CA2548135C - Synthetic hla binding peptide analogues and uses thereof - Google Patents
Synthetic hla binding peptide analogues and uses thereof Download PDFInfo
- Publication number
- CA2548135C CA2548135C CA2548135A CA2548135A CA2548135C CA 2548135 C CA2548135 C CA 2548135C CA 2548135 A CA2548135 A CA 2548135A CA 2548135 A CA2548135 A CA 2548135A CA 2548135 C CA2548135 C CA 2548135C
- Authority
- CA
- Canada
- Prior art keywords
- seq
- cells
- cancer
- peptide
- human
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 346
- 206010028980 Neoplasm Diseases 0.000 claims abstract description 77
- 201000011510 cancer Diseases 0.000 claims abstract description 66
- 230000002163 immunogen Effects 0.000 claims abstract description 33
- 230000028993 immune response Effects 0.000 claims abstract description 32
- 239000000203 mixture Substances 0.000 claims abstract description 26
- 239000008194 pharmaceutical composition Substances 0.000 claims abstract description 20
- 230000001991 pathophysiological effect Effects 0.000 claims abstract description 10
- 241000124008 Mammalia Species 0.000 claims abstract description 9
- 210000004027 cell Anatomy 0.000 claims description 130
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 45
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 claims description 41
- 210000002865 immune cell Anatomy 0.000 claims description 36
- 208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 claims description 28
- 208000010833 Chronic myeloid leukaemia Diseases 0.000 claims description 27
- 208000033761 Myelogenous Chronic BCR-ABL Positive Leukemia Diseases 0.000 claims description 27
- 108090000623 proteins and genes Proteins 0.000 claims description 22
- 230000015572 biosynthetic process Effects 0.000 claims description 21
- 230000001939 inductive effect Effects 0.000 claims description 21
- 150000001413 amino acids Chemical class 0.000 claims description 20
- 230000035755 proliferation Effects 0.000 claims description 20
- 102000004169 proteins and genes Human genes 0.000 claims description 20
- 210000000612 antigen-presenting cell Anatomy 0.000 claims description 19
- 208000032839 leukemia Diseases 0.000 claims description 19
- 210000004443 dendritic cell Anatomy 0.000 claims description 18
- 108700020467 WT1 Proteins 0.000 claims description 14
- 102000040856 WT1 Human genes 0.000 claims description 14
- 230000001684 chronic effect Effects 0.000 claims description 12
- 206010025323 Lymphomas Diseases 0.000 claims description 11
- 206010027406 Mesothelioma Diseases 0.000 claims description 11
- 206010061535 Ovarian neoplasm Diseases 0.000 claims description 11
- 208000024313 Testicular Neoplasms Diseases 0.000 claims description 11
- 238000001727 in vivo Methods 0.000 claims description 11
- 208000020816 lung neoplasm Diseases 0.000 claims description 11
- 206010006187 Breast cancer Diseases 0.000 claims description 9
- 208000026310 Breast neoplasm Diseases 0.000 claims description 9
- 206010058467 Lung neoplasm malignant Diseases 0.000 claims description 9
- 206010033128 Ovarian cancer Diseases 0.000 claims description 9
- 206010057644 Testis cancer Diseases 0.000 claims description 9
- 239000003937 drug carrier Substances 0.000 claims description 9
- 201000005202 lung cancer Diseases 0.000 claims description 9
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 claims description 9
- 201000003120 testicular cancer Diseases 0.000 claims description 9
- 239000013598 vector Substances 0.000 claims description 9
- 239000002671 adjuvant Substances 0.000 claims description 7
- 230000003213 activating effect Effects 0.000 claims description 6
