FROM A PHARMACEUTICAL COMPOSITION TO TREAT OR PREVENT CANCER

Abstract

The present invention relates to a method for selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer, characterized in that it comprises: determining the presence or absence of a mutation in the p53 tumor protein gene (TP53) and the BCL6 corepressor gene (BCOR) using a sample of body fluid taken from the subject; and provide an indication that the subject is a potential beneficiary of the pharmaceutical composition in the case of wild-type TP53 and wild-type BCOR, wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof,The cancer is selected from the group consisting of acute myeloid leukemia (AML), myelodysplastic syndrome (MDS), myeloproliferative neoplasia (MPN), chronic myeloid leukemia (CML), chronic myelomonocytic leukemia (CMML), and juvenile myelomonocytic leukemia (JMML). Wild-type TP53 refers to the case in which there is no mutation present in the TP53 gene, or the case in which the TP53 gene, even when a mutation is present, does not lose its original function or is not accompanied by abnormality. Wild-type BCOR refers to the case in which there is no mutation present in the BCOR gene, or the case in which the BCOR gene, even when a mutation is present, does not lose its original function or is not accompanied by abnormality.

Description

BRIEF DESCRIPTION OF THE INVENTION technical problem Accordingly, an object of the present invention is to provide a method for selecting a potential subject who will benefit from a pharmaceutical composition for treating or preventing cancer. Here, the pharmaceutical composition comprises a WT1 killer peptide and / or a WT1 helper peptide. Problem solution The present inventors have carried out laborious studies to achieve the objective and consequently completed the present invention by finding a method for selecting a potential subject who will benefit from a pharmaceutical composition for treating or preventing cancer on the basis of the presence or absence of a mutation. in the tumor protein gene p53 (TP53) and / or the BCL6 corepressor gene (NCOR), and the degree of mRNA expression of the WT1 gene, etc. Specifically, the present invention includes, for example, the following invention. [1] A method for selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer, comprising: determining the presence or absence of a mutation in the TP53 gene and / or the BCOR gene using a sample taken from the subject; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition in the case of wild-type TP53 and / or wild-type BCOR, wherein the pharmaceutical composition comprises a peptide comprising a selected amino acid sequence of the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO : 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof. [2] The method according to subsection [1], wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8 ), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), or a pharmaceutically acceptable salt thereof. [3] The method according to subsection [1] or [2], wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof. [4] The method according to any of subsections [1] to [3], wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), and a peptide comprising a amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof. [5] The method according to any of subsections [1] to [4], wherein the pharmaceutical composition comprises a compound represented by formula (1): O η II π--------:------------ HL X X . JTumor antigenic peptide A rOH x8γ ----------------r(i) Yo R1 where X and Ya represent a single bond, tumor antigenic peptide A represents a peptide consisting of any of the amino acid sequences selected from the following amino acid sequences: RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 7) : 9), the amino group of the N-terminal amino acid of tumor antigenic peptide A is linked to Yade formula (1), the carbonyl group of the C-terminal amino acid of tumor antigenic peptide A is linked to the hydroxy group of formula (1 ), R1 represents a hydrogen atom or a B tumor antigen peptide, B tumor antigen peptide differs in sequence from A tumor antigen peptide and represents a peptide consisting of any amino acid sequence selected from the following amino acid sequences: CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), and the thioether group of the cysteine ​​residue of the tumor antigenic peptide B is linked to the thioether group of formula (1), or a pharmaceutically acceptable salt thereof . [6] The method according to any of items [1] to [5], wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of RMFPNAPYL (SEQ ID NO: 2), or a pharmaceutically acceptable salt of the same. [7] The method according to any of items [1] to [5], wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of YMFPNAPYL (SEQ ID NO: 2), or a pharmaceutically acceptable salt of the same. [8] The method according to any of items [1] to [5], wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of CCMTWNQMNL (the bond between C and C represents a disulfide bond, SEQ ID NO: 21), or a pharmaceutically acceptable salt thereof. [9] The method according to any of items [1] to [5], wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of CCYTWNQMNL (the bond between C and C represents a disulfide bond, SEQ ID NO: 10), or a pharmaceutically acceptable salt thereof.

[10] The method according to any of items [1] to [9], wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15), or a pharmaceutically acceptable salt of the same.

[11] The method according to any of items [1] to [9], wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt of the same.

[12] The method according to any of items [1] to [9], wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt of the same.

[13] The method according to item [5], wherein the compound represented by formula (1) is a compound represented by formula (2): CRMFPNAPYL CMTWNQMNL(2) wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof.

[14] The method in accordance with subsection [5], wherein the compound represented by formula (1) is a compound represented by formula (3): CRMFPNAPYL I (3) CYTWNQMNL wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof.

[15] The method according to any of items [1] to

[14] , wherein the pharmaceutical composition further comprises a peptide comprising an amino acid sequence selected from the group consisting of CNKRYFKLSHLQMHSRK (SEQ ID NO: 11 ), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a salt pharmaceutically acceptable thereof.

[16] The method in accordance with subsection [5], wherein the compound represented by formula (1) is a compound represented by formula (2): CRMFPNAPYL CMTWNQMNL(2) wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition further comprises WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt thereof .

[17] The method in accordance with subsection [5], wherein the compound represented by formula (1) is a compound represented by formula (3): CRMFPNAPYL CYTWNQMNL(3) wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition further comprises WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt thereof .

[18] The method according to any of items [1] to

[17] , wherein the pharmaceutical composition comprises a pharmaceutically acceptable carrier.

[19] The method according to any of items [1] to [8], wherein in the case of wild-type TP53, an indication is provided that the subject is a potential subject to benefit from the pharmaceutical composition .

[20] The method according to any of items [1] to

[19] , where in the case of wild-type TP53 and wild-type BCOR, an indication is provided that the subject is a potential subject that is benefit from the pharmaceutical composition.

[21] The method according to any of items [1] to

[20] , further comprising: determining the degree of expression of WT1 gene mRNA using a sample taken from the subject; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the degree of WT1 gene mRNA expression is less than a reference value or the reference value or less.

[22] The method in accordance with any of subsections [1] to

[21] , which also includes: detecting WT1 antigen peptide-specific CD8 T cells using a sample taken from the subject to which the pharmaceutical composition or the peptide or pharmaceutically acceptable salt thereof is administered according to any of items [1] to

[18] ; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when WT1 antigen peptide-specific CD8 T cells have been elevated as compared to a sample taken from the subject prior to administration.

[23] The method according to item

[22] , wherein the detection of WT1 antigen peptide-specific CD8 T cells is performed by reacting a complex of a WT1 peptide and an HLA molecule with the sample, and examining the presence or number of WT1 antigenic peptide-specific CD8 T cells that recognize the complex contained in the sample.

[24] The method according to item

[23] , wherein the complex of a WT1 peptide and an HLA molecule is in the form of a tetramer.

[25] The method in accordance with subsection

[23] or

[24] , wherein the HLA molecule is compatible with the HLA of the subject.

[26] The method according to any of items

[22] to

[25] , wherein detection of WT1 antigen peptide-specific CD8 T cells comprises analysis by a flow cytometry method.

[27] The method according to any of items [1] to

[26] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when a hypersensitivity reaction is detected late type in the subject to which the pharmaceutical composition, or the peptide or pharmaceutically acceptable salt thereof according to any of items [1] to

[18] is administered a plurality of times.

[28] The method according to subparagraph

[27] , further comprising comparing the reaction at the site of administration of the pharmaceutical composition or the peptide or pharmaceutically acceptable salt thereof according to any of the subparagraphs [ 1] to

[18] in the subject, with the reaction at a site without administration of the pharmaceutical composition or the peptide or pharmaceutically acceptable salt thereof in the subject, and providing an indication that the subject is a potential subject to be benefit from the pharmaceutical composition when the difference between the reaction at the site of administration and the reaction at a site without administration is a reference value or greater.

[29] The method according to any of items [1] to

[28] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when IPSS-based karyotyping revised (IPSS-R) of the subject is different from very bad.

[30] The method in accordance with any of subsections [1] to

[29] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the value obtained by dividing the proportion of myeloblasts in a sample taken from the subject to whom the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is administered according to any of subsections [1] to

[18] in the subject, between the proportion of myeloblasts in a sample taken from the subject before administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof, is less than a reference value or the reference value or less.

[31] The method in accordance with any of subsections [1] to

[30] , wherein the sample is selected from the group consisting of body fluid, mucous membrane, a cell, a tissue and a cell or tissue culture, and combinations thereof.

[32] The method in accordance with any of subsections [1] to

[31] , wherein the cancer is selected from the group consisting of leukemia, myelodysplastic syndrome, multiple myeloma, malignant lymphoma, stomach cancer, colorectal cancer, cancer lung cancer, breast cancer, germ cell cancer, liver cancer, skin cancer, urinary bladder cancer, prostate cancer, uterine cancer, cervical cancer, ovarian cancer and brain tumor.

[33] A method for the treatment of cancer, comprising: selecting a potential subject who will benefit from a pharmaceutical composition for treating or preventing cancer, by a method according to any of subsections [1] to

[32] ; and administering the pharmaceutical composition according to subsections [1] to

[18] to the selected subject.

[34] A pharmaceutical composition for use in a method of treating cancer, comprising: a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: : 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof, wherein The treatment method includes: selecting a potential subject who will benefit from a pharmaceutical composition for treating or preventing cancer, by a method according to any of subsections [1] to

[33] ; and administering the pharmaceutical composition to the selected subject.

[35] A method for selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer, comprising: determining the degree of mRNA expression of the WT1 gene using a sample taken from the subject; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the degree of expression of the WT1 gene is less than a reference value or the reference value or less, wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL ( SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12 ), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[36] The method according to subsection

[35] , wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8 ), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), or a pharmaceutically acceptable salt thereof.

[37] The method according to subsection

[35] or

[36] , wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof.

[38] The method according to any of subsections

[35] to

[38] , wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), and a peptide comprising a amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof.

[39] The method according to any of subsections

[35] to

[38] , wherein the pharmaceutical composition comprises a compound represented by formula (1): EITHER Η II ------------------------K x JTumor antigenic peptide A rOH xaγ -------------Γ(η Yo R1 where X and Ya represent a single bond, tumor antigenic peptide A represents a peptide consisting of any of the amino acid sequences selected from the following amino acid sequences: RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 7) : 9), the amino group of the N-terminal amino acid of tumor antigenic peptide A is linked to Yade formula (1), the carbonyl group of the C-terminal amino acid of tumor antigenic peptide A is linked to the hydroxy group of formula (1 ), R1 represents a hydrogen atom or a tumor antigenic peptide B, the tumor antigenic peptide B differs in its sequence from the tumor antigenic peptide A and represents a peptide consisting of any amino acid sequence selected from the following amino acid sequences: CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), and the thioether group of the cysteine ​​residue of the tumor antigenic peptide B is linked to the thioether group of the formula (1), or a pharmaceutically acceptable salt thereof .

[40] The method according to any of subsections

[35] to

[39] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of RMFPNAPYL (SEQ ID NO: 2), or a pharmaceutically acceptable salt of the same.

[41] The method according to any of subsections

[35] to

[39] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of YMFPNAPYL (SEQ ID NO: 2), or a pharmaceutically acceptable salt of the same.

[42] The method according to any of subsections

[35] to

[39] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of C-CMTWNQMNL (the bond between C and C represents a bond of disulfide, SEQ ID NO: 21), or a pharmaceutically acceptable salt thereof.

[43] The method according to any of subsections

[35] to

[39] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of C-CYTWNQMNL (the bond between C and C represents a bond of disulfide, SEQ ID NO: 10), or a pharmaceutically acceptable salt thereof.

[44] The method according to any of subsections

[35] to

[43] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15), or a pharmaceutically acceptable salt of the same.

[45] The method according to any of subsections

[35] to

[43] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt of the same.

[46] The method according to any of subsections

[35] to

[43] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt of the same.

[47] The method in accordance with subsection

[39] , wherein the compound represented by formula (1) is a compound represented by formula (2): CRMFPNAPYL CMTWNQMNL(2) wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof.

[48] ​​The method in accordance with subsection

[39] , wherein the compound represented by formula (1) is a compound represented by formula (3): CRMFPNAPYL I (3) CYTWNQMNL wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof.

[49] The method according to any of subsections

[35] to

[48] , wherein the pharmaceutical composition further comprises a peptide consisting of an amino acid sequence selected from the group consisting of CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[50] The method in accordance with subsection

[39] , wherein the compound represented by formula (1) is a compound represented by formula (2): CRMFPNAPYL CMTWNQMNL(2) wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition further comprises WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt thereof .

[51] The method according to item

[39] , wherein the compound represented by formula (1) is a compound represented by formula (3): CRMFPNAPYL I (3) CYTWNQMNL wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition further comprises WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt thereof.

[52] The method according to any of items

[35] to

[50] , wherein the pharmaceutical composition comprises a pharmaceutically acceptable carrier.

[53] The method in accordance with any of subsections

[35] to

[52] , which also includes: determining the presence or absence of a mutation in the TP53 gene and / or the BCOR gene using a sample taken from the subject; and providing, in the case of wild-type TP53 and / or wild-type BCOR, an indication that the subject is a potential subject to benefit from the pharmaceutical composition.

[54] The method according to item

[53] , wherein in the case of wild-type TP53, an indication is provided that the subject is a potential subject to benefit from the pharmaceutical composition.

[55] The method according to

[53] or

[54] , where in the case of wild-type TP53 and wild-type BCOR, an indication is provided that the subject is a potential subject to benefit from the pharmaceutical composition.

[56] The method in accordance with any of subsections

[35] to

[55] , which also includes: detecting WT1 antigen peptide-specific CD8 T cells using a sample taken from the subject to which the pharmaceutical composition or the peptide or pharmaceutically acceptable salt thereof is administered according to any of items

[35] to

[52] ; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when WT1 antigen peptide-specific CD8 T cells have been elevated as compared to a sample taken from the subject prior to administration.

[57] The method according to item

[56] , wherein the detection of WT1 antigen peptide-specific CD8 T cells is performed by reacting a complex of a WT1 peptide and an HLA molecule with the sample, and examining the presence or number of WT1 antigen peptide-specific CD8 T cells that recognize the complex contained in the sample.

[58] The method according to item

[57] , wherein the complex of a WT1 peptide and an HLA molecule is in the form of a tetramer.

[59] The method according to item

[57] or

[58] , wherein the HLA molecule is HLA-matched to the subject.

[60] The method according to any of subsections

[56] to

[59] , wherein the detection of WTl antigenic peptide-specific CD8 T cells comprises an analysis by a flow cytometry method.

[61] The method in accordance with any of subsections

[35] to

[60] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when a hypersensitivity reaction is detected late type in the subject to whom the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is administered a plurality of times according to any of subsections

[35] to

[52] .

[62] The method in accordance with subsection

[61] , further comprising comparing the reaction at the site of administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof according to any of the subsections [ 35] to

[52] in the subject, with the reaction at a site without administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof in the subject, and providing an indication that the subject is a potential subject to be benefit from the pharmaceutical composition when the difference between the reaction at the site of administration and the reaction at a site without administration is a reference value or greater.

[63] The method in accordance with any of subsections

[35] to

[62] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when karyotyping based on the IPSS revised (IPSS-R) of the subject is different from very bad.

[64] The method in accordance with any of subsections

[35] to

[63] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the value obtained by dividing the proportion of myeloblasts in a sample taken from the subject to whom the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is administered according to any of subsections

[35] to

[52] in the subject, between the proportion of myeloblasts in a sample taken from the subject before administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof, is less than a reference value or the reference value or less.

[65] The method in accordance with any of subsections

[35] to

[64] , wherein the sample is selected from the group consisting of body fluid, mucous membrane, a cell, a tissue and a cell or tissue culture, and combinations thereof.

[66] The method in accordance with any of subsections

[35] to

[65] , wherein the cancer is selected from the group consisting of leukemia, myelodysplastic syndrome, multiple myeloma, malignant lymphoma, stomach cancer, colorectal cancer, cancer lung cancer, breast cancer, germ cell cancer, liver cancer, skin cancer, urinary bladder cancer, prostate cancer, uterine cancer, cervical cancer, ovarian cancer and brain tumor.

[67] A method for the treatment of cancer, comprising: selecting a potential subject who will benefit from a pharmaceutical composition for treating or preventing cancer by the method according to any of subsections

[35] to

[66] ; and administering the pharmaceutical composition according to subsections

[35] to

[52] to the selected subject.

[68] A pharmaceutical composition for use in a method of treating cancer, comprising: a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: : 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof, wherein The treatment method includes: selecting a potential subject who will benefit from a pharmaceutical composition for treating or preventing cancer by the method according to any of subsections

[35] to

[66] ; and administering the pharmaceutical composition to the selected subject.

[69] The use of the TP53 gene and / or the BCOR gene as a marker to provide an indication of whether or not a potential subject will benefit from a pharmaceutical composition for treating or preventing cancer, wherein the pharmaceutical composition comprises a peptide that comprises an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12) , CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[70] Use in accordance with subsection

[69] , where an indication is provided of whether or not a potential subject will benefit from a pharmaceutical composition to treat or prevent cancer, based on the presence or absence of a gene mutation.

[71] The use of the WT1 gene as a marker to provide an indication of whether or not a potential subject will benefit from a pharmaceutical composition for treating or preventing cancer, based on the degree of mRNA expression of the WT1 gene, wherein The pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: : 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO : 16), or a pharmaceutically acceptable salt thereof.

[72] Use in accordance with subsection

[71] , wherein an indication that a potential subject will benefit from a pharmaceutical composition to treat or prevent cancer is provided when the degree of mRNA expression of the WT1 gene is less than a reference value or the reference value or less.

[73] A method for evaluating the effect of a candidate substance of a pharmaceutical composition for treating or preventing cancer, comprising: detecting WT1 antigenic peptide-specific CD8 T cells using a sample taken from a subject administered the pharmaceutical composition, or a peptide or a pharmaceutically acceptable salt thereof contained in the pharmaceutical composition; and provide an indication that the candidate substance likely produces an effect on the treatment and prevention of cancer when WT1 antigenic peptide-specific CD8 T cells have been elevated compared to a sample taken from the subject before administration, wherein the composition pharmaceutical comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6 ), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[74] A method for evaluating the effect of a candidate substance of a pharmaceutical composition for treating or preventing cancer, comprising: provide an indication that the candidate substance is likely to produce an effect on the treatment and prevention of cancer when a late-type hypersensitivity reaction is detected in a subject administered a plurality of times the pharmaceutical composition, or a peptide or a pharmaceutically acceptable salt of the same content in the pharmaceutical composition, wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO : 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[75] A method for selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer, comprising: providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the karyotype based on the revised IPSS (IPSS-R) of the subject is other than very poor, wherein the pharmaceutical composition comprises a peptide comprising a amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: : 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[76] The method according to subsection

[75] , wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8 ), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), or a pharmaceutically acceptable salt thereof.

[77] The method according to subsection

[75] or

[76] , wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof.

[78] The method according to any of subsections

[75] to

[77] , wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), and a peptide comprising a amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof.

[79] The method according to any of subsections

[75] to

[78] , wherein the pharmaceutical composition comprises a compound represented by formula (1): IVIA / a / ZUZ I U 044 h Tumor antigenic peptide A rOH (1) s I R1where X and Ya represent a single bond, tumor antigenic peptide A represents a peptide consisting of any of the amino acid sequences selected from the following amino acid sequences: RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 7) : 9), the amino group of the N-terminal amino acid of tumor antigenic peptide A is linked to Yade formula (1), the carbonyl group of the C-terminal amino acid of tumor antigenic peptide A is linked to the hydroxy group of formula (1 ), R1 represents a hydrogen atom or a tumor antigenic peptide B, the tumor antigenic peptide B differs in its sequence from the tumor antigenic peptide A and represents a peptide consisting of any amino acid sequence selected from the following amino acid sequences: CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), and the thioether group of the cysteine ​​residue of the tumor antigenic peptide B is linked to the thioether group of formula (1), or a pharmaceutically acceptable salt thereof .

[80] The method according to any of subsections

[75] to

[79] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of RMFPNAPYL (SEQ ID NO: 2), or a pharmaceutically acceptable salt of the same.

[81] The method according to any of subsections

[75] to

[79] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of YMFPNAPYL (SEQ ID NO: 8), or a pharmaceutically acceptable salt of the same.

[82] The method according to any of subsections

[75] to

[79] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of C-CMTWNQMNL (the bond between C and C represents a bond of disulfide, SEQ ID NO: 21), or a pharmaceutically acceptable salt thereof.

[83] The method according to any of subsections

[75] to

[79] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of C-CYTWNQMNL (the bond between C and C represents a disulfide bond, SEQ ID NO: 10), or a pharmaceutically acceptable salt thereof.

[84] The method according to any of subsections

[75] to

[83] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15), or a pharmaceutically acceptable salt of the same.

[85] The method according to any of subsections

[75] to

[83] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt of the same.

[86] The method according to any of subsections

[75] to

[83] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt of the same.

[87] The method in accordance with subsection

[79] , wherein the compound represented by formula (1) is a compound represented by formula (2): CRMFPNAPYL CMTWNQMNL(2) where the bond between C and C represents a disulfide bond, which is the compound or the pharmaceutically acceptable salt thereof according to subsection [1].

[88] The method in accordance with subsection

[79] , wherein the compound represented by formula (1) is a compound represented by formula (3): CRMFPNAPYL I (3) CYTWNQMNL wherein the bond between C and C represents a disulfide bond, which is the compound or the pharmaceutically acceptable salt thereof according to item [1].