- 239000003085 diluting agent Substances 0.000 claims description 6
- 108010088751 Albumins Proteins 0.000 claims description 5
- 102000009027 Albumins Human genes 0.000 claims description 5
- 239000002253 acid Substances 0.000 claims description 5
- 210000002798 bone marrow cell Anatomy 0.000 claims description 5
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 claims description 5
- 210000002540 macrophage Anatomy 0.000 claims description 5
- 230000006698 induction Effects 0.000 claims description 4
- 238000004519 manufacturing process Methods 0.000 claims description 4
- 230000004913 activation Effects 0.000 claims description 2
- 239000003814 drug Substances 0.000 claims description 2
- 238000001802 infusion Methods 0.000 claims 3
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 141
- 238000000034 method Methods 0.000 abstract description 28
- 102100022748 Wilms tumor protein Human genes 0.000 description 44
- 210000001744 T-lymphocyte Anatomy 0.000 description 36
- 101000621309 Homo sapiens Wilms tumor protein Proteins 0.000 description 26
- 230000004044 response Effects 0.000 description 25
- 235000001014 amino acid Nutrition 0.000 description 22
- 108020004414 DNA Proteins 0.000 description 16
- 239000000427 antigen Substances 0.000 description 16
- 235000018102 proteins Nutrition 0.000 description 16
- 108010088729 HLA-A*02:01 antigen Proteins 0.000 description 15
- 108091007433 antigens Proteins 0.000 description 14
- 102000036639 antigens Human genes 0.000 description 14
- 238000003556 assay Methods 0.000 description 14
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 12
- 239000002953 phosphate buffered saline Substances 0.000 description 12
- 230000003053 immunization Effects 0.000 description 11
- 108010074328 Interferon-gamma Proteins 0.000 description 10
- 238000006467 substitution reaction Methods 0.000 description 10
- WEVYNIUIFUYDGI-UHFFFAOYSA-N 3-[6-[4-(trifluoromethoxy)anilino]-4-pyrimidinyl]benzamide Chemical compound NC(=O)C1=CC=CC(C=2N=CN=C(NC=3C=CC(OC(F)(F)F)=CC=3)C=2)=C1 WEVYNIUIFUYDGI-UHFFFAOYSA-N 0.000 description 9
- 102000008070 Interferon-gamma Human genes 0.000 description 9
- 238000003114 enzyme-linked immunosorbent spot assay Methods 0.000 description 9
- 229940044627 gamma-interferon Drugs 0.000 description 9
- 230000005847 immunogenicity Effects 0.000 description 9
- 230000000638 stimulation Effects 0.000 description 9
- 238000002649 immunization Methods 0.000 description 8
- 108010056708 bcr-abl Fusion Proteins Proteins 0.000 description 7
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 7
- 102000037865 fusion proteins Human genes 0.000 description 7
- 108020001507 fusion proteins Proteins 0.000 description 7
- 230000001976 improved effect Effects 0.000 description 7
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 6
- 108091054437 MHC class I family Proteins 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 102000004441 bcr-abl Fusion Proteins Human genes 0.000 description 6
- 201000010099 disease Diseases 0.000 description 6
- 238000011534 incubation Methods 0.000 description 6
- 210000001616 monocyte Anatomy 0.000 description 6
- 230000006641 stabilisation Effects 0.000 description 6
- 238000011105 stabilization Methods 0.000 description 6
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 5
- 101150049556 Bcr gene Proteins 0.000 description 5
- 210000001266 CD8-positive T-lymphocyte Anatomy 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 239000011159 matrix material Substances 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- 239000002243 precursor Substances 0.000 description 5
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 4