[89] The method according to any of subsections

[75] to

[88] , wherein the pharmaceutical composition further comprises a peptide comprising an amino acid sequence selected from the group consisting of CNKRYFKLSHLQMHSRK (SEQ ID NO: 11 ), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a salt pharmaceutically acceptable thereof.

[90] The method according to item

[79] , wherein the compound represented by formula (1) is a compound represented by formula (2): CRMFPNAPYL CMTWNQMNL(2) wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition further comprises WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt thereof .

[91] The method in accordance with subsection

[79] , wherein the compound represented by formula (1) is a compound represented by formula (3): CRMFPNAPYL I (3) CYTWNQMNL wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition further comprises WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt thereof.

[92] The method according to any of subsections

[75] to

[91] , wherein the pharmaceutical composition comprises a pharmaceutically acceptable carrier.

[93] The method in accordance with any of subsections

[75] to

[92] , which also includes: determining the presence or absence of a mutation in the TP53 gene and / or the BCOR gene using a sample taken from the subject; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition in the case of wild-type TP53 and / or wild-type BCOR.

[94] The method according to subsection

[93] , wherein in the case of wild-type TP53, an indication is provided that the subject is a potential subject to benefit from the pharmaceutical composition.

[95] The method in accordance with subsection

[92] or

[93] , wherein in the case of wild-type TP53 and wild-type BCOR, an indication is provided that the subject is a potential subject to benefit from the pharmaceutical composition.

[96] The method in accordance with any of subsections

[75] to

[95] , further comprising: determining the degree of mRNA expression of the WT1 gene using a sample taken from the subject; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the degree of mRNA expression of the WT1 gene is less than a reference value or the reference value or less.

[97] The method in accordance with any of subsections

[75] to

[96] , which also includes: detecting WT1 antigenic peptide-specific CD8 T cells using a sample taken from the subject to whom the pharmaceutical composition or peptide or the pharmaceutically acceptable salt thereof is administered according to any of subsections

[75] to

[92] ; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when WT1 antigenic peptide-specific CD8 T cells have been elevated compared to a sample taken from the subject prior to administration.

[98] The method according to subsection

[97] , wherein the detection of CD8 T cells specific for WT1 antigenic peptide is carried out by reacting a complex of a WT1 peptide and an HLA molecule with the sample, and examining the presence or number of WT1 antigenic peptide-specific CD8 T cells that recognize the complex contained in the sample.

[99] The method according to subsection

[98] , wherein the complex of a WT1 peptide and an HLA molecule is in the form of a tetramer.

[100] The method in accordance with subsection

[98] or

[99] , wherein the HLA molecule is compatible with the HLA of the subject.

[101] The method according to any of subsections

[97] to

[100] , wherein the detection of WT1 antigenic peptide-specific CD8 T cells comprises an analysis by a flow cytometry method.

[102] The method in accordance with any of subsections

[75] to

[101] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when a hypersensitivity reaction is detected late type in the subject to which the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is administered a plurality of times according to any of subsections

[75] to

[92] ,

[103] The method in accordance with subsection

[102] , further comprising comparing the reaction at the site of administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof according to any of the subsections [ 75] to

[92] in the subject, with the reaction at a site without administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof in the subject, and providing an indication that the subject is a potential subject to be benefit from the pharmaceutical composition when the difference between the reaction at the site of administration and the reaction at a site without administration is a reference value or greater.

[104] The method in accordance with any of subsections

[75] to

[103] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the value obtained by dividing the proportion of myeloblasts in a sample taken from the subject to whom the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is administered according to any of subsections

[75] to

[92] in the subject, between the proportion of myeloblasts in a sample taken from the subject before administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof, is less than a reference value or the reference value or less.

[105] The method in accordance with any of subsections

[75] to

[104] , wherein the sample is selected from the group consisting of body fluid, mucous membrane, a cell, a tissue and a cell or tissue culture, and combinations thereof.

[106] The method according to any of subsections

[75] to

[105] , wherein the cancer is selected from the group consisting of leukemia, myelodysplastic syndrome, multiple myeloma, malignant lymphoma, stomach cancer, colorectal cancer, cancer lung, breast cancer, germ cell cancer, liver cancer, skin cancer, urinary bladder cancer, prostate cancer, uterine cancer, cervical cancer, ovarian cancer, and brain tumor.

[107] A method for the treatment of cancer, comprising: selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer by the method according to any of items

[75] to

[106] ; And administer the pharmaceutical composition according to subsections

[75] to

[92] to the selected subject.

[108] A pharmaceutical composition for use in a method of treating cancer, comprising: a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO : 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof, wherein The treatment method includes: selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer by the method according to any of items

[75] to

[107] ; and administering the pharmaceutical composition to the selected subject.

[109] A method of selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer, wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL ( SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14 ), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof; The method includes: provide an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the value obtained by dividing the proportion of myeloblasts in a sample taken from the subject to whom the pharmaceutical composition is administered or the peptide or pharmaceutically acceptable salt thereof Likewise, between the proportion of myeloblasts in a sample taken from the subject before administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof, is less than a reference value or the reference value or less.

[110] The method according to subsection

[109] , wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8 ), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), or a pharmaceutically acceptable salt thereof.

[111] The method according to item

[109] or

[110] , wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof.

[112] The method according to any of items

[109] to

[111] , wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), and a peptide comprising a amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof.

[113] The method in accordance with any of subsections

[109] to

[112] , in IVIA / a / ZUZ I U 044 where the pharmaceutical composition comprises a compound represented by formula (1): O where X and Ya represent a single bond, tumor antigenic peptide A represents a peptide consisting of any of the amino acid sequences selected from the following amino acid sequences: RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 7) : 9), the amino group of the N-terminal amino acid of tumor antigenic peptide A is linked to Yade formula (1), the carbonyl group of the C-terminal amino acid of tumor antigenic peptide A is linked to the hydroxy group of formula (1 ), R1 represents a hydrogen atom or a tumor antigenic peptide B, the tumor antigenic peptide B differs in its sequence from the tumor antigenic peptide A and represents a peptide consisting of any amino acid sequence selected from the following amino acid sequences: CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), and the thioether group of the cysteine ​​residue of the tumor antigenic peptide B is linked to the thioether group of formula (1), or a pharmaceutically acceptable salt thereof .

[114] The method according to any of items

[109] to

[113] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of RMFPNAPYL (SEQ ID NO: 2), or a pharmaceutically acceptable salt of the same.

[115] The method according to any of subsections

[109] to

[113] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of YMFPNAPYL (SEQ ID NO: 8), or a pharmaceutically acceptable salt of the same.

[116] The method according to any of subsections

[109] to

[113] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of C-CMTWNQMNL (the bond between C and C represents a bond of disulfide, SEQ ID NO: 21), or a pharmaceutically acceptable salt thereof.

[117] The method according to any of subsections

[109] to

[113] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of C-CYTWNQMNL (the bond between C and C represents a bond of disulfide, SEQ ID NO: 10), or a pharmaceutically acceptable salt thereof.

[118] The method according to any of subsections

[109] to

[117] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15), or a pharmaceutically acceptable salt of the same.

[119] The method according to any of subsections

[109] to

[117] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt of the same.

[120] The method according to any of subsections

[109] to

[117] , wherein the pharmaceutical composition comprises a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt of the same.

[121] The method in accordance with subsection

[113] , wherein the compound represented by formula (1) is a compound represented by formula (2): CRMFPNAPYL CMTWNQMNL(2) where the bond between C and C represents a disulfide bond, which is the compound or the pharmaceutically acceptable salt thereof according to subsection [1].

[122] The method in accordance with subsection

[113] , wherein the compound represented by formula (1) is a compound represented by formula (3): CRMFPNAPYL | (3) CYTWNQMNL wherein the bond between C and C represents a disulfide bond, which is the compound or the pharmaceutically acceptable salt thereof according to item [1],

[123] The method in accordance with any of the items

[109] to

[122] , wherein the pharmaceutical composition further comprises a peptide comprising an amino acid sequence selected from the group consisting of CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[124] The method in accordance with subsection

[113] , wherein the compound represented by formula (1) is a compound represented by formula (2): CRMFPNAPYL CMTWNQMNL(2) wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition further comprises WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt thereof .

[125] The method in accordance with subsection

[113] , wherein the compound represented by formula (1) is a compound represented by formula (3): CRMFPNAPYL I (3) CYTWNQMNL wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition further comprises WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), or a pharmaceutically acceptable salt thereof.

[126] The method according to any of subsections

[109] to

[125] , wherein the pharmaceutical composition comprises a pharmaceutically acceptable carrier.

[127] The method in accordance with any of subsections

[109] to

[126] , which also includes: determining the presence or absence of a mutation in the TP53 gene and / or the BCOR gene using a sample taken from the subject; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition in the case of wild-type TP53 and / or wild-type BCOR.

[128] The method in accordance with subsection

[127] , wherein in the case of wild-type TP53, an indication is provided that the subject is a potential subject to benefit from the pharmaceutical composition.

[129] The method in accordance with subsection

[127] or

[128] , wherein in the case of wild-type TP53 and wild-type BCOR, an indication is provided that the subject is a potential subject to benefit from the pharmaceutical composition.

[130] The method in accordance with any of subsections

[109] to

[129] , further comprising: determining the degree of mRNA expression of the WT1 gene using a sample taken from the subject; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the degree of WT1 gene mRNA expression is less than a reference value or the reference value or less.

[131] The method in accordance with any of subsections

[109] to

[130] , which also includes: detecting WT1 antigenic peptide-specific CD8 T cells using a sample taken from the subject to whom the pharmaceutical composition or peptide or the pharmaceutically acceptable salt thereof is administered according to any of subsections

[109] to

[126] ; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when WT1 antigen peptide-specific CD8 T cells have been elevated as compared to a sample taken from the subject prior to administration.

[132] The method according to subsection

[131] , wherein the detection of WT1 antigenic peptide-specific CD8 T cells is carried out by reacting a complex of a WT1 peptide and an HLA molecule with the sample, and examining the presence or number of WT1 antigenic peptide-specific CD8 T cells that recognize the complex contained in the sample.

[133] The method according to subsection

[132] , wherein the complex of a WT1 peptide and an HLA molecule is in the form of a tetramer.

[134] The method in accordance with subsection

[132] or

[133] , wherein the HLA molecule is compatible with the HLA of the subject.

[135] The method according to any of subsections

[131] to

[134] , wherein the detection of WT1 antigenic peptide-specific CD8 T cells comprises an analysis by a flow cytometry method.

[136] The method in accordance with any of subsections

[109] to

[135] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when a hypersensitivity reaction is detected late type in the subject to whom the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is administered a plurality of times according to any of subsections

[109] to

[126] .

[137] The method in accordance with subsection

[136] , further comprising comparing the reaction at the site of administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof according to any of the subsections [ 109] to

[126] in the subject, with the reaction at a site without administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof in the subject, and providing an indication that the subject is a potential subject to be benefit from the pharmaceutical composition when the difference between the reaction at the site of administration and the reaction at a site without administration is a reference value or greater.

[138] The method in accordance with any of subsections

[109] to

[137] , further comprising providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when karyotyping based on the IPSS revised (IPSS-R) of the subject is different from very bad.

[139] The method in accordance with any of subsections

[109] to

[138] , wherein the sample is selected from the group consisting of body fluid, mucous membrane, a cell, a tissue and a cell or tissue culture, and combinations thereof.

[140] The method in accordance with any of subsections

[109] to

[139] , wherein the cancer is selected from the group consisting of leukemia, myelodysplastic syndrome, multiple myeloma, malignant lymphoma, stomach cancer, colorectal cancer, cancer lung cancer, breast cancer, germ cell cancer, liver cancer, skin cancer, urinary bladder cancer, prostate cancer, uterine cancer, cervical cancer, ovarian cancer and brain tumor.

[141] A method for the treatment of cancer, comprising: selecting a potential subject who benefits from a pharmaceutical composition for treating or preventing cancer by the method according to any of subsections

[109] to

[140] ; and administering the pharmaceutical composition according to subsections

[109] to

[126] to the selected subject.

[142] A pharmaceutical composition for use in a method of treating cancer, comprising: a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: : 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof, wherein The treatment method includes: selecting a potential subject who benefits from a pharmaceutical composition for treating or preventing cancer by the method according to any of subsections

[109] to

[140] ; and administering the pharmaceutical composition to the selected subject.

[143] A method for the treatment of cancer, comprising: determining the presence or absence of a mutation in the TP53 gene and / or the BCOR gene using a sample taken from a subject; and administering an effective amount of a pharmaceutical composition to treat or prevent cancer to a subject having wild-type TP53 and / or wild-type BCOR, wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group that consists of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13) , WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[144] A method for the treatment of cancer, comprising: determining the degree of mRNA expression of the WT1 gene using a sample taken from a subject; and administering an effective amount of a pharmaceutical composition to treat or prevent cancer to a subject in which the degree of mRNA expression of the WT1 gene is less than a reference value or the reference value or less, wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6) , RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[145] A method for the treatment of cancer, comprising: administering an effective amount of a pharmaceutical composition to treat or prevent cancer to a subject, when the karyotype based on the revised IPSS (IPSS-R) of a subject is other than very poor, wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NOT: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO : 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