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 4
- 102000008949 Histocompatibility Antigens Class I Human genes 0.000 description 4
- 230000000890 antigenic effect Effects 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 239000011230 binding agent Substances 0.000 description 4
- 230000002950 deficient Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 102000027450 oncoproteins Human genes 0.000 description 4
- 108091008819 oncoproteins Proteins 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 230000005945 translocation Effects 0.000 description 4
- 101000946889 Homo sapiens Monocyte differentiation antigen CD14 Proteins 0.000 description 3
- 108010002350 Interleukin-2 Proteins 0.000 description 3
- 102000004388 Interleukin-4 Human genes 0.000 description 3
- 108090000978 Interleukin-4 Proteins 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- 102000043129 MHC class I family Human genes 0.000 description 3
- 102100035877 Monocyte differentiation antigen CD14 Human genes 0.000 description 3
- 230000005867 T cell response Effects 0.000 description 3
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 3
- 102000003425 Tyrosinase Human genes 0.000 description 3
- 108060008724 Tyrosinase Proteins 0.000 description 3
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000009089 cytolysis Effects 0.000 description 3
- 238000002784 cytotoxicity assay Methods 0.000 description 3
- 231100000263 cytotoxicity test Toxicity 0.000 description 3
- 238000013461 design Methods 0.000 description 3
- 238000010494 dissociation reaction Methods 0.000 description 3
- 230000005593 dissociations Effects 0.000 description 3
- 230000009851 immunogenic response Effects 0.000 description 3
- 230000002147 killing effect Effects 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 201000001441 melanoma Diseases 0.000 description 3
- 238000009738 saturating Methods 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 229960005486 vaccine Drugs 0.000 description 3
- 239000004474 valine Substances 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- 208000024893 Acute lymphoblastic leukemia Diseases 0.000 description 2
- 208000014697 Acute lymphocytic leukaemia Diseases 0.000 description 2
- 102100030346 Antigen peptide transporter 1 Human genes 0.000 description 2
- 102100040501 Contactin-associated protein 1 Human genes 0.000 description 2
- 102100028967 HLA class I histocompatibility antigen, alpha chain G Human genes 0.000 description 2
- 101710197836 HLA class I histocompatibility antigen, alpha chain G Proteins 0.000 description 2
- 108010002586 Interleukin-7 Proteins 0.000 description 2
- 102000000704 Interleukin-7 Human genes 0.000 description 2
- 108010063738 Interleukins Proteins 0.000 description 2
- 102000015696 Interleukins Human genes 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 108010010995 MART-1 Antigen Proteins 0.000 description 2
- 108010023335 Member 2 Subfamily B ATP Binding Cassette Transporter Proteins 0.000 description 2
- 108010057081 Merozoite Surface Protein 1 Proteins 0.000 description 2
- 241000699660 Mus musculus Species 0.000 description 2
- 108091061960 Naked DNA Proteins 0.000 description 2
- 208000006664 Precursor Cell Lymphoblastic Leukemia-Lymphoma Diseases 0.000 description 2
- 239000012979 RPMI medium Substances 0.000 description 2
- 239000012980 RPMI-1640 medium Substances 0.000 description 2
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 108091008874 T cell receptors Proteins 0.000 description 2
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 2
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
- 239000000556 agonist Substances 0.000 description 2
- 102000015736 beta 2-Microglobulin Human genes 0.000 description 2
- 108010081355 beta 2-Microglobulin Proteins 0.000 description 2
- 210000000481 breast Anatomy 0.000 description 2
- KQNZDYYTLMIZCT-KQPMLPITSA-N brefeldin A Chemical compound O[C@@H]1\C=C\C(=O)O[C@@H](C)CCC\C=C\[C@@H]2C[C@H](O)C[C@H]21 KQNZDYYTLMIZCT-KQPMLPITSA-N 0.000 description 2
- JUMGSHROWPPKFX-UHFFFAOYSA-N brefeldin-A Natural products CC1CCCC=CC2(C)CC(O)CC2(C)C(O)C=CC(=O)O1 JUMGSHROWPPKFX-UHFFFAOYSA-N 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 229910052804 chromium Inorganic materials 0.000 description 2
- 239000011651 chromium Substances 0.000 description 2
- 210000000349 chromosome Anatomy 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 231100000433 cytotoxic Toxicity 0.000 description 2
- 230000001472 cytotoxic effect Effects 0.000 description 2
- 230000003013 cytotoxicity Effects 0.000 description 2
- 231100000135 cytotoxicity Toxicity 0.000 description 2
- 239000007857 degradation product Substances 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 206010022000 influenza Diseases 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- ZAHQPTJLOCWVPG-UHFFFAOYSA-N mitoxantrone dihydrochloride Chemical compound Cl.Cl.O=C1C2=C(O)C=CC(O)=C2C(=O)C2=C1C(NCCNCCO)=CC=C2NCCNCCO ZAHQPTJLOCWVPG-UHFFFAOYSA-N 0.000 description 2
- 230000009826 neoplastic cell growth Effects 0.000 description 2
- 210000001672 ovary Anatomy 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 210000005259 peripheral blood Anatomy 0.000 description 2
- 239000011886 peripheral blood Substances 0.000 description 2
- 210000004214 philadelphia chromosome Anatomy 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000002062 proliferating effect Effects 0.000 description 2
- 238000000159 protein binding assay Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 230000002269 spontaneous effect Effects 0.000 description 2
- 230000004936 stimulating effect Effects 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 230000002381 testicular Effects 0.000 description 2
- 210000001550 testis Anatomy 0.000 description 2
- 238000011830 transgenic mouse model Methods 0.000 description 2
- 238000011282 treatment Methods 0.000 description 2
- 102000003390 tumor necrosis factor Human genes 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- GHCZTIFQWKKGSB-UHFFFAOYSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;phosphoric acid Chemical compound OP(O)(O)=O.OC(=O)CC(O)(C(O)=O)CC(O)=O GHCZTIFQWKKGSB-UHFFFAOYSA-N 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 102100030343 Antigen peptide transporter 2 Human genes 0.000 description 1
- 208000003950 B-cell lymphoma Diseases 0.000 description 1
- 102100024222 B-lymphocyte antigen CD19 Human genes 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102100035793 CD83 antigen Human genes 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 1
- VYZAMTAEIAYCRO-BJUDXGSMSA-N Chromium-51 Chemical compound [51Cr] VYZAMTAEIAYCRO-BJUDXGSMSA-N 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 238000011510 Elispot assay Methods 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 108010074032 HLA-A2 Antigen Proteins 0.000 description 1
- 102000025850 HLA-A2 Antigen Human genes 0.000 description 1
- 108010013476 HLA-A24 Antigen Proteins 0.000 description 1
- 108010088652 Histocompatibility Antigens Class I Proteins 0.000 description 1
- 101000980825 Homo sapiens B-lymphocyte antigen CD19 Proteins 0.000 description 1
- 101000946856 Homo sapiens CD83 antigen Proteins 0.000 description 1
- 101000746373 Homo sapiens Granulocyte-macrophage colony-stimulating factor Proteins 0.000 description 1