[146] A method of treating cancer, comprising administering an effective amount of a pharmaceutical composition to treat or prevent cancer to a subject, when the value obtained by dividing the proportion of myeloblasts in a sample taken from the subject to whom it is administered the pharmaceutical composition, comprising a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11) , CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutical salt acceptable thereof, or the peptide or the pharmaceutically acceptable salt thereof, between the proportion of myeloblasts in a sample taken from the subject before administration of the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof, is less than a value reference or reference value or less. Advantageous effects of the invention According to the present invention there is provided a method for selecting a potential subject who will benefit from a pharmaceutical composition for treating or preventing cancer. Here, the pharmaceutical composition comprises a WT1 killer peptide and / or a WT1 helper peptide, or a pharmaceutically acceptable salt thereof. By selecting a potential subject to benefit from each pharmaceutical composition, effective treatment or prevention of cancer can be performed using the pharmaceutical composition. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 shows the test results of a WT1 peptide cocktail vaccine and the comparison results with a control (BSC) in the ONTIME trial of rigosertib. Figure 2 shows the survival curves of wild-type TP53 and wild-type BCOR and mutant TP53 or mutant BCOR. Figure 3 shows the results of the comparison of survival curves, based on the positivity or negativity of the antigenic peptide-specific immune response. WT1 for wild-type TP53 and wild-type BCOR, and mutant TP53 or mutant BCOR. Figure 4 shows the results of the comparison of survival curves according to the degree of WT1 mRNA expression of Example 5 (results (1)). Figure 5 shows the results of the comparison of survival curves, based on the positivity or negativity of the WT1 antigenic peptide-specific immune response for the degree of WT1 mRNA expression (results (1)). Figure 6 shows the results of the comparison of survival curves according to the degree of WT1 mRNA expression of Example 5 (results (2)). Figure 7 shows the results of the comparison of survival curves, based on the positivity or negativity of the WT1 antigenic peptide-specific immune response for the degree of WT1 mRNA expression (results (2)). Figure 8 shows the results of an HLA tetramer assay analysis and the results of a bidirectional analysis of the determination of a DTH assay using a WT1 killer peptide conjugate. Figure 9 shows the results of the comparison of survival curves for the positivity or negativity of the WT1 antigenic peptide-specific immune response and the stabilization of myeloblasts. Figure 10 shows the results of the comparison of transition periods to acute myeloid leukemia (AML), based on the positivity or negativity of the WT1 antigenic peptide-specific immune response. Figure 11 shows the results of the comparison of survival curves, based on the positivity or negativity of the WT1 antigenic peptide-specific immune response. Figure 12 shows the results of the comparison of survival curves, based on the positivity or negativity of the WT1 antigenic peptide-specific immune response for the IPSS-R karyotype. Figure 13 shows the results of the comparison of the median survival time of each sex difference with historical data and the median survival time of BSC from a rigosertib trial. Figure 14 shows the results of the comparison of the survival curves, based on the degree of expression of WT1 mRNA from Example 11. Figure 15 shows the results of the comparison of survival curves, based on the positivity or negativity of the WT1 antigen peptide-specific immune response to the degree of WT1 mRNA expression. Figure 16 shows the relationship between the degree of expression of WT1 mRNA in peripheral blood and the degree of expression of WT1 mRNA in bone marrow fluid. DESCRIPTION OF THE MODALITIES OF THE INVENTION The embodiments of the present invention will be described in detail below. In the present specification, the amino acid residue means a portion corresponding to a unit of an amino acid constituting a peptide or a protein in a peptide or protein molecule. Examples of the amino acid residue include natural or unnatural o-amino acid residues, β-amino acid residues, γ-amino acid residues and δ-amino acid residues. Specifically, examples thereof include natural o-amino acid residues, ornithine residue, homoserine residue, homocysteine ​​residue, β-alanine, γ-aminobutanoic acid and δ-aminopentanoic acid. When the amino acid residue is an optically active form, the L-form is preferred, although either the L-form or the D-form is acceptable. In the present specification, the amino acid residue may be indicated by an abbreviation which is described in the following abbreviations. Ala or A: alanine residue Arg or R: arginine residue Asn or N: asparagine residue Asp or D: aspartic acid residue Cys or C: cysteine ​​residue Gln or Q: glutamine residue Glu or E: glutamic acid residue Gly or G: glycine residue His or H: Histidine residue Lie or I: Isoleucine residue Leu or L: Leucine residue Lys or K: Lysine residue Met or M: Methionine residue Phe or F: Phenylalanine residue Pro or P: Proline residue Ser o S: serine residue Thr o T: threonine residue Trp o W: tryptophan residue Tyr o Y: tyrosine residue Val or V: valine residue Abu: 2-aminobutyric acid residue (also called o-aminobutyric residue) Orn: ornithine residue Cit: citrulline residue In the present specification, the amino acid sequence of the peptide is described in such a way that the amino acid residue of the N-terminal amino acid is placed on the left side and the amino acid residue of the C-terminal amino acid is placed on the right side, so according to the conventional method. In the peptide, the amino group of the amino acid residue of the N-terminal amino acid is attached to a hydrogen atom, and the carbonyl group of the amino acid residue of the C-terminal amino acid is attached to a hydroxy group, unless otherwise specified. another way. The divalent group of the peptide means a group that is linked through the amino group of the amino acid residue of the N-terminal amino acid and the carbonyl group of the amino acid residue of the C-terminal amino acid. In the present specification, for example in a compound represented by formula (2) and (3), the amino group of the amino acid residue of the N-terminal amino acid is also attached to a hydrogen atom, and the carbonyl group of the residue of The C-terminal amino acid is also attached to a hydroxy group, for a peptide corresponding to its partial structure, unless otherwise specified. In the present specification, R1 represents a hydrogen atom or a tumor antigenic peptide B and is preferably tumor antigenic peptide B. As for the compound of formula (1) where R1 is a hydrogen atom, its sequence is not completely the same. same as the partial sequence of the WT1 protein. Specifically, the compound of formula (1) wherein R1 is a hydrogen atom is one in which a cysteine ​​residue is added to the N-terminal side of the tumor antigenic peptide A, and therefore is not a partial peptide consisting of amino acids. from 8 to 35 consecutive residues in the human WT1 amino acid sequence described in SEQ ID NO: 1. Examples of the compound of formula (1) where R1 is a hydrogen atom include the following amino acid sequences: CRMFPNAPYL (SEQ ID NO: 40), CCMTWNQMNL (SEQ ID NO: 41), CCYTWNQMNL (SEQ ID NO: 42), CALLPAVPSL (SEQ ID NO: 43), CSLGEQQYSV (SEQ ID NO: 44) and CRVPGVAPTL (SEQ ID NO: 45). In the present specification, X and Ya independently represent a single bond or a bivalent group of a peptide consisting of amino acids of 1 to 4 residues. The sum of the number of amino acid residues of X and the number of amino acid residues of Ya is an integer from 0 to 4. For example, the sum is an integer of 0 means that Examples of the case where the sum is an integer of 4 include the case where Xa is independently a divalent group of a peptide consisting of amino acids of 2 residues, the case where Xa is a divalent group of a peptide consisting of amino acids of 3 residues and Ya is a divalent group of a peptide consisting of the 1-residue amino acid, and the case where Xa is a divalent group of a peptide consisting of 4-residue amino acids and Ya is a single bond. Preferably, the integer of the sum is from 0 to 2, preferably from 0 to 1, most preferably 0. Specifically, the case where both Xa and Ya are a single bond is highly preferred. Examples of the case where the integer of the sum is 2 include the case where Xa is a divalent group of a peptide consisting of 2-residue amino acids and Ya is a single bond, the case where X and Ya are independently a divalent group of a polypeptide which consists of a 1-residue amino acid, and the case where Xa is a single bond and Ya is a divalent group of a peptide consisting of 2-residue amino acids. Examples of the case where the integer of the sum is 1 include the case where Xa is a divalent group of a peptide consisting of a 1-residue amino acid and Ya is a single bond, and the case where Xa is a single bond and Ya is a divalent group of a peptide consisting of a 1-residue amino acid. Among them, the case where Xa is a single bond and Ya is an alanine residue, a leucine residue or a methionine residue is preferred. In the present embodiment, the pharmaceutical composition comprises a particular WT1 killer peptide and / or WT1 helper peptide, or a pharmaceutically acceptable salt thereof, that is, a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL ( SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9 ), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof. The pharmaceutical composition according to the present embodiment is not exempt from containing a peptide or pharmaceutically acceptable salt thereof different from those described above, and the pharmaceutical composition may also contain a peptide different from those described above, for example, another peptide. WT1 killer and / or WT1 helper peptide. In the present specification, the WT1 peptide is a peptide comprising a portion consisting of consecutive amino acids present in the human WT1 amino acid sequence described in SEQ ID NO: 1. WT1 killer peptide means a WT1 peptide restricted to MHC class I. In the present specification, restricted to MHC class I means the property of inducing CTL by binding to an MHC class I molecule, which is class I of the major histocompatibility complex (MHC). The MHC class I-restricted WT1 peptide is a peptide that is presented as a complex upon binding to the MHC class I antigen in vitro and / or in vivo, and means a peptide that induces CTL as a result of the complex being recognized. by precursor T cells. The MHC is referred to as human leukocyte antigen (HLA) for humans. HLA corresponding to the MHC class I molecule is classified into subtypes such as HLA-A, B, Cw, F and G. Examples of restricted to MHC class I include, preferably, restricted to HLA-A, restricted to HLA-B and restricted to HLA-Cw. Regarding HLA subtypes, polymorphisms (alleles) are known. Examples of HLA-A polymorphism include TI or more, such as HLA-A1, HLA-A2 (A0201, A0206, etc.) and HLAA24; examples of HLA-B polymorphism include 59 or more, such as HLA-B7, HLA-B40 and HLAB4403; and examples of HLA-Cw polymorphism include 10 or more, such as HLA-Cw0301, HLACw0401 and HLA-Cw0602. Among these polymorphisms, HLA-A2 or HLA-A24 is preferred. The MHC class I-restricted WT1 peptide (WT1 killer peptide) is also referred to as the MHC class I-restricted WT1 epitope. In the present specification, the MHC class Γ-restricted WT1 epitope means the peptide itself that is binds to an MHC class I antigen and is presented as a complex. Specifically, the MHC class I-restricted WT1 peptide produces an MHC class I-restricted WT1 epitope through the intracellular degradation of a proteasome conjugate, such as gamma interferon-inducible lysosomal thiol reductase (GILT, GLT). ) and / or protease (proteolysis, reductive cleavage of a disulfide bond), and / or cleavage at the optimal number of residues by endoplasmic reticulum aminopeptidase 1 (ERAP1, ERaminopeptidase 1) in vitro and / or in vivo. In production, there is a possible main production process in which, first, the C-terminal amino acid of the MHC class I-restricted WT1 epitope arises as a result of degradation by proteasome and / or protease, and then the amino acid N-terminal of the MHC class I-restricted WT1 epitope arises as a result of cleavage by ERAP1. However, the production process may go through a different process than the production process. ERAP1 is now called ERAAP (ER antigen presentation-associated aminopeptidase) and was previously called A-LAP, PILS-AP or ARTS-1. Thus, as the MHC class I-restricted WT1 peptide, a peptide consisting of the amino acids produced by adding an amino acid to the carbonyl group of the C-terminal amino acid of an MHC class I-restricted WT1 epitope is preferable. The length of the WT1 killer peptide is not particularly limited, as long as it functions as a WT1 killer peptide and, for example, one consisting of amino acids of 7 to 30 residues, 7 to 15 residues, 8 to 12 residues, 8 to 11 residues, 8 residues, or 9 residues, or a conjugate thereof. The WT1 killer peptide may consist of amino acids of 7 residues or more or 8 residues or more, or a conjugate thereof, and may consist of amino acids of 30 residues or less, 25 residues or less, 22 residues or less, 20 residues or less, 18 residues or less, 15 residues or less, 12 residues or less, 11 residues or less, 10 residues or less or 9 residues or less, or a conjugate thereof. Examples of the WT1 killer peptide include peptides comprising the amino acid sequences described in RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6 ), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), and peptides comprising an altered amino acid sequence containing a amino acid residue variation in any amino acid sequence selected from SEQ ID NOs: 1 to 9 and having CTL-inducing activity. The pharmaceutical composition according to the present embodiment may comprise, for example, a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4) or a pharmaceutically acceptable salt thereof. Also, the pharmaceutical composition according to the present embodiment may comprise, for example, a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), which corresponds to the HLA A2 subtype (A-0201, A0206, etc. .), or a pharmaceutically acceptable salt thereof, or may comprise, for example, a peptide comprising an amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), corresponding to the HLA subtype A24 (A-2402, etc.), or a pharmaceutically acceptable salt thereof. Furthermore, the pharmaceutical composition according to the present embodiment may comprise, for example, a peptide consisting of the amino acid sequence of RMFPNAPYL (SEQ ID NO: 2) or a pharmaceutically acceptable salt thereof; may comprise a peptide consisting of the amino acid sequence of YMFPNAPYL (SEQ ID NO: 8) or a pharmaceutically acceptable salt thereof; may comprise a peptide consisting of the amino acid sequence of C-CYTWNQMNL (the bond between C and C represents a disulfide bond, SEQ ID NO: 10) or a pharmaceutically acceptable salt thereof; or may comprise a peptide consisting of the amino acid sequence of C-CMTWNQMNL (the bond between C and C represents a disulfide bond, SEQ ID NO: 21) or a pharmaceutically acceptable salt thereof. In the present specification, the peptide comprising an amino acid sequence encompasses a peptide consisting of the amino acid sequence and a peptide in which an additional amino acid is added at the N-terminal amino acid and / or C-terminal amino acid of the sequence. of amino acids. In case the MHC class I restricted WT1 peptide is added, a peptide having the addition on the C-terminal side is preferable. In case the MHC class I restricted epitope of WT1 is added, the addition on the C-terminal side is preferable. The peptide comprising an altered amino acid sequence containing an amino acid residue variation in the amino acid sequence and having CTL-inducing activity according to the present invention is also called an altered killer peptide. The altered killer peptide means a peptide that consists of an amino acid sequence in which 1 to 3 amino acids are deleted, substituted and / or added in the amino acid sequence, and induces CTL by binding to MHC class I. Examples of the Substitution position of the amino acid to be replaced include, in the case of a peptide consisting of 9-residue amino acids, position 1 (N-terminus), position 2, position 3, and position 9. The number of amino acids to be added (also included insert) is preferably 1 or 2, most preferably 1. A preferred addition position is the C terminus. The number of amino acids to be deleted is preferably 1. For variation, the amino acid to be added or the amino acid to be substituted may be an unnatural amino acid different from the 20 types of amino acids encoded by a gene. It is known that for each HLA subtype polymorphism there is regularity (binding motif) of the amino acid sequence of a peptide that can bind to an HLA antigen. For example, regarding the HLA-A24 binding motif, it is known that in a peptide consisting of amino acids of 8 to 11 residues, the amino acid at position 2 is Tyr, Phe, Met or Trp, and the amino acid at C end is Phe, Leu, lie, Trp or Met (J. Immunol., 152, p. 3913, 1994; J. ImmunoL, 155, p. 4307, 1994; and Immunogenetics, 41, p. 178, 1995). Therefore, for example, in the case of a peptide consisting of 9-residue amino acids, it is possible that position 2 is replaced by Tyr, Phe, Met or Trp and / or position 9 is replaced by Phe, Leu, Lie. , Trp or Met, and as the altered killer peptide a peptide that has undergone the substitution is preferable. Likewise, regarding the binding motif of HLA-A*02:01, it is known that in a peptide consisting of amino acids of 8 to 11 residues, the amino acid at position 2 is Leu or Met and the amino acid at the C terminus It is Val or leu. Therefore, for example, in the case of a peptide consisting of 9-residue amino acids, it is possible that position 2 is replaced by Leu or Met and / or position 9 is replaced by Val or Leu, and as a killer peptide altered, a peptide that has undergone the substitution is preferable. Examples of the altered killer peptide include the following peptides: RYFPNAPYL (SEQ ID NO: 22) (see International Publication No. WO 03 / 106682); FMFPNAPYL (SEQ ID NO: 23), RLFPNAPYL (SEQ ID NO: 24), RMMPNAPYL (SEQ ID NO: 25), RMFPNAPYV (SEQ ID NO: 26) and YMFPNAPYL (SEQ ID NO: 7) (see International Publication No. WO 2009 / 072610) which are altered killer peptides of RMFPNAPYL (SEQ ID NO: 2); CYTWNQMNL (SEQ ID NO: 4) (see International Publication No. WO 02 / 79253) which is an altered killer peptide of CMTWNQMNL (SEQ ID NO: 3); Xaa-Met-Thr-Trp-Asn-GIn-Met-Asn-Leu (SEQ ID NO: 27) (in this sequence, Xaa represents Ser or Ala) and Xaa-Tyr-Thr-Trp-Asn-GIn-Met-Asn-Leu (SEQ ID NO: 28) (in this sequence, ) (see international publication No. WO 2004 / 026897); AYLPAVPSL (SEQ ID NO: 29) (see International Publication No. WO 2003 / 106682) which is an altered killer peptide of ALLPAVPSL (SEQ ID NO: 5); FLGEQQYSV (SEQ ID NO: 30), SMGEQQYSV (SEQ ID NO: 31) and SLMEQQYSV (SEQ ID NO: 32) (see International Publication No. WO 2009 / 072610) which are altered killer peptides of SLGEQQYSV (SEQ ID NO: 6); and RYPGVAPTL (SEQ ID NO: 33) (see International Publication No. WO 2003 / 106682) which is an altered killer peptide of RVPGVAPTL (SEQ ID NO: 7). From the point of view of broadly covering HLA subtypes, it is preferable that the pharmaceutical composition according to the present embodiment comprises a plurality of peptides corresponding to different HLA subtypes, respectively. For example, it is preferable to comprise both the peptide corresponding to the HLA A2 subtype, or a pharmaceutically acceptable salt thereof, and the peptide corresponding to the HLA A24 subtype, or a pharmaceutically acceptable salt thereof. In this case, for example, the pharmaceutical composition may comprise a compound represented by formula (1): EITHER H || ---------------------hL X X Tumor antigenic peptide AHOH x8Y>al-------- (η Yo R1where X and Ya represent a single bond, tumor antigenic peptide A represents a peptide consisting of any amino acid sequence selected from the following amino acid sequences: RMFPNAPYL (SEQ ID NO: 2), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), YMFPNAPYL (SEQ ID NO: 8) and VLDFAPPGA (SEQ ID NO: 8) : 9), the amino group of the N-terminal amino acid of tumor antigenic peptide A is linked to Yade formula (1), the carbonyl group of the C-terminal amino acid of tumor antigenic peptide A is linked to the hydroxy group of formula (1 ), R1 represents a hydrogen atom or a tumor antigenic peptide B, the tumor antigenic peptide B differs in its sequence from the tumor antigenic peptide A and represents a peptide consisting of any amino acid sequence selected from the following amino acid sequences: CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), and the thioether group of the cysteine ​​residue of the tumor antigenic peptide B is linked to the thioether group of the formula (1), or a pharmaceutically acceptable salt thereof . The compound represented by the formula (1) above is excellent in stability against an oxidizing agent or the like in a solution and has a certain quality as a drug raw material because, for example, the cysteine ​​residue forms a disulfide bond. In case the pharmaceutical composition according to the present embodiment comprises a compound represented by formula (1) above (conjugate of a WT1 killer peptide) (except for the case where R1 is a hydrogen atom), the conjugate is degraded in the body by the reductive cleavage of the disulfide bond between the N-terminal cysteine ​​residues by ERAP1, to produce two types of epitopes corresponding to different HLA subtypes. As in the conjugate represented by formula (1), a conjugate from which a plurality of epitope types corresponding to different HLA subtypes are produced is capable of widely dealing with different HLA subtypes among subjects, and a conjugate can cover a large population and therefore can efficiently induce CTL in subjects (see International Publication No. WO 2014 / 157692). The tumor antigenic peptide A according to the present embodiment is an MHC class I restricted WT1 peptide consisting of amino acids of 7 to 30 residues. In formula (1), the amino group of the N-terminal amino acid of peptide A of tumor antigen is linked to Yade formula (1), and the carbonyl group of the C-terminal amino acid of peptide A of tumor antigen is linked to the group hydroxy of formula (1). The compound represented by formula (1) above may be a compound represented by formula (2): CRMFPNAPYL CMTWNQMN.(2)where the bond between C and C represents a disulfide bond, or may be a compound represented by formula (3): CRMFPNAPYL l (3) CYTWNQMNL where the bond between C and C represents a disulfide bond. The compound represented by formula (1) above may be a compound represented by formula (2): CRMFPNAPYL CMTWNQMN.(2) wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition may further comprise WAPVLDFAPPGASAYGSL (SEQ ID NO: 14) or a pharmaceutically acceptable salt thereof , or the compound represented by formula (1) may be a compound represented by formula (3): CRMFPNAPYL I (3) CYTWNQMNL wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof, and the pharmaceutical composition may further comprise WAPVLDFAPPGASAYGSL (SEQ ID NO: 14) or a pharmaceutically acceptable salt thereof. The pharmaceutical composition according to the present embodiment may further comprise a WT1 auxiliary peptide. The pharmaceutical composition according to the present embodiment, when it comprises a peptide comprising an amino acid sequence selected from the group consisting of CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), may also comprise a peptide comprising a different amino acid sequence selected from the group and / or a peptide additional WT1 auxiliary different from them. WT1 helper peptide means a WT1 peptide restricted to MHC class II. In the present specification, MHC class II restricted means the property of inducing helper T cells by binding to an MHC class II molecule. HLA corresponding to the MHC class II molecule is classified into subtypes, such as HLA-DR, DQ and DP. Examples of class Π MHC restricted include preferably HLA-DR restricted, HLA-DQ restricted, and HLA-DP restricted. In the present specification, MHC class Π-restricted WT1 peptide means a peptide that induces T helper cells by binding to an MHC class II antigen in vitro and / or in vivo. The length of the WT1 helper peptide is not particularly limited, as long as it functions as a WT1 helper peptide, and, for example, one consisting of amino acids of 7 to 30 residues or 14 to 30 residues is acceptable. The WT1 helper peptide may consist of amino acids of 7 residues or more, 8 residues or more, 10 residues or more, 12 residues or more, or 14 residues or more, and may consist of amino acids of 30 residues or less, 25 residues or less , 22 residues or less or 20 residues or less. Examples of the WT1 auxiliary peptide include peptides comprising the amino acid sequences described in CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14 ), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15), WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), SGQAYMFPNAPYLPSCLES (SEQ ID NO: 17) (see International Publication No. WO 2007 / 120673), RSDELVRHHNMHQRNMTKL (SEQ ID NO: 18) ( see International Publication No. WO 2007 / 120673), PGCNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 19) (see International Publication No. WO 2007 / 120673) and KRYFKLSHLQMHSRKH (SEQ ID NO: 20) (see International Publication No. WO 2005 / 045027), and peptides comprising an altered amino acid sequence containing an amino acid residue variation in any amino acid sequence selected from the group consisting of SEQ ID NOs: 11 to 20, and having T helper cell inducing activity. The pharmaceutical composition according to the present embodiment may comprise, for example, a peptide comprising an amino acid sequence selected from the group consisting of CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof. Also, the pharmaceutical composition according to the present embodiment may comprise, for example, a peptide consisting of the amino acid sequence of CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) or a pharmaceutically acceptable salt thereof; may comprise a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16) or a pharmaceutically acceptable salt thereof; or may comprise a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSL (SEQ ID NO: 14) or a pharmaceutically acceptable salt thereof. The peptide comprising an amino acid sequence means, as mentioned above, a peptide consisting of the amino acid sequence and a peptide in which an additional amino acid is added at the N-terminal amino acid and / or C-terminal amino acid of the amino acid sequence. The WT1 helper peptide may contain 1 or 2 or more cysteine ​​residues in the amino acid sequence. The cysteine ​​residue, when added to the amino acid sequence, can be added to the N-terminal side and / or the C-terminal side of the amino acid sequence. In the present specification, the peptide comprising an altered amino acid sequence that contains an amino acid residue variation in the amino acid sequence and has T helper cell inducing activity is also called altered helper peptide. The altered helper peptide means a peptide that consists of an amino acid sequence in which 1 to 3 amino acids are deleted, substituted and / or added in the amino acid sequence, and induces helper T cells by binding to MHC class II. The number of amino acids to be added (insert is also included) is preferably 1 to 3. The number of amino acids to be deleted is preferably 1 to 5. For variation, the amino acid to be added or the amino acid to be substituted may be a non-natural amino acid different from the 20 types of amino acids encoded by a gene. Examples of the altered auxiliary peptide include the following peptides: SGQAYMFPNAPYLPSCLES (SEQ ID NO: 35) (see patent document 6), SGQARMFPNAPYLPSC (SEQ ID NO: 36) and SGQAYMFPNAPYLPSC (SEQ ID NO: 37) which are altered auxiliary peptides of SGQARMFPNAPYLPSCLES (SEQ ID NO: 34); and pgcnkryfklshlqmhsrk (seq id no: 38), pgnkryfklshlqmhsrkh (seq id no: 39), cnkryfklshlqmhsrk (seq id no: 11), cnkryfklshlqmhsrkh (seq id no: 12) LQMHSRKHTG (SEQ ID NO: 13) that are altered auxiliary peptides from PGCNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 19). The peptide or compound according to the present embodiment may be produced according to a method described in the examples section of the present specification, or a method that is used in usual peptide synthesis. Examples of the production method include the methods described in the literature (Peptide Synthesis, Wiley-Interscience, New York, 1966; The Proteins, Vol. 2, Academic Press Inc., New York, 1976; Peptide Synthesis, Maruzen Publishing Co., Ltd., 1975; Basics and Experiments of Peptide Synthesis, Maruzen Publishing Co., Ltd., 1985; and Development of Medicaments, 2, Vol. 14, Peptide Synthesis, Hirokawa-Shoten Ltd., 1991). For example, for a method of producing a compound represented by formula (1), see also International Publication No. WO 2014 / 157692. Examples thereof include a production method in a solid phase synthesizer using an Fmoc method or a Boc method, and a production method by sequential condensation of Boc-amino acids or Z-amino acids using a liquid phase synthesis method (Fmoc represents a 9-fluorenylmethoxycarbonyl group, Boc represents a t-butoxycarbonyl group and Z represents a benzyloxycarbonyl group). In the intermediate for producing the peptide or compound according to the present embodiment, a functional group such as an amino group, a carboxy group or a mercapto group can be protected with a suitable protecting group and then deprotected if necessary, using techniques of protection and unprotection. Suitable protecting groups, protection methods and deprotection methods are described in detail in Protective Groups in Organic Synthesis 2nd edition (John Wiley & Sons, Inc.; 1990), etc. Examples of the protecting group for the mercapto