- 101001043807 Homo sapiens Interleukin-7 Proteins 0.000 description 1
- 101000914484 Homo sapiens T-lymphocyte activation antigen CD80 Proteins 0.000 description 1
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 238000012404 In vitro experiment Methods 0.000 description 1
- 102100037850 Interferon gamma Human genes 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 102000016200 MART-1 Antigen Human genes 0.000 description 1
- 108010066345 MHC binding peptide Proteins 0.000 description 1
- 102100028389 Melanoma antigen recognized by T-cells 1 Human genes 0.000 description 1
- 102000007298 Mucin-1 Human genes 0.000 description 1
- 108010008707 Mucin-1 Proteins 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 101100166793 Mus musculus Cela2a gene Proteins 0.000 description 1
- 108700020796 Oncogene Proteins 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 1
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 1
- 102000015690 Proto-Oncogene Proteins c-bcr Human genes 0.000 description 1
- 108010024221 Proto-Oncogene Proteins c-bcr Proteins 0.000 description 1
- 230000006044 T cell activation Effects 0.000 description 1
- 230000006052 T cell proliferation Effects 0.000 description 1
- 102100027222 T-lymphocyte activation antigen CD80 Human genes 0.000 description 1
- 210000000662 T-lymphocyte subset Anatomy 0.000 description 1
- 210000000173 T-lymphoid precursor cell Anatomy 0.000 description 1
- 101800000849 Tachykinin-associated peptide 2 Proteins 0.000 description 1
- 108010017842 Telomerase Proteins 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 101710127857 Wilms tumor protein Proteins 0.000 description 1
- 108091007916 Zinc finger transcription factors Proteins 0.000 description 1
- 102000038627 Zinc finger transcription factors Human genes 0.000 description 1
- 230000001594 aberrant effect Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000000875 corresponding effect Effects 0.000 description 1
- 208000035250 cutaneous malignant susceptibility to 1 melanoma Diseases 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000007402 cytotoxic response Effects 0.000 description 1
- 238000002716 delivery method Methods 0.000 description 1
- XEYBRNLFEZDVAW-ARSRFYASSA-N dinoprostone Chemical compound CCCCC[C@H](O)\C=C\[C@H]1[C@H](O)CC(=O)[C@@H]1C\C=C/CCCC(O)=O XEYBRNLFEZDVAW-ARSRFYASSA-N 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- -1 e.g. Substances 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 1
- 102000052622 human IL7 Human genes 0.000 description 1
- 102000057041 human TNF Human genes 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000010185 immunofluorescence analysis Methods 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000004989 laser desorption mass spectroscopy Methods 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000007479 molecular analysis Methods 0.000 description 1
- 229940031348 multivalent vaccine Drugs 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000001613 neoplastic effect Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 230000005868 ontogenesis Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 210000001778 pluripotent stem cell Anatomy 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 239000012713 reactive precursor Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 235000004400 serine Nutrition 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/82—Translation products from oncogenes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/02—Antineoplastic agents specific for leukemia
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4702—Regulators; Modulating activity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4748—Tumour specific antigens; Tumour rejection antigen precursors [TRAP], e.g. MAGE
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Oncology (AREA)
- Veterinary Medicine (AREA)
- Immunology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Hematology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US52595503P | 2003-12-01 | 2003-12-01 | |
| US60/525,955 | 2003-12-01 | ||
| PCT/US2004/040347 WO2005053618A2 (en) | 2003-12-01 | 2004-11-30 | Synthetic hla binding peptide analogues and uses thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2548135A1 CA2548135A1 (en) | 2005-06-16 |
| CA2548135C true CA2548135C (en) | 2014-04-22 |
Family
ID=34652399
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2548135A Expired - Lifetime CA2548135C (en) | 2003-12-01 | 2004-11-30 | Synthetic hla binding peptide analogues and uses thereof |
Country Status (7)
| Country | Link |
|---|---|
| US (3) | US7488718B2 (enExample) |
| EP (2) | EP1708732B2 (enExample) |
| JP (1) | JP2007516966A (enExample) |
| AU (1) | AU2004294345B2 (enExample) |
| CA (1) | CA2548135C (enExample) |
| ES (1) | ES2402184T5 (enExample) |
| WO (1) | WO2005053618A2 (enExample) |
Families Citing this family (44)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20060127409A1 (en) * | 2003-12-01 | 2006-06-15 | Scheinberg David A | Bcr-abl vaccines and methods of use thereof |
| JP2007516966A (ja) * | 2003-12-01 | 2007-06-28 | スローン−ケターリング インスティチュート フォー キャンサー リサーチ | 合成ｈｌａ結合ペプチド類似体及びその使用方法 |
| US7612162B2 (en) | 2004-09-21 | 2009-11-03 | University Of Pittsburgh - Of The Commonwealth System Of Higher Education | Peptide analogs capable of enhancing stimulation of a glioma-specific CTL response |
| WO2007047764A2 (en) | 2005-10-17 | 2007-04-26 | Sloan Kettering Institute For Cancer Research | Wt1 hla class ii-binding peptides and compositions and methods comprising same |
| EP2010209B1 (en) * | 2006-04-10 | 2016-06-15 | Sloan Kettering Institute For Cancer Research | Immunogenic wt-1 peptides and methods of use thereof |
| WO2008048410A2 (en) * | 2006-09-19 | 2008-04-24 | Human Biomolecular Research Institute | Diagnostic methods and genetic markers for alzheimer disease |
| PL2119778T3 (pl) * | 2007-02-27 | 2016-04-29 | Int Inst Cancer Immunology Inc | Sposób aktywacji pomocniczej komórki T oraz kompozycja do zastosowania w tym sposobie |
| EP2216041A4 (en) * | 2007-11-20 | 2012-10-24 | Nec Corp | METHOD OF INDUCING A CYTOTOXIC T-CELL, CYTOTOXIC T-CELL INDUCTOR AND PHARMACEUTICAL COMPOSITION, AND VACCINE WITH THE INDUCTOR |
| CN101888852B (zh) | 2007-12-05 | 2017-02-08 | 株式会社癌免疫研究所 | 癌症疫苗组合物 |
| WO2009137872A1 (en) * | 2008-05-14 | 2009-11-19 | Simons Haplomics Limited | Methods and compositions for the treatment of cancer |
| EP2608799B1 (en) | 2010-08-24 | 2018-12-12 | University of Pittsburgh - Of the Commonwealth System of Higher Education | Interleukin-13 receptor alpha 2 peptide-based brain cancer vaccines |
| AU2012291101B2 (en) | 2011-07-29 | 2016-04-07 | Riken | Cell for use in immunotherapy which contains modified nucleic acid construct encoding Wilms tumor gene product or fragment thereof, method for producing said cell, and said nucleic acid construct |
| US9539299B2 (en) * | 2011-10-27 | 2017-01-10 | International Institute Of Cancer Immunology, Inc. | Combination therapy with WT1 peptide vaccine and temozolomide |
| CN104684577B (zh) | 2012-01-13 | 2018-05-08 | 纪念斯隆凯特林癌症中心 | 免疫原性wt-1肽及其使用方法 |
| EP2914278B1 (en) | 2012-11-05 | 2021-06-02 | Dana-Farber Cancer Institute, Inc. | Xbp1, cd138, and cs1 peptides, pharmaceutical compositions that include the peptides, and methods of using such peptides and compositions |