group include an acetamidomethyl group and a triphyl group. In case the peptide or compound according to the present embodiment has a disulfide bond, the disulfide bond may be formed between two different peptides containing cysteine ​​residues, or between a peptide containing a cysteine ​​residue and cysteine, of according to a method that is used in usual peptide chemistry. Examples of the method of forming a disulfide bond include the methods described in the literature (Peptide Synthesis, Wiley-Interscience, New York, 1966; The Proteins, Vol 2, Academic Press Inc., New York, 1976; Peptide Synthesis, Maruzen Publishing Co. ., Ltd., 1975; Basics and Experiments of Peptide Synthesis, Maruzen Publishing Co., Ltd., 1985; and Development of Medicaments, 2, Vol. 14, Peptide Synthesis, Hirokawa-Shoten Ltd., 1991). Specifically, in case a cysteine ​​residue is contained in a peptide, a compound having a disulfide bond (disulfide compound) can be produced by removing all protecting groups, including a protecting group for a mercapto group on a side chain. of cysteine, followed by oxidation in an inert solvent. It can also be produced by mixing and oxidizing in a suitable solvent two intermediates having mercapto groups. As the oxidation method, a method for forming a disulfide bond known in usual peptide synthesis can be conveniently selected. Examples thereof include oxidation of iodine, an oxidation reaction method in air under alkaline conditions, and a method of forming a disulfide bond by adding an oxidizing agent under alkaline or acidic conditions. Here, examples of the oxidizing agent include iodine, dimethyl sulfoxide (DMSO), and potassium ferricyanide. For example, water, acetic acid, methanol, chloroform, DMF or DMSO, or a combined solution thereof, can be used as a solvent. The oxidation reaction often gives a mixture of symmetrical or asymmetrical disulfide compounds. The asymmetric disulfide compound of interest can be obtained by purification by various types of chromatography or recrystallization. Alternatively, a selective disulfide bond can be formed by mixing an intermediate having an activated mercapto group with an intermediate having a mercapto group. Examples of the intermediate having an activated mercapto group include a mercapto group linked to an Npys group (3-nitro-2-pyridinesulfenyl group). Alternatively, a selective disulfide bond can be formed by pre-mixing one of the intermediates, for example, with 2,2'-dithiob¡s(5-nítrop¡ridina), thus activating the mercapto group, and then adding the another intermediary (Tetrahedron Letters, Vol. 37. No. 9, p. 1347-1350). In case two or more cysteine ​​residues are also contained in a peptide, methods similar to those described above can be used. In this case, isomers are obtained that differ in the pattern of disulfide bonds. By means of a particular combination of protecting groups on the cysteine ​​side chains, a dimer can be obtained that has a disulfide bond formed between the cysteine ​​residues of interest. Examples of the combination of protecting groups include a MeBzl (methylbenzyl) group and an Acm (acetamidomethyl) group; a Trt (trityl) group and an Acm group; an Npys (3-nitro-2-pyridylthio) group and an Acm group; and an SBu-t (S-tert-butyl) group and an Acm group. For example, in the case of the combination of a MeBzl group and an Acm group, examples thereof include a method where the MeBzl group and other protecting groups other than those on the cysteine ​​side chains are first removed, then a solution containing the peptide monomer is subjected to an oxidation reaction in air to form a disulfide bond between the unprotected cysteine ​​residues, and subsequently, deprotection and oxidation with iodine are performed to form a disulfide bond between the protected cysteine ​​residues. the Ac group. The peptide or compound obtained according to the present embodiment can be purified according to methods known to those skilled in the art or a method used in conventional peptide chemistry. It can be purified, for example, by means of various types of chromatography (e.g., silica gel column chromatography, ion exchange column chromatography, gel filtration or reverse phase chromatography) or recrystallization. For example, as a recrystallization solvent you can use an alcohol solvent such as methanol, ethanol or 2-propanol, an ether solvent such as diethyl ether, an ester solvent such as ethyl acetate, an aromatic hydrocarbon solvent such as benzene or toluene, a of ketone such as acetone, a hydrocarbon solvent such as hexane, an aprotic solvent such as dimethylformamide or acetonitrile, water, or a combined solvent thereof. As other purification methods, the methods described in Experimental Chemistry (edited by The Chemical Society of Japan, Maruzen Publishing Co., Ltd.), Vol. 1, etc. can be used. Methods of purification of a disulfide compound are described in the literature (Peptide Synthesis, Wiley-Interscience, New York, 1966; The Proteins, Vol 2, Academic Press Inc., New York, 1976; Peptide Synthesis, Maruzen Publishing Co. , Ltd., 1975; Basics and Experiments of Peptide Synthesis, Maruzen Publishing Co., Ltd., 1985; and Development of Medicaments, 2, Vol. 14, Peptide Synthesis, Hirokawa-Shoten Ltd., 1991), etc. Among others, HPLC is preferred. In case there are one or more chiral centers in the compound according to the present embodiment, it can be produced according to a usual method using raw materials (amino acids) having the chiral centers. To increase the optical purity of the compound according to the present embodiment, optical resolution or the like can be performed at an appropriate stage of a production step. The optical resolution method can be carried out, for example, by the diastereomer method wherein the compound according to the present embodiment or its intermediate forms a salt with an optically active acid (e.g., monocarboxylic acid, such as acid mandelic, N-benzyloxyalanine or lactic acid, dicarboxylic acid such as tartaric acid, o-diisopropylidentartaric acid or melic acid, or sulfonic acid such as camphorsulfonic acid or bromocamphorsulfonic acid) in an inert solvent (e.g., an alcohol solvent such as methanol, ethanol or 2-propanol, an ether solvent such as diethyl ether, an ester solvent such as ethyl acetate, a hydrocarbon solvent such as toluene, or an aprotic solvent such as acetonitrile, and combined solvents thereof). In case the compound or intermediate according to the present embodiment has an acidic functional group, such as a carboxy group, optical resolution can also be carried out by forming a salt with an optically active amine (e.g., organic amine such as a-phenethylamine, quinine, quinidine, cinchonidine, cinchonine and strychnine). The temperature at which the salt is formed is selected from the range of room temperature to the boiling point of the solvent. To improve optical purity it is advisable to temporarily raise the temperature to close to the boiling point of the solvent. By collecting the deposited salt by filtration the performance can be improved, if necessary, by cooling. The amount used of the optically pure acid or amine is conveniently in the range of about 0.5 to about 2.0 equivalents, preferably in the range of about 1 equivalent, relative to the substrate. If necessary, an optically active salt with high purity can also be obtained by recrystallization of crystals in an inert solvent (e.g., an alcohol solvent such as methanol, ethanol or 2-propanol, an ether solvent such as diethyl ether. an ester solvent such as ethyl acetate, a hydrocarbon solvent such as toluene, or an aprotic solvent such as acetonitrile, and combined solvents thereof). If necessary, the free form can also be obtained by treating an optically resolved salt with an acid or a base by a conventional method. In the present specification, examples of the pharmaceutically acceptable salt include acid addition salts and base addition salts. Examples of the acid addition salt include salts of inorganic acids, such as hydrochloride, hydrobromide, sulfate, hydroiodide, nitrate and phosphate, and salts of organic acids, such as citrate, oxalate, acetate, formate, propionate, benzoate, trifluoroacetate, maleate, tartrate, methanesulfonate, benzenesulfonate and ptoluenesulfonate. Examples of the base addition salt include salts of organic bases, such as sodium salt, potassium salt, calcium salt, magnesium salt and ammonium salt, and salts of organic bases, such as triethylammonium salt, triethylammonium salt. triethanolammonium, pyridinium salt and diisopropylammonium salt. Additional examples thereof include salts of basic or acidic amino acids such as arginine, aspartic acid and glutamic acid. Also included in the present embodiment are the hydrates and solvates of the peptide or compound according to the present embodiment or the pharmaceutically acceptable salt thereof, such as an ethanol solvate. Furthermore, the pharmaceutical composition according to the present embodiment also encompasses every possible stereoisomer, such as every diastereomer and enantiomer and every crystal form of the compound represented by formula (1). The pharmaceutical composition according to the present embodiment can be used in the treatment or prevention of a cancer that expresses the WT1 gene or cancer accompanied by elevation of the expression of the WT1 gene (WT1-related cancer). Examples of these cancers include leukemia, myelodysplastic syndrome, multiple myeloma, malignant lymphoma, stomach cancer, colorectal cancer, lung cancer, breast cancer, germ cell cancer, liver cancer, skin cancer, urinary bladder cancer, prostate cancer , uterine cancer, cervical cancer, ovarian cancer, extragonadal germ cell tumor, brain tumor, brain cancer, extracranial germ cell tumor, bone cancer, pancreatic cancer, head and neck cancer, jaw cancer, cancer esophageal, hypopharyngeal cancer, laryngeal cancer, lip and oral cavity cancer, medulloblastoma, melanoma, Merkel cell carcinoma, mesothelioma (such as pleural mesothelioma, pericardial mesothelioma and peritonal mesothelioma), sarcoma (such as osteosarcoma, leiomyosarcoma, sarcoma Kaposi's, malignant fibrous histiocytoma, liposarcoma, Ewing's sarcoma and dermatofibrosarcoma protuberans), neuroblastoma, retinoblastoma, hepatoblastoma, nephroblastoma, glial tumor, malignant cutaneous or intraorbital melanoma, squamous cell cancer, squamous cell neck cancer, intraocular melanoma, cancer bile duct cancer, colon cancer, duodenal cancer, small intestine cancer, rectal cancer, anal cancer, appendix cancer, bile duct cancer, extrahepatic bile duct cancer, islet cell pancreatic cancer, testicular cancer, fallopian tube carcinoma, endometrial carcinoma, uterine cervical carcinoma, vaginal carcinoma, vulvar carcinoma, Hodgkin's disease, non-Hodgkin's lymphoma, lymphoplasmacytic lymphoma, bronchial adenoma / carcinoid, Burkit's lymphoma, carcinoid tumor, cerebellar astrocytoma, chronic cancer of the nasal cavity and sinus, nasopharyngeal cancer, salivary adenocarcinoma, sublingual adenocarcinoma, parathyroid adenocarcinoma, endocrine system cancer, thyroid gland cancer, parathyroid gland cancer, adrenal cancer, soft tissue sarcoma, urethral cancer, penile cancer, astrocytoma , basal cell cancer, chronic or acute leukemia including acute myeloid leukemia, chronic myeloid leukemia, acute lymphoblastic leukemia and chronic lymphoblastic leukemia, pediatric solid cancer, lymphocytic lymphoma, kidney or ureter cancer, renal pelvis carcinoma, nervous system tumor central nervous system (CNS), primary CNS lymphoma, tumor angiogenesis, spinal tumor, brain stem glioma, pituitary adenoma, Kaposi sarcoma, squamous cell cancer, flat cell cancer, T cell lymphoma, glioblastoma multiforme, malignant melanoma, non-small cell lung, small cell lung cancer, renal cell cancer, AIDS-related cancer, and asbestos-induced cancer. The cancer may be selected from the above-mentioned group, for example, or may be selected from the group consisting of leukemia, myelodysplastic syndrome, multiple myeloma, malignant lymphoma, stomach cancer, colorectal cancer, lung cancer, breast cancer, germ cell cancer. , liver cancer, skin cancer, urinary bladder cancer, prostate cancer, uterine cancer, cervical cancer, ovarian cancer and brain tumor. The cancer can be selected, for example, from the group consisting of leukemia, myelodysplastic syndrome, multiple myeloma, urinary bladder cancer, brain tumor, breast cancer, lung cancer, colorectal cancer, malignant lymphoma, esophageal cancer, head and neck cancer. neck, liver cancer, ovarian cancer, pancreatic cancer, prostate cancer and stomach cancer; can be selected from the group consisting of leukemia, myelodysplastic syndrome and multiple myeloma; or it may be selected from the group consisting of myelodysplastic syndrome, breast cancer, lung cancer, colorectal cancer, and urinary bladder cancer. In the present embodiment, the subject may be a human or may be a non-human animal. Preferably the non-human animal would be a mammal. The subject may be a human who has cancer, a human suspected of having cancer, or a human at risk of developing cancer, and is preferable a human who has cancer. The subject, when he has cancer, is also referred to as a patient. The peptide or compound of the present embodiment or its pharmaceutically acceptable salt can be used as an active ingredient for CTL-inducing agents in cancer cellular immunotherapy, as an active ingredient for cancer vaccines or as an active ingredient for pharmaceutical compositions taking a suitable form. according to each peptide or compound or salt thereof. The pharmaceutical composition, peptide or compound of the present embodiment or its pharmaceutically acceptable salt can be administered together with a pharmaceutically acceptable carrier, for example, a suitable adjuvant, so that cell-mediated immunity of the peptide or compound is effectively produced. . For similar reasons, the pharmaceutical composition of the present embodiment may comprise a pharmaceutically acceptable carrier, for example, a suitable adjuvant. Examples of the adjuvant include precipitated adjuvants and oil adjuvants. Precipitated adjuvant refers to an inorganic suspending agent to which a peptide is adsorbed. Specifically, examples of the precipitated adjuvant include sodium hydroxide, aluminum hydroxide (alum), calcium phosphate, aluminum phosphate, potassium aluminum sulfate, HEPES and carboxyvinyl polymers. Oil adjuvant refers to an oil emulsion that encloses an aqueous solution containing a peptide in mineral oil to form a micelle for emulsification. Examples of the oil adjuvant include, specifically, liquid paraffin, lanolin, Freund's adjuvant (complete Freund's adjuvant and incomplete Freund's adjuvant), Montanide and water-in-oil emulsions. They are also applicable as adjuvants, for example, those described in the literature (Clin. Microbio! Rev., 7: 277-289, 1994). Specifically, examples thereof include bacteria-derived components, GM-CSF, cytokines such as interleukin 2, interleukin 7 and interleukin 12, plant-derived components, components derived from marine organisms, mineral gels such as aluminum hydroxide, lysolecithin, surfactants such as Pluronic polyol, polyanions, peptides and oil emulsions (emulsion preparations). Examples of the bacterially derived component include lipid A, its monophosphoryl lipid A derivative, dead bacteria (examples of which include bacteria of the genus Mycobacterium such as Mycobacterium bovis, BCG), bacterially derived proteins, polynucleotides, incomplete Freund's adjuvant, complete adjuvant Freund's, skeletal components of the cell wall (e.g., BCG-CWS), and trehalose dimycolate (TDM). The peptide or compound of the present embodiment may also be administered as a liposome preparation, a granular preparation bound with beads of several pm in diameter, a lipid-bound preparation, a water-in-oil emulsion preparation, or the like. Furthermore, the peptide or compound (conjugate) of the present embodiment can be administered together with an MHC class II restricted WT1 peptide (i.e., an auxiliary peptide). Although the conjugate and the auxiliary peptide can be administered individually as a co-administration method, a cocktail preparation (cocktail agent or cocktail) comprising the conjugate and the auxiliary peptide in a pharmaceutical composition is more preferable. This cocktail preparation comprises a conjugate capable of producing an MHC class I-restricted WT1 peptide (i.e., a killer peptide) and an MHC class II-restricted WT1 peptide (i.e., a helper peptide). Therefore, by administering this prepared cocktail containing the helper peptide as a cancer vaccine in cancer immunotherapy, the activation of helper T cells is also possible, which is important for increasing the functions of other T cells that include CTL, and is may improve the pharmacological function / efficacy (cell-mediated immune competence, etc.) of the conjugate. In the method for selecting a potential subject who benefits from a pharmaceutical composition for treating or preventing cancer according to the present embodiment (hereinafter also referred to as the selection method of the present embodiment), an indication may be provided that a potential subject benefiting on the basis of 1 or 2 or more items in combination selected from the group consisting of items (1) to (6) given below. By providing an indication that a subject would potentially benefit from the pharmaceutical composition, it is also possible to predict the subject's response to the pharmaceutical composition. (1) A mutation in the TP53 gene and / or BCOR gene (2) The degree of mRNA expression of the WT1 gene (3) A karyotype based on the revised IPSS (IPSS-R) (4) The presence or absence of a increase in WT1 antigenic peptide-specific CD8 T cells (5) The presence or absence of a late-type hypersensitivity reaction (6) A change in the proportion of myeloblasts In the case of providing an indication that a potential subject will benefit on the basis of 2 or more items in combination, selected from the group consisting of items (1) to (6), the order of implementation is not limited to the order described above. Experts in the field can adequately establish the steps to be carried out and their order taking into account the efficiency of the selection, the condition or burden on the subject, etc. It is also possible to predict and select an effective combination using artificial intelligence, machine learning or a statistical method, etc., based on big data about a patient's treatment, for example, the disease, medical status, genome information, a treatment risk factor and inspection data. For example, the potential subject who benefits from the pharmaceutical composition can be selected first by performing a selection based on one or more items selected from (1) to (3) that do not require the administration of the pharmaceutical composition or peptide, reducing potential subjects to benefit from the pharmaceutical composition based on the results, and then making a selection based on one or more items selected from (4) to (6) that require administration of the pharmaceutical composition or peptide. On the other hand, for example, it is also possible to first carry out a selection based on one or more items selected from (4) to (6), reduce the potential subjects who benefit from the pharmaceutical composition based on the results and then carry out a selection based on one or more items selected from (1) to (3). For example, when the IPSS-R-based karyotype of a subject has already been determined, it is also possible to reduce the potential subjects who benefit from the pharmaceutical composition by selecting based on item (3) and then performing a selection based on on one or more items selected from (1) to (2) and (4) to (6). In the case of carrying out a selection carried out preferably without the administration of the pharmaceutical composition or peptide to the same subject after carrying out the selection that requires the administration of the pharmaceutical composition or peptide, this can be carried out after a predetermined period has elapsed to sufficiently reduce the influence of the administration of the pharmaceutical composition or the peptide. The sample according to the present embodiment is not particularly limited as long as it can be taken from the subject, and examples thereof include body fluid such as blood, lymph, ascites fluid, pleural effusion, sputum, spinal fluid (cerebrospinal fluid), lacrimal fluid , nasal discharge, saliva, urine, vaginal fluid, seminal fluid and joint fluid, mucous membrane, cells, tissues and cell or tissue cultures. Blood includes plasma, serum, and interstitial fluid. The cells include blood cells such as erythrocytes, leukocytes, platelets, hematopoietic stem cells, bone marrow blood and myeloblasts, and malignant tumor (cancer) cells such as circulating tumor cells, leukemia cells, gemmules accompanied by dysplasia, brain tumor, colorectal cancer cells, lung cancer cells, breast cancer cells, uterine cancer cells, stomach cancer cells, liver cancer cells, prostate cancer cells, kidney cancer cells, pancreatic cancer cells , sarcoma cells, malignant mesothelioma cells and lymphoma cells. A tissue that contains cancer is referred to as a cancerous tissue. The sample may be taken from the subject based on a method known in the art. For example, blood or lymph can be extracted by a known blood collection method. For example, cells or tissue can be taken by a known method, such as puncture, fine needle aspiration, brushing, peritoneal lavage, needle biopsy, or surgical biopsy. The sample according to the present embodiment can be selected from the group consisting of body fluid, mucous membrane, a cell, a tissue and a cell or tissue culture, and combinations thereof; can be selected from the group consisting of blood, spinal fluid, a blood cell, a cancer cell, a cancer tissue and a culture of cancer cells or tissue, and combinations thereof; can be selected from the group consisting of blood, spinal fluid, a cancer cell, a cancer tissue and a culture of cancer cells or cancer tissue, and combinations thereof; or it may be blood or spinal fluid. The effect of the pharmaceutical composition for treating or preventing cancer may differ depending on the type of cancer and the condition of the subject, etc., and examples thereof include prolonging the survival period, stabilizing myeloblasts, decreasing cells. cancer, preventing metastasis and delaying progression (for myelodysplastic syndrome (MDS) patients, prolonging the transition period to acute myeloid leukemia (AML)). The potential subject who benefits from the pharmaceutical composition includes, for example, a subject whose probability of responding to the pharmaceutical composition is high, and a subject whose probability of prolonging the survival period is high with administration of the pharmaceutical composition. The WT1 antigenic peptide-specific immune response is the immune response that is specifically induced by the administration of a WT1 antigenic peptide, etc. The induced WT1 antigenic peptide-specific immune response can be confirmed, for example, by the positivity of the results of the HLA tetramer assay determination, described below, or the positivity of the delayed hypersensitivity reaction. (1) Mutation in the TP53 gene and / or BCOR gene The TP53 gene is a cancer suppressor gene that encodes the nuclear protein p53 consisting of 393 amino acids. The BCOR gene is a corepressor of BCL6 and is a gene that specifically inhibits gene expression by binding to a transcription factor. Both have been reported to be poor prognostic factors. In the present specification, mutation in TP53 gene and / or BCOR gene means mutations in both TP53 gene and BCOR gene, TP53 gene mutation or BCOR gene mutation. The mutation in the TP53 gene and / or the BCOR gene may be the substitution, deletion or insertion of a nucleotide base, or a combination thereof, in each nucleotide sequence. The mutation in the TP53 gene and / or the BCOR gene may be the substitution, deletion or insertion of 1 to 20, 1 to 10, 1 to 8, 1 to 5, 1 to 4, 1 to 3, 1 to 2, or 1 nucleotide bases, or a combination thereof, in each nucleotide sequence. In the present specification, wild-type TP53 refers to the case where there is no mutation in the TP53 gene or the case where the TP53 gene, although having a mutation, does not lose the original function or is not accompanied by abnormality (which includes a silent mutation and a synonymous mutation, etc.). Mutant TP53 refers to the case where a mutation is present in the TP53 gene which therefore loses its original function or is accompanied by an abnormality. Wild-type BCOR refers to the case where there is no mutation in the BCOR gene or the case where the BCOR gene, although having a mutation, does not lose the original function or is not accompanied by an abnormality (including a silent mutation and a synonymous mutation, etc.). Mutant BCOR refers to the case where a mutation is present in the BCOR gene which therefore loses its original function or is accompanied by an abnormality. Thus, wild-type TP53 and / or wild-type BCOR include the case where either TP53 or BCOR is wild-type and the case where both TP53 and BCOR are wild-type. The selection method of the present embodiment comprises: determining the presence or absence of a mutation in the TP53 gene and / or the BCOR gene using a sample taken from the subject; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the subject has wild-type TP53 and / or wild-type BCOR. The subject, sample, pharmaceutical composition, etc., are as mentioned above. The determination of the presence or absence of a mutation in the TP53 gene and / or the BCOR gene is the determination of mutant TP53 and / or mutant BCOR in case a difference (mutation) is found with respect to the nucleotide sequence of wild type in a gene corresponding to the TP53 and / or BCOR gene in the subject, and the mutation is a mutation that abolishes the original function of the wild type or a mutation that is accompanied by an abnormality, and the determination of wild type TP53 and wild-type BCOR in case no difference (mutation) is found with respect to the wild-type nucleotide sequence or in case the mutation is a mutation that does not cause a change in the transcription of each gene and the function of the protein encoded by each gene (which includes a silent mutation and a synonymous mutation). The difference (mutation) of the wild-type nucleotide sequence can be detected by comparing the nucleotide sequence of the gene corresponding to the TP53 gene and / or the BCOR gene in the subject with the wild-type TP53 gene and / or the BCOR gene. . Determination of the nucleotide sequence of the gene corresponding to the TP53 gene and / or the BCOR gene in the subject and comparison with the wild-type nucleotide sequence can be performed by methods known to those skilled in the art. For example, the presence or absence of a mutation can be determined by extracting DNA from a sample by a conventional method, determining the sequence of each gene by next generation sequencing (NGS) or the like, and comparing with the sequence of corresponding wild-type gene. For example, depending on the mutation, the presence or absence of a mutation can also be determined by PCR-RFLP (restriction fragment length polymorphism) without determining the nucleotide sequence. It can also be performed, for example, using a commercially available DNA mutation / polymorphism detection kit. The selection method of the present embodiment may comprise, for example, determining the presence or absence of mutations in the TP53 gene and the BCOR gene and, as a result, may comprise providing an indication that the subject is a potential subject who benefit from the pharmaceutical composition in the case of wild-type TP53, may comprise providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition in the case of wild-type BCOR, or may comprise providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition in the case of wild-type TP53 and wild-type BCOR. The selection method of the present embodiment may comprise, for example, determining the presence or absence of a mutation in the TP53 gene and, as a result, may comprise providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition in the case of wild-type TP53. Likewise, the selection method of the present embodiment may comprise, for example, determining the presence or absence of a mutation in the BCOR gene and, as a result, may comprise an indication that the subject is a potential subject to benefit from the pharmaceutical composition in the case of wild-type BCOR. Furthermore, the selection method of the present embodiment may comprise, for example, in the case of mutant TP53 and / or mutant BCOR, providing an indication that the subject is not a potential subject to benefit from the pharmaceutical composition. The case where the original function is not lost or there is no accompanying abnormality means that each gene is identical or substantially identical to the wild type (which includes a silent mutation and a synonymous mutation, etc.). In this way, the TP53 gene and / or the BCOR gene can be used as markers to provide an indication of whether or not a potential subject is likely to benefit from a pharmaceutical composition for treating or preventing cancer. (2) Degree of WT1 gene mRNA expression In another embodiment, the present invention provides a method for selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer based on the degree of expression of the WT1 gene mRNA. The selection method of this modality includes: determining the degree of expression of the WT1 gene mRNA using a sample taken from the subject; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the degree of expression of the WT1 gene mRNA is less than a reference value or the reference value or less. Determination of the degree of expression of the WT1 gene mRNA can be carried out by a method known to those skilled in the art, such as quantitative PCR. It can also be done, for example, using a commercially available kit, such as the Otsuka WT1 mRNA Measurement Kit II (OTSUKA Pharmaceutical Co., Ltd.). For example, RNA is extracted from a sample and subjected to a quantitative PCR reaction, such as RT-PCR, with a real-time PCR apparatus or the like, using the primers specific for WT1, and the measurement values ​​can be calculated. of WT1 mRNA and housekeeping gene mRNA (GAPDH, β-actin, etc.) as internal control, based on a calibration curve; Then, for example, as shown in the expression given below (expression 1), the degree of expression of WT1 mRNA (copies / pg of RNA) can be calculated by multiplying the value obtained by dividing the measurement value of mRNA of WT1 between the measurement value of housekeeping gene mRNA (number of WT1 mRNA copies per housekeeping gene mRNA copy) times the average number of housekeeping gene mRNA copies per pg of RNA in healthy adult humans (degree of mRNA expression of the constituent gene). In this way, the degree of WT1 mRNA expression (copies / pg RNA) can also be considered as a value calculated according to the following expression (expression 1). Expression 1 WT1 mRNA measurement value (copies / mL) Average WT1 mRNA measurement value Degree of constitutive _ ----------------------------------------xgen mRNA expression per pg RNA in humans WT1 (copies / pg RNA) healthy adults (copies / pg RNA) Constitutive gene mRNA measurement value (copies / mL) In the case of using GAPDH as a housekeeping gene, for example, RNA is extracted from a sample and subjected to a quantitative PCR reaction, such as RT-PCR, with a real-time PCR apparatus or the like, using primers specific for WT1, and measurement values ​​of WT1 mRNA and GAPDH mRNA can be calculated based on a calibration curve. Then, for example, as shown in the expression given below, the degree of expression of WT1 mRNA (copies / pg of RNA) can be calculated by multiplying the value obtained by dividing the measurement value of WT1 mRNA by the measuring value of GAPDH mRNA (number of copies of WT1 mRNA per copy of GAPDH mRNA) by the average number of copies of GAPDH mRNA per pg of RNA in healthy adult humans (degree of GAPDH mRNA expression). In this way, the degree of WT1 mRNA expression (copies / pg RNA) can also be considered as a value calculated according to the following expression (expression 2). An average measurement value of GAPDH mRNA per pg RNA in healthy adult humans is 2.7 x 107 (copies / pg RNA). expression 2 Degree of WT1 mRNA expression (copies / pg RNA) WT1 mRNA measurement value (copies / mL) > --------------------------------------- x 2.7 x 107 (copies / pg RNA) GAPDH mRNA measurement value (copies / mL) The degree of WT1 mRNA expression (copies / pg RNA) can also be considered as a value calculated from the above formula (expression 2) according to the WT1 mRNA Measurement Kit II Otsuka (OTSUKA Pharmaceutical Co., Ltd.) and its attached protocol. In the selection method of the present embodiment, when the degree of expression of the WT1 gene mRNA is less than a reference value or the reference value or less, an indication that the subject is a potential subject can be provided. benefit from the pharmaceutical composition. The reference value of the degree of expression of the WT1 gene mRNA may be, for example, a value between 50 and 100,000 (copies / pg RNA), it may be a value between 100 and 50,000 (copies / pg RNA), it may be a value between 1000 and 20000 (copies / pg RNA), it can be a value between 2000 and 10000 (copies / pg RNA), it can be a value between 3000 and 10000 (copies / pg RNA), or it can be a value between 4000 and 10000 (copies / pg RNA). Also the reference value of the degree of mRNA expression of the WT1 gene may be, for example, a value of 50 (copies / pg RNA) or more, a value of 100 (copies / pg RNA) or more, a value of 250 (copies / pg RNA) or more, a value of 500 (copies / pg RNA) or more, a value of 750 (copies / pg RNA) or more, a value of 1000 (copies / pg RNA) or more, a value of 1000 (copies / pg RNA) or more, a value of 1250 (copies / pg RNA) or more, a value of 1500 (copies / pg RNA) or more, a value of 1750 (copies / pg RNA) or more, 2000 (copies / pg RNA) or more, a value of 2250 (copies / pg RNA) or more, a value of 2500 (copies / pg RNA) or more, a value of 2750 (copies / pg RNA) or more, a value of 3000 (copies / pg RNA) or more, a value of 3250 (copies / pg RNA) or more, a value of 3500 (copies / pg RNA) or more, a value of 3750 (copies / pg RNA), or a value of 4000 (copies / pg RNA) or more, may be a value of 15000 (copies / pg RNA) or less, a value of 14000 (copies / pg RNA) or less, a value of 13000 (copies / pg RNA ) or less, a value of 12000 (copies / pg RNA) or less, a value of 11000 (copies / pg RNA) or less, or a value of 10000 (copies / pg RNA) or less, and may be 50 ( copies / pg RNA), 100 (copies / pg RNA), 250 (copies / pg RNA), 500 (copies / pg RNA), 750 (copies / pg RNA), 1000 (copies / pg RNA), 1000 (copies / pg RNA) pg RNA), 1250 (copies / pg RNA), 1500 (copies / pg RNA), 1750 (copies / pg RNA), 2000 (copies / pg RNA), 2250 (copies / pg RNA), 2500 (copies / pg RNA ), 2750 (copies / pg RNA), 3000 (copies / pg RNA), 3250 (copies / pg RNA), 3500 (copies / pg RNA), 3750 (copies / pg RNA) or more, 4000 (copies / pg RNA ), 15000 (copies / pg RNA), 14000 (copies / pg RNA), 13000 (copies / pg RNA), 12000 (copies / pg RNA), 11000 (copies / pg RNA) or 10000 (copies / pg RNA). In the selection method of the present embodiment, for example, when the mRNA expression degree of the WT1 gene is less than 4000 (copies / pg RNA) or 4000 (copies / pg RNA) or less, an indication can be provided that the subject is a potential subject to benefit from the pharmaceutical composition, or when the degree of mRNA expression of the WT1 gene is less than 10,000 (copies / pg RNA) or 10,000 (copies / pg RNA) or less, may provide an indication that the subject is a potential subject to benefit from the pharmaceutical composition. In the selection method of the present embodiment, it is preferable to provide an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the degree of expression of the WT1 gene mRNA is less than a value between 4000 and 10000 ( copies / pg RNA) or the value or less. In case the subject is a myelodysplastic syndrome (MDS) patient, it is preferable that the reference value of the level of mRNA expression of the WT1 gene is a value of 100,000 (copies / pg RNA) or less, preferably a value between 4000 and 10000 (copies / pg RNA) and most preferably a value of 10000 (copies / pg RNA) or less. When the degree of WT1 gene mRNA expression in a sample taken from the subject is less than the reference value, or the reference value or less, the OS tends to extend. In this way the WT1 gene can be used as a marker to provide an indication of whether or not a potential subject will benefit from a pharmaceutical composition to treat or prevent cancer. (3) Karyotype based on revised IPSS (IPSS-R) In an alternative embodiment, the present invention provides a method for selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer on the basis of karyotyping based on the revised IPSS (IPSS-R). The selection method of the present embodiment comprises providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when karyotyping based on the revised IPSS (IPSS-R, Greenberg et al., B / ood 120, No. 12, pp. 2454-2465 (2012)) of the subject is different from very bad. The selection method of the present embodiment may comprise, prior to this step, determining the IPSS-R-based karyotype of the subject using a sample collected from the subject. The IPSS-R-based karyotype may be determined by analysis by a method known to those skilled in the art, such as a differential G staining method or a differential Q method. When the IPSS-R-based karyotype of the subject is different from very bad, an indication is provided that the subject is a potential subject benefiting from the pharmaceutical composition. The selection method of the present embodiment may provide, for example, an indication that the subject is a potential subject benefiting from the pharmaceutical composition when the IPSS-R-based karyotype of the subject is good / very good, intermediate or poor. ; may provide an indication that the subject is a potential subject who benefits from the pharmaceutical composition when it is intermediate or bad; it can provide an indication that the subject is a potential subject that benefits from the pharmaceutical composition when it is bad; may provide an indication that the subject is a potential subject who benefits from the pharmaceutical composition when good / very good; or it may provide an indication that the subject is a potential subject who benefits from the pharmaceutical composition when it is good / very good or intermediate. Alternatively, where the IPSS-R based karyotype of the subject is very poor, an indication may be provided that the subject is not a potential subject to benefit from the pharmaceutical composition. (4) Presence or absence of an increase in WT1 antigen peptide-specific CD8 T cells In an alternative embodiment, the present invention provides a method for selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer, based on the presence or absence of an increase in antigenic peptide-specific CD8 T cells. WT1. The selection method of the present embodiment comprises: detecting WT1 antigenic peptide-specific CD8 T cells using a sample taken from the subject to whom the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is administered; and providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when WT1 antigenic peptide-specific CD8 T cells are elevated compared to a sample taken from the subject prior to administration. The subject, the sample, the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof, etc., are as mentioned above. Detection of WT1 antigen peptide-specific CD8 T cells can be confirmed, for example, by measuring the presence or number of WT1 antigen peptide-specific CD8 T cells by an HLA monomer method, an HLA dimer method, a of HLA tetramer {Int. J. Cancer, 100, 565-570 (2002)), an HLA pentamer method, an HLA dextramer method, ELISPOT, real-time RT-PCR or limiting dilution method (Nat. Med., 4, 321-327 (1998)). Thus, detection of WT1 antigen peptide-specific CD8 T cells can be by measuring the presence or number of WT1 antigen peptide-specific CD8 T cells. For the detection of WT1 antigen peptide-specific CD8 T cells it is preferable to measure by an HLA tetramer method. The HLA tetramer is prepared by biotinylation of a complex (HLA monomer) of an HLA 0 chain and β2-microglobulin associated with a peptide, and its binding to fluorescently labeled avidin for tetramerization. The presence or number of WT1 antigen peptide-specific CD8 T cells can be measured by labeling the WT1 antigen peptide-specific CD8 T cells with the HLA tetramer and analyzing them in a flow cytometer. Based on similar principles, the presence or number of WT1 antigen peptide-specific CD8 T cells can also be measured by the HLA monomer method, the HLA dimer method, the HLA pentamer method, and the dextramer method. of HLA. Detection of WT1 antigen peptide-specific CD8 T cells can be performed by reacting a complex of a WT1 peptide and an HLA molecule with a sample, and examining the presence or number of WT1 antigen peptide-specific CD8 T cells that recognize the WT1 antigen peptide. complex content in the sample. The complex of WT1 peptide and HLA molecule can be selected, for example, from the group consisting of an HLA monomer, an HLA dimer, an HLA tetramer, an HLA pentamer and an HLA dextramer. Here it is preferable that the HLA molecule is compatible with the HLA of the subject. The HLA molecule may be, for example, an HLA-A24 antigen or an HLA-A2 antigen. Detection of WT1 antigenic peptide-specific CD8 T cells may comprise analysis by a flow cytometry method. Examination for the presence or number of WT1 antigen peptide-specific CD8 T cells that recognize the complex contained in the sample can be performed, for example, by measuring the ratio of HLA tetramer-bound cells to antigen peptide-specific CD8 T cells. WT1 CD8-positive or CD8 / CD3-positive. The presence or number of WT1 antigenic peptide-specific CD8 T cells bound to an HLA tetramer can be determined, for example, by measuring the proportion of cells bound to the HLA tetramer to CD8-positive or CD8 / CD3-positive cells. Here, CD8-positive cells can be labeled and detected, for example, using a fluorescently labeled mouse anti-human CD8 monoclonal antibody. Also, CD3-positive cells can be labeled and detected using a fluorescently labeled mouse anti-human CD3 monoclonal antibody. Here it is necessary that the fluorescent dye used is different from the fluorescent dye used in the HLA tetramer. Specifically, it is necessary to use different fluorescent dyes such that in case of using a PE-labeled HLA tetramer, a FITC-labeled mouse anti-human CD8 monoclonal antibody and a PerCP-labeled mouse anti-human CD3 monoclonal antibody are used. The specific operation includes, to measure the proportion of cells bound to the HLA tetramer to CD8-positive cells, for example, contacting a PE-labeled HLA tetramer with a biological sample, then adding a monoclonal anti-human CD8 antibody of FITC-labeled mouse for the reaction, and analyze the labeled cells on a flow cytometer or a fluorescence microscope. CD8-positive (CD8+) cells are selected and among them the proportion of tetramer-positive cells (tetramer+CD8+) can be used as the proportion of WT1 antigenic peptide-specific CD8 T cells (following): WT1 antigenic peptide (%) (number of tetramer+CD8+ cells / number of CD8+ cells) x 100. To measure the proportion of cells bound to the HLA tetramer to CD3-positive and CD8-positive cells, for example, a PE-tagged HLA tetramer is contacted with a biological sample, then an anti-HLA monoclonal antibody is added for the reaction. FITC-labeled mouse human CD8 and a PerCP-labeled mouse anti-human CD3 antibody, and the labeled cells are analyzed on a flow cytometer or fluorescence microscope. CD3-positive and CD8-positive (CD3+CD8+) cells are selected and among them the proportion of tetramer-positive cells (CD3+CD8+tetramer+) can be used as the proportion of WT1 antigenic peptide-specific CD8 T cells (which go on): WT1 antigenic peptide-specific among the CD8 T cells in the sample taken from the subject after administration has increased to a predetermined ratio or greater, compared to the proportion (positive ratio) of WT1 antigenic peptide-specific CD8 T cells among the cells T CD8 in the sample taken from the subject before administration, WT1 antigenic peptide-specific CD8 T cells can be considered to have increased. Also, for example, (a) in case WT1 antigenic peptide-specific CD8 T cells are not detected in the sample taken from the subject before administration, WT1 antigenic peptide-specific CD8 T cells are detected in the sample taken of the subject after administration, and the proportion (positive proportion) thereof is a reference value or greater, and / or (b) in case the proportion (positive proportion) of antigenic peptide-specific CD8 T cells WT1 among the CD8 T cells in the sample taken from the subject after administration has increased to a predetermined ratio or greater, compared to the proportion (positive ratio) of WT1 antigenic peptide-specific CD8 T cells among the CD8 T cells in the sample taken from the patient before administration, WT1 antigenic peptide-specific CD8 T cells can be considered to have increased. Regarding (a) In case WT1 antigenic peptide-specific CD8 T cells are not detected (not present) in the sample taken from the subject before administration, a multiplication factor can be calculated compared to the number of peptide-specific CD8 T cells. WT1 antigen in the sample taken from the subject after administration. In this case, for example, if it is a preset reference value or higher, WT1 antigenic peptide-specific CD8 T cells can be considered to have increased (positive). For example, those skilled in the art can establish a range in which WT1 antigenic peptide-specific CD8 T cells are considered positive, with respect to the results of a test already performed, etc., and conveniently establish a value that serves as reference to determine that WT1 antigenic peptide-specific CD8 T cells have increased (positive) in terms of the number of WT1 antigenic peptide-specific CD8 T cells included in the range. For example, the detection of WT1 antigenic peptide-specific CD8 T cells comprises a flow cytometric analysis that establishes a framework that includes a cell population positive for CD8 and positive for the WT1 peptide. Provided that the number of WT1 antigen peptide-specific CD8 T cells (event) in the sample taken from the subject after administration included in the range is a reference value or greater, for example, 1 or greater, 2 or greater, 3 or greater, 4 or greater, 5 or greater, 6 or greater, 7 or greater, 8 or greater, 9 or greater, 10 or greater, 15 or greater, or 20 or greater, CD8 T cells specific for WT1 antigenic peptide have increased (positive). Regarding (b) In case WT1 antigen peptide-specific CD8 T cells are detected in the sample taken from the subject prior to administration, WT1 antigen peptide-specific CD8 T cells can be considered to have increased (positive) when the ratio (positive ratio ) of WT1 antigen peptide-specific CD8 T cells among CD8 T cells in the sample taken from the subject after administration has increased to a predetermined ratio or higher, compared to the ratio (positive ratio) of WT1 antigen-peptide-specific CD8 T cells WT1 antigenic peptide between CD8 T cells in the sample taken from the subject prior to administration. For example, those skilled in the art can establish a range in which WT1 antigen peptide-specific CD8 T cells are considered positive, relative to the results of a test already performed, etc., and conveniently establish a value that serves as a reference to determine that WT1 antigen peptide-specific CD8 T cells have increased (positive) in terms of the proportions before and after administration of the number of WT1 antigen peptide-specific CD8 T cells included in the interval. For example, detection of WT1 antigen peptide-specific CD8 T cells comprises flow cytometric analysis that establishes a frame that includes a CD8-positive and WT1 tetramer-positive cell population. When the proportion (positive proportion) of WT1 antigen peptide-specific CD8 T cells among CD8 T cells after administration, in the sample taken from the subject after administration included in the interval, is a proportion that is considered maintained compared to with before administration, or greater, WT1 antigen peptide-specific CD8 T cells can be considered to have increased (positive). When the ratio is considered to be maintained or lower, it can be determined that the WT1 antigen peptide-specific CD8 T cells have decreased (negative). The proportion considered as maintained can be stated, for example, as greater than 0.1 to less than 5.0 times, greater than 0.5 to less than 2.0 times, greater than 0.8 to less than 1.2 times, greater than 0.9 to less than 1.1 times or 1.0 times, etc. The proportion considered as maintained can be, for example, 0.01, 0.05, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95 o 1.0 or greater, and can be 5.0 times, 4.5 times, 4.0 times, 3.5 times, 3.0 times, 2.5 times, 2.0 times, 1.8 times, 1.5 times, 1.4 times, 1.3 times, 1.2 times, 1.1 times, or 1.0 times o minor. In case of administering the pharmaceutical composition or the peptide or pharmaceutically acceptable salt thereof a plurality of times, for example, positivity or maintenance can be determined when it is determined that the WT1 antigenic peptide-specific CD8 T cells have increased (positive) or remain without change (maintained) at any time point after each administration, and negativity can be determined when WT1 antigenic peptide-specific CD8 T cells have decreased (negative) at all time points. As mentioned above, it is also possible to evaluate the effect of a candidate substance of a pharmaceutical composition to treat or prevent cancer based on the presence or absence of an increase in WT1 antigenic peptide-specific CD8 T cells. Specifically, the method for evaluating the effect of a candidate substance of a pharmaceutical composition for treating or preventing cancer according to the present embodiment, comprises: detecting WT1 antigenic peptide-specific CD8 T cells using a sample taken from a subject to whom the pharmaceutical composition or the pharmaceutically acceptable peptide or salt thereof contained in the pharmaceutical composition is administered; and provide an indication that the candidate substance is likely to produce an effect on cancer treatment and prevention when WT1 antigenic peptide-specific CD8 T cells are elevated compared to a sample taken from the subject prior to administration. The subject, the sample, the pharmaceutical composition or the peptide or its pharmaceutically acceptable salt, etc., are as mentioned above. (5) Presence or absence of a delayed-type hypersensitivity reaction In an alternative embodiment, the present invention provides a method for selecting a potential subject to benefit from a pharmaceutical composition for treating or preventing cancer based on the presence or absence of a late-type hypersensitivity reaction. The selection method of the present embodiment comprises providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when a late-type hypersensitivity reaction is detected in the subject to whom it has been administered a plurality of times. the pharmaceutical composition or the peptide or its pharmaceutically acceptable salt. The subject, sample, pharmaceutical composition or peptide or its pharmaceutically acceptable salt, etc., are as mentioned above. When a subject receiving a pharmaceutical composition or a peptide or its pharmaceutically acceptable salt is administered the same pharmaceutical composition or peptide or its pharmaceutically acceptable salt, a late-type hypersensitivity reaction can be detected. Delayed type hypersensitivity reaction (DTH reaction) is an allergic reaction attributable to a cell-mediated immune mechanism that belongs to type IV of the CoomsGelL classification. The presence or absence of this delayed type hypersensitivity reaction can be used as an indication whether or not the immune response of CD8 T cells specific for WT1 antigenic peptide is induced. The delayed type hypersensitivity reaction test (DTH test) can be performed by administering the same pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof to the subject who is administered one or more times the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof. In summary, in the selection method of the present embodiment, the same pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof is administered to the subject to whom the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof is administered one or more times. , and an indication that the subject is a potential subject to benefit from the pharmaceutical composition is provided when a late-type hypersensitivity reaction is detected. The first administration, one or more times, is not the administration for the DTH test, and the second administration of the same pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof corresponds to the administration for the DTH test. Here, the same pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof may be substantially the same and does not exclude two or more types of peptides administered separately and analyzed in the DTH test, for example, the case where the pharmaceutical composition administered one or More often than not, it is a vaccine in which two or more types of peptides are mixed. For example, the case where the pharmaceutical composition administered one or more times comprises a peptide consisting of the amino acid sequence of RMFPNAPYL (SEQ ID NO: 2), a peptide consisting of the amino acid sequence of C-CYTWNQMNL (SEQ ID NO: 10) and a peptide consisting of the amino acid sequence of WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), the DTH test can be performed by separately administering the peptide consisting of the amino acid sequence of RMFPNAPYL (SEQ ID NO: 2 ) and the peptide consisting of the amino acid sequence of C-CYTWNQMNL (SEQ ID NO: 10) and the peptide consisting of the amino acid sequence of C-CYTWNQMNL (SEQ ID NO: 10). The peptide consisting of the amino acid sequence of RMFPNAPYL (SEQ ID NO: 2) and the peptide consisting of the amino acid sequence of C-CYTWNQMNL (SEQ ID NO: 10) may be in the form of a conjugate as shown below. sample in formula (3). In the DTH test, the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is usually administered intradermally. Preferably the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is administered to the subject at a site different from the initial administration. DTH test determination times after administration can be appropriately established by experts in the field; The determination can be made, for example, from 1 hour to 1 week, 12 hours to 5 days, 1 day to 3 days, or 2 days after the most recent administration. For example, it may be immediately after administration or after, and / or within 1 week; may be, for example, less than, or within, 1 day, 2 days, 3 days, 4 days, 5 days or 6 days after administration, or may be 1 day, 2 days, 3 days, 4 days, 5 days or 6 days or more after administration. It is also preferable to perform the DTH test a plurality of times at different times and the delayed type hypersensitivity reaction should be determined from an average value of the results. The number of times the DTH test is done can be, for example, 2 times or more and / or within 20 times; may be, for example, less than, or within, 2 times, 3 times, 4 times, 5 times, 7 times, 10 times, 15 times or 20 times, or may be, for example, 2 times, 3 times , 4 times, 5 times, 7 times, 10 times or 15 times or more. Those skilled in the art can conveniently establish the dose of the pharmaceutical composition or the peptide or its pharmaceutically acceptable salt, sufficient to detect a delayed type hypersensitivity reaction. As for determining whether or not a late-type hypersensitivity reaction (presence or absence of late-type hypersensitivity reaction) is detected in the DTH test, for example, the reaction at the site of administration of the composition is compared pharmaceutical composition or the peptide or its pharmaceutically acceptable salt for the DTH test in the subject to which the pharmaceutical composition or the peptide or its pharmaceutically acceptable salt is administered one or more times, with the reaction at a site without the administration of the pharmaceutical composition or the peptide or its pharmaceutically acceptable salt for DTH testing in the subject, and when the difference between the reaction at the administration site and the reaction at a non-administration site is a reference value or greater, it may be considered to have been detected a late-type hypersensitivity reaction (a late-type hypersensitivity reaction is present). The site without administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof in the subject may be a site where the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof was not administered, or may be a site where only the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof was administered. a vehicle and solvent, etc. (vehicle), except the peptide or the pharmaceutically acceptable salt thereof of the pharmaceutical composition. The difference in reactions between the administration site and the non-administration site can be deduced from the difference in the long axis of redness between the administration site and the non-administration site (control). Those skilled in the art can conveniently establish a reference value to determine whether a specific immune response to the WT1 antigenic peptide is positive. For example, when the major axis of skin redness at the administration site with respect to the non-administration site is a value between +0.1 mm and 100 mm, or more, a delayed-type hypersensitivity reaction may be considered to have been detected. . In the case of a value between +0.5 mm and 50 mm or more, it can be considered that a delayed-type hypersensitivity reaction has been detected. In the case of a value between +1 mm and 100 mm or more, it can be considered that a delayed-type hypersensitivity reaction has been detected. In the case of 2 mm or more, it can be considered that a delayed type hypersensitivity reaction has been detected. Additionally, the lower limit value of the interval of the major axis of redness with which the detection of late-type hypersensitivity reaction is considered, can be 0.1 mm, 0.2 mm, 0.3 mm, 0.4 mm, 0.5 mm, 0.6 mm, 0.7 mm, 0.8 mm, 0.9 mm, or 1.0 mm, and the upper limit value can be 100 mm, 90 mm, 80 mm, 70 mm, 60 mm, 50 mm, 40 mm, 30 mm, 20 mm, 15 mm, or 10 mm. Scores corresponding to the major axis of skin redness at the administration site relative to the non-administration site are determined, and the presence or absence of a delayed-type hypersensitivity reaction can be determined from the scores. For example, for a major axis of redness less than 2 mm a score of 0 may be set, for 2 mm or more and less than 5 mm a score of + / - may be set, for 5 mm or more and less than 10. mm a score of 1 may be established, for 10 mm or more and less than 15 mm a score of 2 may be established, and for 15 mm or more a score of 3 may be established. An average of the subject's scores after administration a plurality of times, or the subject's maximum score after administration may be used. As mentioned above, it is also possible to evaluate the effect of a candidate substance of a pharmaceutical composition to treat or prevent cancer, on the basis of the presence or absence of a late-type hypersensitivity reaction. Specifically, the method for evaluating the effect of a candidate substance of a pharmaceutical composition for treating or preventing cancer according to the present embodiment comprises providing an indication that the candidate substance of the pharmaceutical composition is likely to produce an effect on the treatment and prevention of cancer, when a late-type hypersensitivity reaction is detected in a subject to whom the pharmaceutical composition or peptide or pharmaceutically acceptable salt of the same content in the pharmaceutical composition is administered a plurality of times. It comprises providing an indication that the candidate substance probably produces an effect on the treatment and prevention of cancer when a delayed-type hypersensitivity reaction is detected in the subject to whom the pharmaceutical composition or peptide or salt has been administered a plurality of times pharmaceutically acceptable of the same content in the pharmaceutical composition. The subject, the sample, the pharmaceutical composition or the peptide or its pharmaceutically acceptable salt are as mentioned above. (6) Change in the proportion of myeloblasts The selection method of the present embodiment comprises providing an indication that the subject is a potential subject who benefits from the pharmaceutical composition when the value obtained by dividing the proportion of myeloblasts in a sample taken from the subject to whom the pharmaceutical composition is administered or the peptide or the pharmaceutically acceptable salt thereof, between the proportion of myeloblasts in a sample taken from the subject before administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, is less than a reference value, or the value reference or less. The subject, sample, pharmaceutical composition or peptide or its pharmaceutically acceptable salt, etc., are as mentioned above. When the change in the proportion of myeloblasts in a sample, such as bone marrow fluid, is smaller between before and after administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, the myeloblasts are considered more stable. For example, when the ratio obtained by dividing the proportion of myeloblasts in the subject after administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof by the proportion of myeloblasts in the subject before administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof (hereinafter also referred to as myeloblast change) is 0% to 300% or less, 0% to 200% or less, 0% to 150% or less, 0% to 100% or less , or 0% to 50% or less, an indication that the subject is a potential subject to benefit from the pharmaceutical composition may be provided. Here the myeloblast change ratio may be, for example, 0% or greater or 300% or less, may be, for example, 50%, 100%, 150%, 200% or 250% or greater, or may be 50%, 100%, 150%, 200% or 250% or less. For example, based on the average change ratio of myeloblasts at one time point to several time points, it can be determined to be less than the reference value or the reference value or less, or based on the maximum value of the ratio of change of myeloblasts at one time point to several time points, it can be determined to be less than the reference value or the reference value or less. For example, when there is a change less than the reference value or the reference value or less at two or more time points, it can be determined to be less than the reference value or the reference value or less. The time point means the time of measurement of the proportion of myeloblasts after administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof. The measurement time of myeloblast proportion can be, for example, every 1 day to 365 days, every 1 day to 180 days, every 1 day to 90 days, every 1 day to 60 days, every 1 day to 30 days, or every 1 day to 4 weeks. The measurement time can be, for example, every 1 day or more or less than 365 days, it can be every 180 days, 90 days, 60 days, 30 days, 4 weeks, 3 weeks, 2 weeks, 1 week, 3 days or 1 day or more, or it can be 180 days, 90 days, 60 days, 30 days, 4 weeks, 3 weeks, 2 weeks, 1 week or 3 days or less. For example, when the myeloblast change rate up to 100 days after treatment changes 150% or less at two or more time points, it can be determined that the myeloblast change rate is 150% or less. (7) Sex difference The selection method of the present embodiment can provide an indication of whether a potential subject benefits based on 1 or 2 or more points in combination, selected from the group consisting of points (1) to (6) described above. It may also comprise providing an indication that the subject is a potential subject to benefit from the pharmaceutical composition when the sex of the subject is male (in the case of a human subject, a man). Method to treat or prevent cancer The method for treating or preventing cancer of the present embodiment comprises: selecting a potential subject who benefits from a pharmaceutical composition for treating or preventing cancer by the above-mentioned selection method; and administering the pharmaceutical composition to the selected subject. The method for treating or preventing cancer of the present embodiment comprises: determining a subject to whom a pharmaceutical composition is administered to treat or prevent cancer by the selection method based on 1 or 2 or more points in combination, selected from the group consisting of points (1) to (6) above; and administering the pharmaceutical composition. Also, the method for treating or preventing cancer of the present embodiment comprises: determining whether or not to administer the pharmaceutical composition for treating or preventing cancer to a subject by the selection method based on 1 or 2 or more points in combination, selected of the group consisting of points (1) to (6) above; and administering the pharmaceutical composition to the subject. In this way, the method for treating or preventing cancer of the present embodiment comprises: for example, as mentioned above in point (1), determining the presence or absence of a mutation in the TP53 gene and / or the gene BCOR; and administering the pharmaceutical composition to treat or prevent cancer to a subject having wild-type TP53 and / or wild-type BCOR. The method for treating or preventing cancer in the present embodiment comprises: for example, as mentioned above in point (2), determining the degree of mRNA expression of the WT1 gene; and administering the pharmaceutical composition for treating or preventing cancer to a subject whose WT1 gene mRNA expression level is less than a reference value or the reference value or less. The method for treating or preventing cancer of the present embodiment comprises: for example, as mentioned above in point (3), administering the pharmaceutical composition for treating or preventing cancer to a subject whose karyotype based on IPSS-R is different. very bad. The method for treating or preventing cancer of the present embodiment comprises: for example, as mentioned above in point (4), detecting CD8 T cells specific for WT1 antigenic peptide using a sample taken from a subject to whom the composition is administered. pharmaceutical or peptide or pharmaceutically acceptable salt thereof; and administering the pharmaceutical composition to the subject in which WT1 antigenic peptide-specific CD8 T cells have been elevated compared to a sample taken from the subject before administration. The method for treating or preventing cancer of the present modality comprises: for example, as mentioned above in point (5), administering the pharmaceutical composition to a subject in whom a late-type hypersensitivity reaction is detected when administering a plurality of times the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof. The method for treating or preventing cancer of the present embodiment comprises: for example, as mentioned above in point (6), administering the pharmaceutical composition to a subject when the value obtained by dividing the proportion of myeloblasts after the administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, between the proportion of myeloblasts before administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, is less than a reference value or the reference value or less. In the method for treating or preventing cancer of the present embodiment, the dose of the pharmaceutical composition of the present embodiment in a preparation can be conveniently adjusted depending on the disease treated, the age and body weight of the patient, etc., but can be from 0.0001 mg to 1000 mg, it can be 0.001 mg to 1000 mg, or it can be 0.1 mg to 10 mg. For example, a dose may be 1.75 mg to 17.5 mg, 3.5 mg to 10.5 mg, or 10.5 mg. Also a dose can be 0.0001 mg or greater, 0.0005 mg or greater, 0.001 mg or greater, 0.005 mg or greater, 0.01 mg or greater, 0.05 mg or greater, 0.1 mg or greater, 0.25 mg or greater, 0.5 mg or greater , 0.75 mg or greater, 1.0 mg or greater, 1.25 mg or greater, 1.5 mg or greater, 1.75 mg or greater, 2.0 mg or greater, 2.25 mg or greater, 2.5 mg or greater, 2.75 mg or greater, 3.0 mg or greater , 3.25 mg or greater, 3.5 mg or greater, 3.75 mg or greater, 4.0 mg or greater, 4.25 mg or greater, 5.5 mg or greater, 5.75 mg or greater, or 6.0 mg or greater, and may be 1000 mg or less , 750 mg or less, 500 mg or less, 250 mg or less, 125 mg or less, 100 mg or less, 50 mg or less, mg or less, 40 mg or less, 35 mg or less, 30 mg or less, 25 mg or less, 20 mg or less, 15 mg or less, or 10 mg or less. Examples of the administration method include intradermal administration, subcutaneous administration, intramuscular administration, intravenous administration and transdermal administration. Intradermal administration and subcutaneous administration which efficiently induce CTL are preferable. The number of doses and administration intervals can be suitably adjusted depending on the disease treated or prevented and the difference between individual patients, but usually a plurality of times; Preferably administration is carried out once every few days to a few months. For example, administration can be done once every 1 day to 6 months, can be done once every 3 days to 3 months, can be done once every 1 week to 4 weeks, can be done once every 2 weeks to 4 weeks, or it can be done every 6 weeks, 5 weeks, 4 weeks, 3 weeks, 2 weeks or 1 week. Also, the administration can be carried out at least every 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 7 weeks, 1 month, 2 months, 3 months, 4 months, 5 months or 6 months, and at most once every 12 months, 10 months, 8 months, 6 months, 5 months, 4 months, 3 months, 2 months, 1 month, 6 weeks, 5 weeks, 4 weeks, 3 weeks, 2 weeks, 1 week, 6 days or 5 days. The administration time can be changed after a lapse of a predetermined period, for example, after a lapse of 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months or 12 months. For example, administration can be done once every 2 weeks for the first 6 months, can be done once every 2 weeks from 1 month or more to 5 months, and can be done once every 2 weeks to 4 weeks or later. of 6 months. Administration can be done every 2 weeks for the first 6 months and then every 2 weeks to 4 weeks. The present embodiment also includes a pharmaceutical composition for use in a method of treating or preventing cancer. The pharmaceutical composition, the method of treating or preventing cancer, etc., are as mentioned above. Also included in the present embodiment is the method for determining a subject to whom a pharmaceutical composition is administered. The subject may be determined based on one 1 or 2 or more points in combination, selected from the group consisting of points (1) to (6) above. The method comprises: for example, as mentioned in point (1) above, determining the presence or absence of a mutation in the TP53 gene and / or the BCOR gene; and determining a subject having wild-type TP53 and / or wild-type BCOR as the subject to whom a pharmaceutical composition is administered to treat or prevent cancer. The method comprises: for example, as mentioned above in point (2), determining the degree of mRNA expression of the WT1 gene; and determining the subject whose degree of WT1 mRNA expression is less than a reference value or the reference value or less, as the subject to whom the pharmaceutical composition is administered. The method comprises, for example, as mentioned above in point (3), determining the subject whose karyotype based on IPSS-R is different from very bad as the subject who is administered a pharmaceutical composition to treat or prevent cancer . The method comprises: for example, as mentioned above in point (4), detecting WT1 antigenic peptide-specific CD8 T cells using a sample taken from a subject to whom the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof is administered. ; and determining the subject in which WT1 antigenic peptide-specific CD8 T cells have been elevated compared to a sample taken from the subject before administration, such as the subject to whom a pharmaceutical composition is administered to treat or prevent cancer. The method comprises, for example, as mentioned above in point (5), determining a subject in whom a late-type hypersensitivity reaction is detected by administering a plurality of times a pharmaceutical composition or peptide or pharmaceutically acceptable salt of the same, as the subject to whom a pharmaceutical composition is administered to treat or prevent cancer. The method comprises, for example, as mentioned above in point (6), determining a subject in which the value obtained by dividing the proportion of myeloblasts after administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, between the proportion of myeloblasts before administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, is less than a reference value or the reference value or less, such as the subject to whom a pharmaceutical composition is administered to treat or prevent cancer. Also included in the present embodiment is a method for determining whether or not to administer a pharmaceutical composition to treat or prevent cancer. Whether or not a pharmaceutical composition is administered to treat or prevent cancer can be determined based on 1 or 2 or more items in combination selected from the group consisting of items (1) to (6) above. The method comprises: for example, as mentioned above in point (1), determining the presence or absence of a mutation in the TP53 gene and / or the BCOR gene using a sample taken from a subject; and determining a subject to whom, in the case of TP53 wild type and / or BCOR wild type, the subject is administered the pharmaceutical composition to treat or prevent cancer, and in the case of TP53 mutant and / or BCOR mutant, no The pharmaceutical composition is administered to the subject to treat or prevent cancer. The method comprises: for example, as mentioned above in point (2), determining the degree of expression of WT1 gene mRNA in a sample taken from a subject; and determining that, when the degree of expression of WT1 mRNA is less than a reference value or the reference value or less, the pharmaceutical composition is administered to the subject to treat or prevent cancer; and when the degree of WT1 mRNA expression is a reference value or greater than the reference value, the pharmaceutical composition for treating or preventing cancer is not administered to the subject. The method comprises, for example, as mentioned above in point (3), determining that, when the IPSS-R-based karyotype of a subject is other than very bad, the subject is administered the pharmaceutical composition to treat or prevent cancer; and when the IPSS-R-based karyotype of the subject is very bad, the pharmaceutical composition for treating or preventing cancer is not administered to the subject. The method comprises, for example, as mentioned above in point (4), detecting WT1 antigenic peptide-specific CD8 T cells using a sample taken from a subject to whom the pharmaceutical composition or pharmaceutically acceptable peptide or salt is administered; and determining that, when WT1 antigen peptide-specific CD8 T cells have been elevated compared to a sample taken from the subject prior to administration, the pharmaceutical composition is administered to the subject; and when WT1 antigenic peptide-specific CD8 T cells have been maintained or decreased, do not administer the pharmaceutical composition to the subject. The method comprises, for example, as mentioned above in point (5), determining that, when a late-type hypersensitivity reaction is detected in a subject upon administering a plurality of times the pharmaceutical composition or peptide or pharmaceutically acceptable salt of the Likewise, the pharmaceutical composition is administered to the subject; and when a delayed hypersensitivity reaction is not detected in the subject, do not administer the pharmaceutical composition to the subject. The method comprises, for example, as mentioned above in point (6), determining that, when the value obtained by dividing the proportion of myeloblasts after administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, between the proportion of myeloblasts before administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, is less than a reference value or the reference value or less, the pharmaceutical composition is administered to the subject, and when it is the reference value or greater than the reference value, the pharmaceutical composition is not administered to the subject. Also included in the present embodiment is a method for screening subjects who would be administered a pharmaceutical composition to treat or prevent cancer. Screening can be performed based on 1 or 2 or more points in combination, selected from the group consisting of points (1) to (6) above. The method comprises, for example, as mentioned above in point (1), determining the presence or absence of a mutation in the TP53 gene and / or the BCOR gene; and selecting a subject who has wild type TP53 and / or wild type BCOR. The method comprises: for example, as mentioned above in point (2), determining the degree of mRNA expression of the WT1 gene; and selecting a subject whose expression degree of the WT1 gene is less than a reference value or the reference value or less. The method comprises, for example, as mentioned above in point (3), selecting a subject whose karyotype based on the IPSS-R is other than very bad. The method comprises: for example, as mentioned above in point (4), detecting WT1 antigenic peptide-specific CD8 T cells using a sample taken from a subject to whom the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof is administered. ; and selecting a subject in which WT1 antigenic peptide-specific CD8 T cells have been elevated compared to a sample from the subject prior to administration. The method comprises, for example, as mentioned above in point (5), selecting a subject in whom a late-type hypersensitivity reaction is detected by administering the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof a plurality of times. . The method comprises, for example, as mentioned above in point (6), selecting a subject in which the value obtained by dividing the proportion of myeloblasts after administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, between the proportion of myeloblasts before administration of the pharmaceutical composition or peptide or pharmaceutically acceptable salt thereof, is less than a reference value or the reference value or less. EXAMPLES Hereinafter, the present invention will be described in detail with reference to examples. However, the present invention is not limited by these in any way. EXAMPLE 1 Subject in this example and effect of the WT1 peptide cocktail vaccine In the example below, among patients with relapsed / refractory myelodysplastic syndrome (MDS) for whom informed consent was obtained, the number of patients who participated in phase 1 and phase 2 clinical trials of an emulsion cocktail vaccine water in oil, containing the WT1 killer peptide conjugate shown in formula (3) below and the WT1 helper peptide represented by WAPVLDFAPPGASAYGSL (SEQ ID NO: 14) (see International Publication No. WO 2014 / 157692; in hereinafter also referred to as WT1 peptide cocktail vaccine), was 47 cases and the breakdown with respect to the HLA type of the same was 12 cases of myelodysplastic syndrome (MDS) patients HI_A-A*02:01- or HI_A -A*02:06-positive, 28 cases of MDS patients HLA-A*24:02-positive, 5 cases of MDS patients HLA-A*02:01-positive and HLA-A*24:02 -positive, and 2 cases of MDS patients HLA-A*02:06-positive and HLA-A*24:02-positive, usually unless otherwise specified. The cases in the phase 1 clinical trial included 7 cases of high-risk patients (H) and also 5 cases of low-risk patients (L), and the cases in the phase 2 trial were 35 cases of high-risk patients (H). In this example, only high-risk patients were used as subjects and testing was performed using 42 cases of high-risk patients who did not respond to azacitidine as subjects (total of 7 cases from the phase 1 trial and 35 cases from phase 2 trial). High-risk patients correspond to patients at intermediate to very high risk in the revised IPSS risk classification (IPSS-R). The 42 cases of high-risk patients who did not respond to azacitidine included 40 cases who did not respond or no longer responded to azacitidine, and 2 cases who could not continue administration due to adverse reactions of azacitidine. CRMFPNAPYL I (3) CYTWNQMNL where the bond between C and C represents a disulfide bond. In phase 1 and phase 2 clinical trials, the WT1 peptide cocktail vaccine was administered intradermally (ID) every two weeks for 6 months as an induction vaccine. Administration was then continued every 2 weeks to 4 weeks until administration was discontinued. The phase 1 trial was conducted at a dose of 3.5 mg (2 mg WT1 killer peptide conjugate + 1.5 mg WT1 helper peptide) for cohort 1, and at a dose of 10.5 mg (6 mg WT1 killer peptide conjugate WT1 killer + 4.5 mg WT1 helper peptide) for cohort 2. The phase 2 trial was conducted at a recommended dose of 10.5 mg (6 mg WT1 killer peptide conjugate + 4.5 mg WT1 helper peptide) . The median survival time (mOS: median overall survival) in this trial was 8.6 months (90% confidence interval: 6.8-11.1 months) and was found to have a trend to be prolonged compared to 5.6 months in historical data (95% confidence interval: 5.0-7.2 months, Prebet et al., Journal de Clinical Oncologyl^, no. 24, p. 3322-3327 (2011)). EXAMPLE 2 Effect of WT1 peptide vaccine and influence of karyotype Figure 1 shows the results of the comparison of the WT1 peptide cocktail vaccine trial of Example 1 with a control (BSC from the rigosertib trial) in the ONTIME trial of rigosertib (phase 3 clinical trial, Table SI MDS cytogenetic prognosis by GarciaManero et al., The Lancet OncologyY7, no. 4, p. 496-508 (2016)). Considering the difference of a patient population in the phase 3 trial of rigosertib, the comparison was made in 33 cases of the 42 cases of example 1, which exclude 2 non-responder cases attributable to adverse reactions of azacitidine and 6 cases of high risk with gemmule number <5% or less and 1 case with unknown karyotype. Karyotype-based mOS tended to be longer in the good / very good to poor groups, except very poor karyotype, compared to the rigosertib BSC test, suggesting the possibility that the mOS lengthening was produced by the effect of WT1 peptide cocktail vaccine. In the very poor karyotype group, mOS in the WT1 peptide cocktail vaccine administration group was equivalent to BSC from the rigosertib trial. EXAMPLE 3 Search for a genetic biomarker to select potential patients who benefit from treatment with a WT1 peptide vaccine Among the 42 high-risk cases described in example 1, a genetic test associated with myelodysplastic syndrome (MDS) was performed in 29 cases of which informed consent was obtained. In the subsequent genetic analysis, of the 29 cases, 28 cases were used, except for 1 case which was a non-responder case attributable to azacitidine adverse reactions. Bone marrow fluid was collected from patients within 28 days before the start of administration of the WT1 peptide cocktail vaccine. DNA extraction from bone marrow fluid v specimen quality assessment DNA extraction was performed on 0.5 mL of a bone marrow fluid sample using the Wizard Genomic DNA Purification kit (Promega Corp.) according to the protocol included in this kit (3A Genomic DNA Isolation from Whole Blood). As an evaluation of the quality of the extracted DNA, it was confirmed whether a clear band could be detected in a high molecular region by agarose gel electrophoresis. Fluorescence intensity was measured in a plate reader using the Quant-iT PicoGreen dsDNA Assay kit (Life Technologies Corp.), and the concentration was calculated from a calibration curve. Next Generation Sequencing (NGS) Assay A next-generation sequencing (NGS) assay was performed using TruSight Myeloid Sequencing Panel (Illumina, Inc.) targeted mutations associated with myeloid malignancies such as acute myeloid leukemia (AML), myelodysplastic syndrome (MDS), myeloproliferative neoplasia (MPN), chronic myeloid leukemia (CML), chronic myelomonocytic leukemia (CMML), and juvenile myelomonocytic leukemia (JMML). Genomic DNA extracted from bone marrow fluid was analyzed for the selected sequence by TruSight Myeloid Sequencing Panel. The region to be measured was amplified using the panel to prepare a collection. Chain length distribution was then confirmed by electrophoresis analysis using the Agilent DNA1000 Kit (Agilent Technologies, Inc.) and quantified using a real-time PCR apparatus (Applied Biosystems). The quantification results were corrected with the average collection size and the collection concentration was calculated. Nucleotide sequences were determined on MiSeq (Illumina, Inc.). The panel covers 40 genes shown in Table 1 below. TABLE 1 CEBPA SF3B1 ASXL1 IDH1 NOTCH1 SMC1A ATRX IDH2 NPM1 SMC3 BCOR DNMT3A NRAS SRSF2 BCORL1 ETV6 / TEL JAK2 STAG2 BRAF EZH2 PHF6 TET2 FBXW7 KDM6A TP53 CBL FLT3 KIT PTPN11 U2AF1 CBLB GATA1 KRAS RAD21 WT1 GATA2 RUNX1 ZRS R2 GNAS MPL Bioinformatic analysis Genetic mutations of nucleotide sequences determined on the MiSeq (Illumina, Inc.) were analyzed by bioinformatics using MiSeq Reporter (Illumina, Inc.). Results Table 2 shows the results of the genetic mutation analysis. In the table, the thick horizontal line is a line representing mOS and the survival period (OS: overall survival) becomes longer in order from top to bottom. The description about the IPSS-R karyotype of patients with good / very good or intermediate IPSS-IR karyotype was omitted. TABLE 2 Karyotype ID IPSS-R TP53 BCOR 1 Very bad X 2 Very bad X 3 Very bad X Bad 18 19 20 21 22 23 Very bad 24 25 26 27 28 29 For cases that have mutant TP53 or mutant BCOR it was found that OS tends to be short. This suggested the possibility that the presence or absence of mutations in the TP53 and BCOR gene may be useful as a genetic marker to select potential patients who would benefit from treatment with the WT1 peptide vaccine. Also, in a population that has short OS, the trend of many cases with very poor karyotype was observed. EXAMPLE 4 Utility of the TP53 / BCOR gene mutation as a genetic marker To verify the usefulness of the presence or absence of mutations in the TP53 and BCOR gene as genetic markers, a comparison of survival curves was made based on the presence or absence of mutations. The patients described in Example 1 were divided into 17 cases of patients having wild-type TP53 and wild-type BCOR, and 11 cases of patients having mutant TP53 or mutant BCOR, and the survival curves were compared. As shown in Figure 2, the mean overall survival (mOS) of wild-type TP53 and wild-type BCOR tends to be long compared to the mOS of mutant TP53 or BCOR. For the 17 cases that have wild-type TP53 and wild-type BCOR and the 11 cases that have mutant TP53 or mutant BCOR, a WT1 antigenic peptide-specific immune response induced by the WT1 peptide cocktail vaccine was confirmed by aforementioned HLA tetramer assay and the late-type hypersensitivity reaction. Figure 3 shows the results of the comparison of the periods of survival (OS) and immune response for wild-type TP53 and wild-type BCOR and mutant TP53 or mutant BCOR. The results shown in Figure 3 are about 15 cases that have wild-type TP53 and wild-type BCOR, and 9 cases that have mutant TP53 or mutant BCOR, except 4 cases in which determination of the immune response was impossible. It was observed that for wild-type TP53 and wild-type BCOR the overall survival tends to be long. Many positive cases for immune response were also found in wild-type TP53 and wild-type BCOR (14 cases / 15 cases). On the other hand, it was observed that for mutant TP53 or mutant BCOR the overall survival tends to be short, regardless of the positivity or negativity of the immune response. With this, it was demonstrated that the presence or absence of mutations in the TP53 and BCOR gene is useful as a genetic marker to select potential patients who benefit from treatment with the WT1 peptide vaccine. EXAMPLE 5 Utility of WT1 mRNA as a genetic marker - 1 Of the 42 cases of high-risk patients in Example 1 who did not respond to azacitidine, WT1 mRNA expression was confirmed in 40 cases, except for 2 cases that were non-responder cases attributed to adverse reactions of azacitidine. DNA extraction from peripheral blood v specimen quality assessment Peripheral blood and bone marrow fluid were collected from patients within 28 days before the start of WT1 peptide cocktail vaccine administration. RNA extraction and purification were done in 7 mL of whole blood or 0.5 mL of bone marrow fluid using the QIAcube fully automatic RNA purification apparatus (Qiagen N.V.). Reagents, tubes, etc. of the RNeasy mini Kit (Qiagen N.V.) and the sample were loaded according to the QIAcube user manual. The RNeasy-Mini-program was selected from the QIAcube Standard Program stored in QIAcube, and RNA was extracted. Analysis of WT1 mRNA expression Analysis of WT1 mRNA expression was performed using the Otsuka WT1 mRNA Measurement Kit II (OTSUKA Pharmaceutical Co., Ltd.). Thereafter, the reagents included in the kit were used unless otherwise specified. The concentration of the extracted RNA was adjusted to 50 ng / pL by adding ribonuclease-free water. A standard solution of WT1 / GAPDH mixed RNA was prepared as standard solution 1; Standard solution 1 was diluted 10 times with a standard solution diluent to prepare standard solution 2, and the 10-fold dilution was repeated to prepare up to standard solution 5. A mixture of 10 pL was used as the reaction solution. of a mixture for RTPCR (Rl) and 5 pL of a metal ion solution at this ratio per reaction. A real-time PCR apparatus (Applied Biosystems 7500 Fast Dx, Applied Biosystems) was used and the RT-PCR reaction was performed according to section 3. Measurement operation of the protocol included in the kit. The measurement values ​​of WT1 mRNA and GSDPH mRNA in the sample were calculated using a calibration curve prepared from standard solutions 1 to 5. The level of WT1 mRNA expression was calculated according to section 4. Method for calculating WT1 mRNA expression level of the protocol included in the kit, as follows. Specifically, as shown in the expression given below, the expression degree of WT1 mRNA was calculated by multiplying the value obtained by dividing the measurement value of WT1 mRNA by the measurement value of GAPDH mRNA (copy number of WTl mRNA per copy of GAPDH mRNA) by the average number of copies of GAPDH mRNA per pg of RNA in healthy adult humans (degree of GAPDH mRNA expression). An average measurement value of GAPDH mRNA per pg RNA in healthy adult humans is 2.7 x 107 (copies / pg RNA). Expression 3 WTl mRNA measurement value Level of mRNA expression=--------------(co^mL)-------------- *χ (cOp¡as / pg RNA) WTl (copies / pg RNA) GAPDH mRNA measurement value}(copies / mL) Results (1) The results of WTl mRNA expression analysis are shown in Figure 4. WTl mRNA expression was found in the peripheral blood in all cases among the 40 cases. The mOS of cases whose WTl mRNA expression degree was less than 10,000 copies / pg RNA tends to be longer compared to the mOS of cases whose WTl mRNA expression degree was 10,000 copies / pg RNA or elderly. For the 27 cases whose WTl mRNA expression level was less than 10,000 copies / pg RNA and 13 cases whose WTl mRNA expression level was 10,000 copies / pg RNA or greater, an antigenic peptide-specific immune response was confirmed. WTl by the HLA tetramer assay mentioned below and the late-type hypersensitivity reaction. The results of the comparison of survival periods (OS) and WTl antigenic peptide-specific immune response for the degree of WTl mRNA expression are shown in Figure 5. The results shown in Figure 5 are about 25 cases whose degree of expression of WTl mRNA was less than 10,000 copies / pg RNA and 11 cases whose degree of expression of WTl mRNA was 10,000 copies / pg RNA or greater, except 4 cases for which the determination of the specific immune response to WTl antigenic peptide was impossible. It was observed that for the group whose level of WTl mRNA expression was less than 10,000 copies / pg RNA, the OS in cases where a specific immune response to WTl antigenic peptide was found tends to be long. On the other hand, no OS difference was observed between the positivity and negativity of the WTl antigenic peptide-specific immune response in the group whose WTl mRNA expression level was 10,000 copies / pg RNA or higher. It was also confirmed that the degree of WTl mRNA expression in peripheral blood and the degree of WTl mRNA expression in bone marrow fluid are correlated, and similar trends were also observed in bone marrow fluid (Figure 16). Results (2) The results of WT1 mRNA expression analysis are shown in Figure 6. In all 40 cases, WT1 mRNA expression was found in peripheral blood. The mOS of cases whose WT1 mRNA expression level was less than 4000 copies / pg RNA tends to be long compared with the mOS of cases whose WT1 mRNA expression level was 4000 copies / pg RNA or higher . For 22 cases whose WT1 mRNA expression level was less than 4000 copies / pg RNA and 18 cases whose WT1 mRNA expression level was 4000 copies / pg RNA or greater, a WT1 antigenic peptide-specific immune response was confirmed. by the HLA tetramer assay mentioned below and the late-type hypersensitivity reaction. The results of the comparison of survival times (OS) and WT1 antigenic peptide-specific immune response for the degree of WT1 mRNA expression are shown in Figure 7. The results shown in Figure 7 are about 21 cases whose degree of expression of WT1 mRNA was less than 4000 copies / pg RNA and 15 cases whose degree of expression of WT1 mRNA was 4000 copies / pg RNA or greater, except 4 cases for which the determination of the specific immune response to WT1 antigenic peptide was impossible. It was observed that for the group whose WT1 mRNA expression level was less than 4000 copies / pg RNA, the OS in cases where WT1 antigenic peptide-specific immune response was found tends to be long. On the other hand, no OS difference was observed between the positivity and negativity of the WT1 antigenic peptide-specific immune response in the group whose WT1 mRNA expression level was 4000 copies / pg RNA or higher. It was also confirmed that the degree of WT1 mRNA expression in peripheral blood and the degree of WT1 mRNA expression in bone marrow fluid are correlated, and similar trends were also observed in bone marrow fluid (Figure 16). Thus, the degree of WT1 mRNA expression was shown to be useful as a genetic marker to select potential patients who would benefit from treatment with the WT1 peptide vaccine. It was also shown that both 10000 copies / pg RNA and 4000 copies / pg RNA are useful as marker reference values. EXAMPLE 6 Detection of WT1 Antigenic Peptide-Specific Immune Response by HLA Tetramer Assay Measurement of the proportion of WT1 antigenic peptide-specific CD8 T cells among lymphocytes or among CD8-positive lymphocytes was carried out by a flow cytometry method using a tetramer reagent for blood collected from patients before and after administration of the vaccine. WT1 peptide cocktail. Administration and blood collection The 42 high-risk patient cases from Example 1 who did not respond to azacitidine were tested. The breakdown of the 42 cases with respect to HLA type was 10 cases of myelodysplastic syndrome (MDS) patients HLA-A*02:01- or HLA-A*02:06-positive, 25 cases of MDS patients HLA- A*24:02-positive, 5 cases of MDS patients HLA-A*02:01-positive and HLAA*24:02-positive, and 2 cases of MDS patients HLA-A*02:06-positive and HLA-A *24:02-positive. Peripheral blood collection from the patients and the test were done within 28 days before the start of administration of the pharmaceutical composition, 15 days after the second administration, 15 days after the sixth administration, 15 days after the twelfth administration, 15 days after the eighteenth administration, subsequently 15 days after administration of every 6th dose and within 28 days after the final administration. For administration, the patient was administered 1.75 mg, 3.5 mg, or 10.5 mg of the WT1 peptide cocktail vaccine per dose. HLA tetramer reagent Since WT1 antigenic peptide-specific CD8 T cells are HLA-restricted, the measurement was done using a tetramer reagent compatible with the patients' HLA. For HLA-A*24:02-positive patients, an HLA-A*24:02 tetramer was used (T-Select HLA-A*24:02 WTl(mutant)Tetramer-CYTWNQMNL PE-labeled, Medical & Biological Laboratories Co., Ltd.) labeled with the fluorescent dye phycoerythrin (PE), prepared using a peptide consisting of CYTWNQMNL (SEQ ID NO: 4) from the WT1 protein. Hereinafter, this reagent is also referred to as PE-labeled WT1 2402. For HLA-A*02:01- or HLA-A*02:06-positive patients, an HLAA*02:01 tetramer (T-Select HLA-A*02:01 WTI126-134 Tetramer-RMFPNAPYL-APC) was used. , Medical & Biological Laboratories Co., Ltd., capable of detecting both HLA-A*02:01 and HLA-A*02:06) labeled with the fluorescent dye allophycocyanin (APC), prepared using a peptide consisting of RMFPNAPYL ( SEQ ID NO: 2) of the WT1 protein, and a tetramer of HLA-A*02:01 in which a peptide consisting of VLDFAPPGA (SEQ ID NO: 9) of the WT1 protein was labeled with the fluorescent dye phycoerythrin ( PE) (HLA-A*02:01 Tetramer-VLDFAPPGA-PE, produced by Medical & Biological Laboratories Co., Ltd., capable of detecting both HLA-A*02:01 and HLA-A*02:06) . Hereinafter, the first reagent is also referred to as WT1 0201 labeled with APC and the second reagent is also referred to as WT1 0201 labeled with PE. Tetramer reagents were placed in microtubes before use and centrifuged at 1620 × g at room temperature for 5 minutes, and the supernatants were used. Dialing Labeling of patient subjects who have HLA-A*24:02 was performed as follows: 2.5 mL of the drawn blood was placed in a sample tube and the remaining amount was placed in a control tube. 5 pL of PE-labeled WT1 2402 was added to the sample tube. After reaction at room temperature for 10 minutes in the dark, 15 pL of FITC-labeled CD8 (CytoStat / Coulter Clone T8-FITC, Beckman Coulter K.K.) and 12.5 pL each of 7-AAD ( 7-AAD Staining Solution, Nippon Becton Dickinson Co., Ltd.), CD4 labeled with PC5 (IO Test CD4-PC5, Beckman Coulter K.K.) and CD19 labeled with PC5 (IO Test CD19-PC5, Beckman Coulter K.K.), and they waved. After reaction at room temperature for 15 minutes, 26 mL of a prepared lysis solution (BD FACSTM Lysing solution (Nippon Becton Dickinson Co., Ltd.) diluted 10 times with purified water) was added and shaken, leaving it to rest at room temperature for 15 minutes. 10 minutes; then it was centrifuged at 300 x g for 5 minutes. The supernatant was removed by suction with an aspirator and after shaking, 30 mL of PBS with azide (PBS containing 1% sodium azide) was added to each tube and centrifuged at 300 x g for 5 minutes. After removing the supernatant by suction with an aspirator, the resulting product was resuspended in 300 μL of a prepared cell fixation solution (BD FACS Cell Fix, Nippon Becton Dickinson Co., Ltd.) and transferred to a tube for measurement. . Labeling of patient subjects who have HLA-A*02:01 or HLA-A*02:06 was performed as follows: 2.5 mL of the drawn blood was placed in a sample tube and the remaining amount was placed in a control tube. 5 pL each of APC-labeled WT1 0201 and PE-labeled WT1 0201 were added to the sample tube. After reaction at room temperature for 10 minutes in the dark, 15 pL of FITC-labeled CD8 and 12.5 pL each of 7-AAD, APC-H7-labeled CD3 were added to the sample tube. , Nippon Becton Dickinson Co., Ltd.), CD4 labeled with Pacific Blue (lOTest CD4-Pacific Blue, Beckman Coulter K.K.) and CD19 labeled with PE-Cy7 (lOTest CD19-PC7, Beckman Coulter K.K.), and shaken. After reaction at room temperature for 15 minutes, 26 mL of a prepared lysis solution was added and shaken carefully. The resulting product was allowed to stand at room temperature for 10 minutes and then centrifuged at 300 x g for 5 minutes. The supernatant was removed by suction with an aspirator and after shaking, 30 mL of PBS with azide was added to each tube and centrifuged at 300 x g for 5 minutes. After removing the supernatant by suction with an aspirator, the resulting product was resuspended in 300 μL of a prepared cell fixation solution and transferred to a tube for measurement. The labeling of the patient subjects that have both HLA-A*24:02 and HLAA*02:01 or HLA-A*02:06 was carried out using both operations of marking the patient subjects that have HLA-A*24: 02 and the marking of patient subjects who have HLA-A*02:01 or HLAA*02:06. Flow cytometry analysis Measurement of the proportion of WT1 antigenic peptide-specific CD8 T cells among lymphocytes or among CD8-positive lymphocytes was carried out by a flow cytometry method. Samples prepared as described above were measured on a FACS Canto II flow cytometer (BD Biosciences). In the flow cytometer, scattered light is generated (forward scatter light (FSC) that reflects the size and side scattered light (SSC) that reflects the internal structure) that have intensity according to the characteristics of the cells (size and structure). internal) and fluorescence that depends on the amount of labeled antibody bound. The intensity of these parameters was measured for individual cells in the samples. A particular population can be calculated by converting the distribution of individual cells into a graph, based on the intensity obtained from the parameters. Lymphocyte fractions corresponding to lymphocytes of the size and internal structure of the cells were extracted and were negative for the anti-CD4 antibody / anti-CD19 / 7-AAD antibody labeling solution and positive only for the antiCD8 antibody (patient subjects who have HLA-A*02:01 or HLA-A*02:06) or positive for both anti-CD3 antibody and anti-CD8 antibody (patient subjects who have HLA-A*02:01 / 06), and in The fractions were evaluated as the fraction of tetramer-positive lymphocytes or the fraction of tetramer-positive CD8-positive cells. A framework for the population of FITC-labeled CD8 positive and PE-labeled WT1 2402 positive cells with 103on the K axis (CD8(+)tet(+) framework) was established as a guide. A framework for the population of FITC-labeled CD8 positive and PE-labeled WT1 0201 positive cells with 3 x 102 on the K axis (CD8(+)tet(+) framework) was established as a guide. A framework for the population of FITC-labeled CD8 positive and APC-labeled WT1 0201 positive cells with 3 x 102 on the K axis (CD8(+)tet(+) framework) was established as a guide. For HLA-A*24:02 patients, when an event was found in the CD8(+)tet(+) frame before administration of the WT1 peptide cocktail vaccine, the proportions of WT1 24:02 cells were compared. PE-labeled positive cells with strongly CD8 positive lymphocytes, before and after administration of the WT1 peptide cocktail vaccine, as denominators. When no event was found in the CD8(+)tet(+) frame before administration, the number of events in the CD8(+)tet(+) frame after administration was calculated. For HLA-A*02:01 or HLA-A*02:06 patients, when an event was found in the CD8(+)tet(+) setting before administration of the WT1 peptide cocktail vaccine, we compared The proportions of PE-labeled WT1 2:1 or 2:6 positive cells and APC-labeled WT1 2:1 or 2:6 positive cells with strongly CD8 positive lymphocytes, before and after administration of the WT1 peptide cocktail vaccine , as denominators. When no event was found in the CD8(+)tet(+) frame before administration, the number of events in the CD8(+)tet(+) frame after administration was calculated. A baseline was established to determine whether the WT1 antigenic peptide-specific immune response was positive or negative according to the HLA tetramer assay, as follows. When positivity or maintenance was determined at any time point after administration, the determination according to the HLA tetramer assay was positivity or maintenance. When negativity was determined at all time points after administration, the determination according to the HLA tetramer assay was negativity. TABLE 3 When no cells were found in the frame CD8+tet+ before administration CD8+tet+ tet+ / CD8+ after administration with respect to before administration Determination according to the tetramer assay > 10 - Positivity < 10 - Negativity When found cells in the frame CD8+tet+before administration CD8+tet+ tet+ / CD8+ after administration with respect to before administration Determination according to the tetramer assay > 10 > 2 times Positivity > 10 More than 1 / 2 times - less than 2 times Maintenance > 10 1 / 2 times > Negativity < 10 - Negativity Results As a result of the determination in the 47 cases based on the reference, 30 cases (63.8%) were determined positive in the determination by the tetramer assay, 3 cases (6.4%) remained in the determination by the HLA tetramer assay and 13 cases (27.7%) negative in the determination using the HLA tetramer assay. For 1 case (2.1%), determination by the HLA tetramer assay was impossible. EXAMPLE 7 Detection of a delayed hypersensitivity reaction (DTH) Preparation of drug solution for DTH 2 mL of injectable water and 1.8 mL of injectable water were added to 20 mg of the WT1 killer peptide conjugate and 18 mg of the WT1 helper peptide, respectively, of the WT1 peptide cocktail vaccine shown in Example 1, to prepare a WT1 killer peptide conjugate solution (10 mg / mL) and a WT1 helper peptide solution (10 mg / mL). Additionally, each was diluted 10-fold (1 mg / mL) using lactated Ringer's solution. DTH drug solutions were used within 3 hours after preparation. Inoculation and measurement 100 pL (100 pg) of each of the two types of DTH drug solutions (WT1 killer peptide conjugate solution and WT1 helper peptide solution) were injected intradermally into the forearm of a patient, with a separation of 3 cm or greater. As a negative control, 100 pL of a lactated Ringer's solution (control solution) was injected intradermally on the same side of the forearm, with a separation of 3 cm or greater from the administration sites of the DTH drug solutions. Two days after administration, the diameters of the redness [major axis, minor axis and properties (double redness, hardening, ulcer, etc.)] were measured. The difference between the major reddening axis of the control solution and the major reddening axis of the WT1 killer peptide conjugate solution or the WT1 helper peptide solution was calculated, and the DTH reaction was scored from the difference according to the following table. TABLE 4 Diameter difference of redness Score Less than 2 mm 0 2 mm or greater and less than 5 mm + / - 5 mm or greater and less than 10 mm 1 10 mm or greater and less than 15 mm 2 Greater than 15 mm 3 The DTH test was performed before the start of administration of the WT1 peptide cocktail vaccine (within 28 days before administration), 2 days after the second administration, 2 days after the twelfth administration and after final administration (within 28 days after administration). DTH reaction scores were determined based on the reference. The maximum score of each case after administration was subjected to subsequent analysis. Results As a result of determining scores for the 47 cases, based on the reference, 11 cases (23.4%) were given a score of 0, 4 cases (8.5%) were given a score + / -, 9 cases (19.1%) were given a score of 1, 4 cases (8.5%) were given a score of 2, 9 cases (19.1%) were given a score of 3; The patients for whom score determination was impossible were 7 cases (14.9%) and the patients for whom the DTH test could not be performed were 3 cases (6.4%). EXAMPLE 8 Establishment of a reference to classify the positivity or neqativity of the WT1 antigenic peptide-specific immune response For the WT1 antigenic peptide-specific immune response induced by the WT1 peptide cocktail vaccine, a reference was established to classify the positivity or negativity of the WT1 antigenic peptide-specific immune response by making a bidirectional analysis of the HLA tetramer assay results. and the maximum score of the DTH test using the WT1 killer peptide conjugate. Since this example was aimed at the complete determination of the WT1 antigenic peptide-specific immune response, a total of 47 cases, 42 high-risk cases and also 5 low-risk cases described in Example 1, were used as subjects for analysis. However, among them, 1 case for which the determination of the HLA tetramer assay of example 6 was impossible, and 10 cases for which the determination of DTH scores was impossible or for which it was not possible, were excluded from this analysis. The DTH test of Example 7 could be performed. It was found that the majority of cases determined to be positive in HLA tetramer assay determination results also had a score of + / - or greater in DTH assay determination using WT1 killer peptide conjugate (left diagram of figure 8). It was also found that most of the cases that have a score less than + / - in the determination of the DTH test using the WT1 killer peptide conjugate, were determined as negative in the HLA tetramer assay (right diagram of the figure 8). From these results, the positions indicated by the respective arrows in the right diagram and left diagram of Figure 8 were established as positive references for the WT1 antigenic peptide-specific immune response. Specifically, when the results of the HLA tetramer assay determination are positive, or the DTH test determination using WT1 killer peptide conjugate is a score of + / - or greater (difference from control is 2 mm or more), the WT1 antigenic peptide-specific immune response caused by the WT1 peptide cocktail vaccine can be determined to be positive. On the other hand, when the results of the determination of the HLA tetramer assay are maintenance or negativity, and the determination of the DTH test using the WT1 killer peptide conjugate is 0 (difference from the control is less than 2 mm), can determine that the WT1 antigenic peptide-specific immune response caused by the WT1 peptide cocktail vaccine is negative. When the 47 cases were qualified by the reference, it was determined that 33 cases (70.2%) were positive for the WT1 antigenic peptide-specific immune response and 9 cases (19.1%) were negative for the WT1 antigenic peptide-specific immune response. For 5 cases the determination was impossible because the DTH test was not performed or internal bleeding was observed due to the DTH test, thus, the specific immune response to WT1 antigenic peptide was unknown (10.7%). EXAMPLE 9 Analysis of WT1 antigenic peptide-specific immune response and clinical effect The relationship with the clinical effect was analyzed as follows for a total of 36 cases, 28 cases determined as positive for the specific immune response of WT1 antigenic peptide and 8 cases determined as negative for the same according to the reference of example 8 , among the 42 cases of high-risk patients who did not respond to azacitidine described in example 1. 2 cases were excluded from the analysis that were non-responder cases attributed to the adverse reactions of azacitidine, and 4 cases for which it was impossible determination of the WT1 antigenic peptide-specific immune response because the DTH test was not performed or internal bleeding was observed due to the DTH test. Myeloblast change The WT1 antigenic peptide-specific immune response and myeloblast change were analyzed. In the case of a Pre value change in the proportion of myeloblasts with a change of 150% or less at two or more time points up to approximately 3 months after initial administration (bone marrow fluid was removed approximately 15 days after of the second administration and / or approximately 15 days after the sixth administration in administration every 2 weeks), it was determined that gemmule stabilization was present. In the case of a change in the Pre value in the proportion of myeloblasts greater than 150%, it was determined that gemmule stabilization was absent (exacerbation). As shown in Figure 9, many cases where gemmules were stabilized for a long period were found in the group positive for the WT1 antigenic peptide-specific immune response. AML transition period Periods of transition to acute myeloid leukemia (AML) were compared based on the positivity or negativity of the WT1 antigenic peptide-specific immune response. As shown in Figure 10, the transition period to AML tends to be long in the WT1 antigenic peptide-specific immune response positive group. Survival curve Survival curves based on the positivity or negativity of the WT1 antigenic peptide-specific immune response were compared. As shown in Figure 11, the mOS of 28 cases positive for WT1 antigenic peptide-specific immune response tends to be long compared to the mOS of 8 cases negative for WT1 antigenic peptide-specific immune response. Myeloblast stabilization and survival curve As shown in Figure 9, in 8 cases negative for the WT1 antigenic peptide-specific immune response, myeloblast stabilization was found to be absent. On the other hand, in 28 cases positive for the specific immune response of WT1 antigenic peptide, stabilization of myeloblasts was found in 15 cases (53.6%). The mOS of cases that were positive for the WT1 antigenic peptide-specific immune response and have myeloblast stabilization tended to be longer. Karyotype and survival curve Thirty-five cases, except 1 case whose karyotype was unknown, were classified based on IPSS-R karyotype, and the WT1 antigenic peptide-specific immune response and survival curves were compared. As shown in Figure 12, for the good / intermediate / bad groups, it was found that the mOS of the WT1 antigenic peptide-specific immune response positive group tends to be long compared with the peptide-specific immune response negative group. WT1 antigenic. Likewise, in the poor prognosis group with very poor karyotype, the mOS of the group positive for WT1 antigenic peptide-specific immune response tends to be longer than that of the group negative for WT1 antigenic peptide-specific immune response. Results Many cases were found in which myeloblasts were stabilized and a prolongation of the transition period to AML was found in the WT1 antigenic peptide-specific immune response-positive group, compared to the WT1 antigenic peptide-specific immune response-negative group. . Also, the tendency to prolong mOS was observed. The possibility suggested that a specific immune response of WT1 antigenic peptide was induced, whereby the myeloblasts were stabilized and, along with this, the prolongation of the transition period to AML and the survival period was found. When performing a stratified analysis on the good prognosis group and the poor prognosis group of karyotype, the tendency to prolong mOS was also observed. EXAMPLE 10 Analysis by sex difference The median survival time for each sex difference was compared to historical data and the median BSC survival time from a trial of rigosertib, for 40 cases of the 42 high-risk patient cases from Example 1 who did not respond to the test. azacitidine, except 2 cases that were non-responders attributable to adverse reactions of azacitidine. As shown in Table 5, many cases determined to be positive for the WT1 antigenic peptide-specific immune response were found in men. As a result of the comparison with historical data (Prebet et al., Journal of Clínica / Oncology 29, no. 24, 3322-3327) and a control (BSC of the rigosertib trial) in the ONTIME trial of rigosertib (Garcia- Manero et al., The Lancet Oncology 17, no. 4, p. 496-508 (2016)), as shown in Figure 13, the WT1 peptide cocktail vaccine was found to prolong OS in men more than in women, suggesting the possibility that the effect is high. TABLE 5 WT1 peptide cocktail vaccine trial Men Women Total Number of cases (%) 31 (77.5%) 9 (22.5%) 40 Immune response Positive: 26 (83.9%) Positive: 2 (22.2%) Positive: 28 (70%) Negative: 4 (12.9%) Negative: 4 (44.4%) Negative: 8 (20%) Impossible determination: 1 (3.2%) Impossible determination: 3 (33.3%) Impossible determination: 4 (10%) EXAMPLE 11 Utility of WT1 mRNA as a genetic marker - 2 WT1 mRNA expression was confirmed in 40 cases of the 42 high-risk patient cases of Example 1 who did not respond to azacitidine, except for 2 cases that were non-responder cases attributable to adverse reactions of azacitidine. DNA extraction from peripheral blood and specimen quality assessment Peripheral blood and bone marrow fluid were collected from patients within 28 days before the start of WT1 peptide cocktail vaccine administration. RNA extraction and purification were done in 7 mL of whole blood or 0.5 mL of bone marrow fluid using the QIAcube fully automatic RNA purification apparatus (Qiagen N.V.). Reagents, tubes, etc. of the RNeasy mini Kit (Qiagen N.V.) and the sample were loaded according to the QIAcube user manual. The RNeasy-Mini-program was selected from the QIAcube Standard Program stored in QIAcube, and RNA was extracted. Analysis of WT1 mRNA expression Analysis of WT1 mRNA expression was performed using the Otsuka WT1 mRNA Measurement Kit II (OTSUKA Pharmaceutical Co., Ltd.). Hereinafter, the reagents included in the kit were used, unless otherwise specified. The concentration of the extracted RNA was adjusted to 50 ng / pL with the addition of ribonuclease-free water. A mixed WT1 / GAPDH RNA standard solution was prepared as standard solution 1; Standard solution 1 was diluted 10 times with a standard solution diluent to prepare standard solution 2, and the 10-fold dilution was repeated to prepare up to standard solution 5. A mixture of 10 pL was used as the reaction solution. of a mixture for RTPCR (Rl) and 5 pL of a metal ion solution at this ratio per reaction. A real-time PCR apparatus (Applied Biosystems 7500 Fast Dx, Applied Biosystems) was used and the RT-PCR reaction was performed according to section 3. Measurement operation of the protocol included in the kit. The measurement values ​​of WT1 mRNA and GSDPH mRNA in the sample were calculated using a calibration curve prepared from standard solutions 1 to 5. The level of WT1 mRNA expression was calculated according to section 4. Method for calculating WT1 mRNA expression level of the protocol included in the kit, as follows. Specifically, as shown in the expression given below, the expression degree of WT1 mRNA was calculated by multiplying the value obtained by dividing the measurement value of WT1 mRNA by the measurement value of GAPDH mRNA (copy number of WT1 mRNA per copy of GAPDH mRNA) by the average number of copies of GAPDH mRNA per pg of RNA in healthy adult humans (degree of GAPDH mRNA expression). An average measurement value of GAPDH mRNA per pg of RNA in healthy adult humans is 2.7 x 107 (copies / pg RNA). Expression 4 WT1_mRNA measurement value. . ., . . (copies / mL) · Degree of mRNA expression of=---------------í---------------χ 2 7 χ 10? (copies / pg RNA) WT1 (copies / pg RNA) GAPDH mRNA measurement value}(copies / mL) In Figure 14 the results of the WT1 mRNA expression analysis are shown. WT1 mRNA expression was found in peripheral blood in all cases among the 40 cases. The mOS of cases whose WT1 mRNA expression level was 10,000 copies / pg RNA or less tends to be long compared with the mOS of cases whose WT1 mRNA expression level was greater than 10,000 copies / pg RNA . For the 30 cases whose WT1 mRNA expression level was 10,000 copies / pg RNA or less and 10 cases whose WT1 mRNA expression level was greater than 10,000 copies / pg RNA, an antigenic peptide-specific immune response was confirmed. WT1 by means of the aforementioned HLA tetramer assay and the late-type hypersensitivity reaction. The results of the comparison of survival times (OS) and WT1 antigenic peptide-specific immune response for the degree of WT1 mRNA expression are shown in Figure 15. The results shown in Figure 15 are about 28 cases whose degree of expression of WT1 mRNA was 10,000 copies / pg RNA or less and 8 cases whose degree of expression of WT1 mRNA was greater than 10,000 copies / pg RNA, except 4 cases for which determination of the WT1 antigen peptide-specific immune response was impossible. With this, it was demonstrated that the level of WT1 mRNA expression is useful as a genetic marker to select potential patients who benefit from treatment with the WT1 peptide vaccine. 10,000 copies / pg RNA was also shown to be useful as a marker reference value. It was shown, for the group whose WT1 mRNA expression level was 1000 copies / pg RNA or lower, the OS of cases where a WT1 antigenic peptide-specific immune response was found tends to be long. On the other hand, no OS difference was observed between the positivity and negativity of the WT1 antigenic peptide-specific immune response in the group whose level of WT1 mRNA expression was greater than 10,000 copies / pg RNA. It was also confirmed that the degree of WT1 mRNA expression in peripheral blood and the degree of WT1 mRNA expression in bone marrow fluid are correlated, and similar trends were also observed in bone marrow fluid (Figure 16).