| PL2945647T3 (pl) | 2013-01-15 | 2021-03-08 | Memorial Sloan Kettering Cancer Center | Immunogenne peptydy wt-1 i sposoby ich zastosowania |
| US10815273B2 (en) | 2013-01-15 | 2020-10-27 | Memorial Sloan Kettering Cancer Center | Immunogenic WT-1 peptides and methods of use thereof |
| US9228207B2 (en) | 2013-09-06 | 2016-01-05 | President And Fellows Of Harvard College | Switchable gRNAs comprising aptamers |
| US10077453B2 (en) | 2014-07-30 | 2018-09-18 | President And Fellows Of Harvard College | CAS9 proteins including ligand-dependent inteins |
| EP3365356B1 (en) | 2015-10-23 | 2023-06-28 | President and Fellows of Harvard College | Nucleobase editors and uses thereof |
| KR20250099263A (ko) | 2015-11-20 | 2025-07-01 | 메모리얼 슬로안 케터링 캔서 센터 | 암 치료 방법 및 조성물 |
| CA3034666A1 (en) | 2016-08-23 | 2018-03-01 | Oncopep, Inc. | Peptide vaccines and durvalumab for treating breast cancer |
| WO2018039203A1 (en) | 2016-08-23 | 2018-03-01 | Oncopep, Inc. | Peptide vaccines and durvalumab for treating multiple myeloma |
| JP7209963B2 (ja) | 2016-11-30 | 2023-01-23 | 住友ファーマ株式会社 | Ｗｔ１ヘルパーペプチド及びこれと癌抗原ペプチドコンジュゲート体との組合せ |
| WO2018165631A1 (en) | 2017-03-09 | 2018-09-13 | President And Fellows Of Harvard College | Cancer vaccine |
| KR20190127797A (ko) | 2017-03-10 | 2019-11-13 | 프레지던트 앤드 펠로우즈 오브 하바드 칼리지 | 시토신에서 구아닌으로의 염기 편집제 |
| JPWO2018181648A1 (ja) | 2017-03-30 | 2020-02-13 | 大日本住友製薬株式会社 | Ｗｔ１癌抗原ペプチドおよびこれを含むペプチドコンジュゲート体 |
| WO2019023680A1 (en) | 2017-07-28 | 2019-01-31 | President And Fellows Of Harvard College | METHODS AND COMPOSITIONS FOR EVOLUTION OF BASIC EDITORS USING PHAGE-ASSISTED CONTINUOUS EVOLUTION (PACE) |
| WO2019083960A1 (en) | 2017-10-24 | 2019-05-02 | Oncopep, Inc. | PEPTIDE VACCINES AND HDAC INHIBITORS FOR THE TREATMENT OF MULTIPLE MYELOMA |
| EP3700575A1 (en) | 2017-10-24 | 2020-09-02 | Oncopep, Inc. | Peptide vaccines and pembrolizumab for treating breast cancer |
| WO2019118949A1 (en) | 2017-12-15 | 2019-06-20 | The Broad Institute, Inc. | Systems and methods for predicting repair outcomes in genetic engineering |
| CN113382746A (zh) | 2018-09-28 | 2021-09-10 | 大日本住友制药株式会社 | 注射用组合物 |
| US12281338B2 (en) | 2018-10-29 | 2025-04-22 | The Broad Institute, Inc. | Nucleobase editors comprising GeoCas9 and uses thereof |
| WO2020154500A1 (en) | 2019-01-23 | 2020-07-30 | The Broad Institute, Inc. | Supernegatively charged proteins and uses thereof |
| MX2021011426A (es) | 2019-03-19 | 2022-03-11 | Broad Inst Inc | Metodos y composiciones para editar secuencias de nucleótidos. |
| EP3956349A1 (en) | 2019-04-17 | 2022-02-23 | The Broad Institute, Inc. | Adenine base editors with reduced off-target effects |
| US12435330B2 (en) | 2019-10-10 | 2025-10-07 | The Broad Institute, Inc. | Methods and compositions for prime editing RNA |
| CA3182959A1 (en) | 2020-05-12 | 2021-11-18 | Sumitomo Pharma Co., Ltd. | Pharmaceutical composition for treating cancer |
| US11058751B1 (en) | 2020-11-20 | 2021-07-13 | Think Therapeutics, Inc. | Compositions for optimized RAS peptide vaccines |
| US11421015B2 (en) | 2020-12-07 | 2022-08-23 | Think Therapeutics, Inc. | Method of compact peptide vaccines using residue optimization |
| CN116710115A (zh) | 2020-11-20 | 2023-09-05 | 思维疗法股份有限公司 | 用于优化的肽疫苗的组合物和方法 |
| US11464842B1 (en) | 2021-04-28 | 2022-10-11 | Think Therapeutics, Inc. | Compositions and method for optimized peptide vaccines using residue optimization |
| CN118076382A (zh) | 2021-08-12 | 2024-05-24 | 株式会社癌免疫研究所 | 用于治疗或预防癌症的药用组合物和方法 |