Claims

1. A method for selecting a potential subject to benefit from a pharmaceutical composition useful for treating or preventing cancer, comprising: determining the presence or absence of a mutation in the p53 tumor protein gene (TP53) and / or the BCL6 corepressor gene (BCOR) using a sample taken from the subject;and provide an indication that the subject is a potential beneficiary of the pharmaceutical composition in the case of wild-type TP53 and / or wild-type BCOR, wherein the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7), VLDFAPPGA (SEQ ID NO: 9), CMTWNQMNL (SEQ ID NO: 3), CYTWNQMNL (SEQ ID NO: 4), CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.; 2. The method according to claim 1, further characterized in that the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), or a pharmaceutically acceptable salt thereof. 3 - The method according to claim 1 or 2, further characterized in that the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof.

4. The method according to any of claims 1 to 3, further characterized in that the pharmaceutical composition comprises a peptide comprising an amino acid sequence selected from the group consisting of RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), and a peptide comprising an amino acid sequence selected from the group consisting of CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), or a pharmaceutically acceptable salt thereof.

5. The method according to any one of claims 1 to 4, further characterized in that the pharmaceutical composition comprises a compound represented by formula (1): Tumor antigenic peptide A rOH (1) wherein Xa and Ya represent a single bond, the tumor antigenic peptide A represents a peptide consisting of any of the amino acid sequences selected from the following amino acid sequences: RMFPNAPYL (SEQ ID NO: 2), YMFPNAPYL (SEQ ID NO: 8), ALLPAVPSL (SEQ ID NO: 5), SLGEQQYSV (SEQ ID NO: 6), RVPGVAPTL (SEQ ID NO: 7) and VLDFAPPGA (SEQ ID NO: 9), the amino group of the N-terminal amino acid of the tumor antigenic peptide A is attached to Ya of formula (1), the carbonyl group of the C-terminal amino acid of the tumor antigenic peptide A is attached to the hydroxyl group of formula (1), R1 represents a hydrogen atom or a tumor antigenic peptide B,Tumor antigenic peptide B differs in its sequence from tumor antigenic peptide A and represents a peptide consisting of any amino acid sequence selected from the following amino acid sequences: CMTWNQMNL (SEQ ID NO: 3) and CYTWNQMNL (SEQ ID NO: 4), and the thioether group of the cysteine ​​residue of tumor antigenic peptide B is attached to the thioether group of formula (1), or a pharmaceutically acceptable salt thereof.

6. The method according to claim 5, further characterized in that the compound represented by formula (1) is a compound represented by formula (2): CRMFPNAPYL CMTWNQMNL (2) wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof. 7.- The method according to claim 5, further characterized in that the compound represented by formula (1) is a compound represented by formula (3): CRMFPNAPYL I (3) CYTWNQMNL wherein the bond between C and C represents a disulfide bond, or a pharmaceutically acceptable salt thereof.

8. The method according to any of claims 1 to 7, further characterized in that the pharmaceutical composition further comprises a peptide comprising an amino acid sequence selected from the group consisting of CNKRYFKLSHLQMHSRK (SEQ ID NO: 11), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 12), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 13), WAPVLDFAPPGASAYGSL (SEQ ID NO: 14), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 15) and WAPVLDFAPPGASAYGSLC (SEQ ID NO: 16), or a pharmaceutically acceptable salt thereof.

9. The method in accordance with any of claims 1 to 8, further characterized in that the pharmaceutical composition comprises a pharmaceutically acceptable vehicle.

10. The method in accordance with any of claims 1 to 9, further characterized in that, in the case of wild-type TP53, an indication is provided that the subject is a potential subject to benefit from the pharmaceutical composition. 11.- The method in accordance with any of claims 1 to 10, further characterized in that in the case of wild type TP53 and wild type BCOR, an indication is provided that the subject is a potential subject to benefit from the pharmaceutical composition. 12.- The method according to any of claims 1 to 11, further characterized in that it additionally comprises: determining the degree of mRNA expression of the WT1 gene using a sample taken from the subject; and providing an indication that the subject is a potential beneficiary of the pharmaceutical composition when the degree of mRNA expression of the WT1 gene is less than a reference value or the reference value or less.

13. The method according to any of claims 1 to 12, further characterized in that it additionally comprises: detecting WT1 antigenic peptide-specific CD8 T cells using a sample taken from the subject to whom the pharmaceutical composition or the peptide or the pharmaceutically acceptable salt thereof is administered according to any of claims 1 to 9; and providing an indication that the subject is a potential beneficiary of the pharmaceutical composition when the WT1 antigenic peptide-specific CD8 T cells have been elevated compared to a sample taken from the subject prior to administration. 14.- The method according to claim 13, further characterized in that the detection of WT1 antigenic peptide-specific CD8 T cells is carried out by reacting a complex of a WT1 peptide and an HLA molecule with the sample, and examining the presence or number of WT1 antigenic peptide-specific CD8 T cells that recognize the complex contained in the sample.

15. The method according to claim 14, further characterized in that the complex of a WT1 peptide and an HLA molecule is in the form of a tetramer.

16. The method according to claim 14 or 15, further characterized in that the HLA molecule is compatible with the subject's HLA.

17. The method according to any of claims 13 to 16, further characterized in that the detection of WT1 antigenic peptide-specific CD8 T cells comprises an analysis by a flow cytometry method.

18. The method according to any of claims 1 to 17, further characterized in that it additionally comprises providing an indication that the subject is a potential beneficiary of the pharmaceutical composition when a delayed-type hypersensitivity reaction is detected in the subject who is administered a plurality of times the pharmaceutical composition or the peptide or pharmaceutically acceptable salt thereof according to any of claims 1 to 9.

19. The method according to claim 18, further characterized in that it additionally comprises comparing the reaction at the site of administration of the pharmaceutical composition or the peptide or pharmaceutically acceptable salt thereof according to any of claims 1 to 9 in the subject, with the reaction at a site without administration of the pharmaceutical composition or the peptide or pharmaceutically acceptable salt thereof in the subject, and providing an indication that the subject is a potential beneficiary of the pharmaceutical composition when the difference between the reaction at the site of administration and the reaction at a site without administration is a reference value or greater.