| CN114149970B (zh) * | 2021-11-09 | 2024-06-18 | 因诺伟(北京)生物医疗科技有限公司 | 一种外周血造血干细胞来源致敏树突状细胞的制备方法及应用 |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6156316A (en) * | 1995-05-08 | 2000-12-05 | Sloan-Kettering Institute For Cancer Research | Oncogene fusion protein peptide vaccines |
| US20030235557A1 (en) * | 1998-09-30 | 2003-12-25 | Corixa Corporation | Compositions and methods for WT1 specific immunotherapy |
| GB9823897D0 (en) * | 1998-11-02 | 1998-12-30 | Imp College Innovations Ltd | Immunotherapeutic methods and molecules |
| CA2401070A1 (en) * | 2000-02-22 | 2001-08-30 | Corixa Corporation | Compositions and methods for diagnosis and therapy of malignant mesothelioma |
| JP2007516966A (ja) * | 2003-12-01 | 2007-06-28 | スローン−ケターリング インスティチュート フォー キャンサー リサーチ | 合成ｈｌａ結合ペプチド類似体及びその使用方法 |
-
2004
- 2004-11-30 JP JP2006542741A patent/JP2007516966A/ja active Pending
- 2004-11-30 ES ES04812790.6T patent/ES2402184T5/es not_active Expired - Lifetime
- 2004-11-30 EP EP04812790.6A patent/EP1708732B2/en not_active Expired - Lifetime
- 2004-11-30 WO PCT/US2004/040347 patent/WO2005053618A2/en not_active Ceased
- 2004-11-30 US US10/999,425 patent/US7488718B2/en active Active
- 2004-11-30 CA CA2548135A patent/CA2548135C/en not_active Expired - Lifetime
- 2004-11-30 AU AU2004294345A patent/AU2004294345B2/en not_active Expired
- 2004-11-30 EP EP11189059A patent/EP2478913A1/en not_active Withdrawn
-
2005
- 2005-09-12 US US11/223,139 patent/US7598221B2/en active Active
-
2009
- 2009-10-06 US US12/574,555 patent/US20100239547A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| AU2004294345A1 (en) | 2005-06-16 |
| EP1708732B2 (en) | 2016-05-18 |
| EP1708732A4 (en) | 2009-09-02 |
| EP1708732A2 (en) | 2006-10-11 |
| WO2005053618A3 (en) | 2006-02-23 |
| ES2402184T5 (es) | 2016-10-25 |
| WO2005053618A2 (en) | 2005-06-16 |
| US20050119185A1 (en) | 2005-06-02 |
| ES2402184T3 (es) | 2013-04-29 |
| US20060084609A1 (en) | 2006-04-20 |
| CA2548135A1 (en) | 2005-06-16 |
| JP2007516966A (ja) | 2007-06-28 |
| US7488718B2 (en) | 2009-02-10 |
| EP2478913A1 (en) | 2012-07-25 |
| EP1708732B1 (en) | 2013-01-02 |
| AU2004294345B2 (en) | 2012-02-23 |
| US7598221B2 (en) | 2009-10-06 |
| US20100239547A1 (en) | 2010-09-23 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2548135C (en) | Synthetic hla binding peptide analogues and uses thereof | |
| US10221224B2 (en) | WT1 HLA class II-binding peptides and compositions and methods comprising same | |
| CN104684577B (zh) | 免疫原性wt-1肽及其使用方法 | |
| US9265816B2 (en) | Immunogenic WT-1 peptides and methods of use thereof | |
| AU2018241209A1 (en) | Immunogenic WT-1 peptides and methods of use thereof | |
| WO2003106682A1 (ja) | Ｈｌａ−ａ２４拘束性癌抗原ペプチド | |
| JP4051602B2 (ja) | 腫瘍抗原 | |
| JPWO2001011044A1 (ja) | 腫瘍抗原 | |
| WO2007047653A2 (en) | Synthetic hla binding peptide analogues of mutant v617f jak2 enzyme and uses therefor | |
| WO2007120603A2 (en) | Immunogenic bcr-abl peptides and methods of use thereof | |
| US20060153861A1 (en) | BCR-ABL imatinib resistance-associated peptides and methods of use thereof | |
| AU2012202819A1 (en) | Synthetic HLA binding peptide analogues and uses thereof | |
| US20060134129A1 (en) | Synthetic HLA binding peptide analogues and uses thereof | |
| US20060127409A1 (en) | Bcr-abl vaccines and methods of use thereof | |
| HK40054568A (en) | Immunogenic wt-1 peptides and uses thereof | |
| HK40045843A (en) | Immunogenic wt-1 peptides and methods of use thereof | |
| HK40012212A (en) | Immunogenic wt-1 peptides and methods of use thereof | |
| Borras-Cuesta et al. | Identification of an antigenic epitope for helper T lymphocytes from carcinoembryonic antigen | |
| Myers | Custom designed MHC binding peptides for cancer immunotherapy |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |