ES2357960T3 - Procedimiento para generar células t activadas y células presentadoras de antígenos pulsadas con antígenos. - Google Patents
Procedimiento para generar células t activadas y células presentadoras de antígenos pulsadas con antígenos. Download PDFInfo
- Publication number
- ES2357960T3 ES2357960T3 ES05076809T ES05076809T ES2357960T3 ES 2357960 T3 ES2357960 T3 ES 2357960T3 ES 05076809 T ES05076809 T ES 05076809T ES 05076809 T ES05076809 T ES 05076809T ES 2357960 T3 ES2357960 T3 ES 2357960T3
- Authority
- ES
- Spain
- Prior art keywords
- cells
- peptide
- muc
- cell
- antigen
- 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
- 239000000427 antigen Substances 0.000 title claims abstract description 146
- 108091007433 antigens Proteins 0.000 title claims abstract description 146
- 102000036639 antigens Human genes 0.000 title claims abstract description 146
- 210000001744 T-lymphocyte Anatomy 0.000 title description 196
- 210000004027 cell Anatomy 0.000 title description 122
- 238000000034 method Methods 0.000 title description 91
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 230
- 108010008707 Mucin-1 Proteins 0.000 claims abstract description 115
- 102100034256 Mucin-1 Human genes 0.000 claims abstract description 109
- 150000001413 amino acids Chemical class 0.000 claims abstract description 36
- 230000005867 T cell response Effects 0.000 claims abstract description 29
- 125000001924 fatty-acyl group Chemical group 0.000 claims abstract description 3
- 125000003473 lipid group Chemical group 0.000 claims abstract 2
- 239000002502 liposome Substances 0.000 claims description 84
- 150000002632 lipids Chemical class 0.000 claims description 33
- 239000000203 mixture Substances 0.000 claims description 17
- 125000001312 palmitoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 7
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims description 6
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 claims description 3
- 125000003074 decanoyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C(*)=O 0.000 claims description 2
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims description 2
- 125000001419 myristoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 2
- 125000003696 stearoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 2
- 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 claims 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 75
- KXJTWOGIBOWZDJ-LELJLAJGSA-N l-blp25 Chemical compound C([C@@H](C(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(O)=O)NC(=O)[C@H](C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H]1N(CCC1)C(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@@H](N)CO)[C@@H](C)O)C1=CNC=N1 KXJTWOGIBOWZDJ-LELJLAJGSA-N 0.000 description 55
- 241000282414 Homo sapiens Species 0.000 description 42
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 31
- 108010017838 cyclo-(lysyl-prolyl-glycyl-prolyl-glycyl-glutamyl-prolyl-glycyl-prolyl-glycyl)cyclo(1epsilon-6gamma)glycyl-glycine Proteins 0.000 description 30
- 206010028980 Neoplasm Diseases 0.000 description 29
- 102000004127 Cytokines Human genes 0.000 description 28
- 108090000695 Cytokines Proteins 0.000 description 28
- 102100034922 T-cell surface glycoprotein CD8 alpha chain Human genes 0.000 description 26
- 210000000265 leukocyte Anatomy 0.000 description 26
- 102100034540 Adenomatous polyposis coli protein Human genes 0.000 description 25
- 101000924577 Homo sapiens Adenomatous polyposis coli protein Proteins 0.000 description 25
- 108010028921 Lipopeptides Proteins 0.000 description 25
- 238000000338 in vitro Methods 0.000 description 24
- 229940024606 amino acid Drugs 0.000 description 23
- 235000001014 amino acid Nutrition 0.000 description 23
- 210000000612 antigen-presenting cell Anatomy 0.000 description 22
- 230000000890 antigenic effect Effects 0.000 description 20
- 239000002609 medium Substances 0.000 description 20
- 230000009696 proliferative response Effects 0.000 description 20
- 239000006228 supernatant Substances 0.000 description 19
- 230000004044 response Effects 0.000 description 18
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 17
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 17
- 238000002965 ELISA Methods 0.000 description 16
- 108090000978 Interleukin-4 Proteins 0.000 description 16
- 102000004388 Interleukin-4 Human genes 0.000 description 16
- 238000003556 assay Methods 0.000 description 16
- 239000012634 fragment Substances 0.000 description 16
- 108010002350 Interleukin-2 Proteins 0.000 description 15
- 102000000588 Interleukin-2 Human genes 0.000 description 15
- 230000000638 stimulation Effects 0.000 description 15
- 102100025137 Early activation antigen CD69 Human genes 0.000 description 14
- 101000934374 Homo sapiens Early activation antigen CD69 Proteins 0.000 description 14
- 108091054437 MHC class I family Proteins 0.000 description 13
- 230000001472 cytotoxic effect Effects 0.000 description 13
- 238000002474 experimental method Methods 0.000 description 12
- 238000004007 reversed phase HPLC Methods 0.000 description 12
- 108090000174 Interleukin-10 Proteins 0.000 description 11
- 201000011510 cancer Diseases 0.000 description 11
- 238000011534 incubation Methods 0.000 description 11
- 239000000463 material Substances 0.000 description 11
- 101000914514 Homo sapiens T-cell-specific surface glycoprotein CD28 Proteins 0.000 description 10
- 102000043129 MHC class I family Human genes 0.000 description 10
- NWIBSHFKIJFRCO-WUDYKRTCSA-N Mytomycin Chemical compound C1N2C(C(C(C)=C(N)C3=O)=O)=C3[C@@H](COC(N)=O)[C@@]2(OC)[C@@H]2[C@H]1N2 NWIBSHFKIJFRCO-WUDYKRTCSA-N 0.000 description 10
- 102100027213 T-cell-specific surface glycoprotein CD28 Human genes 0.000 description 10
- 230000004913 activation Effects 0.000 description 10
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 9
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 9
- QTBSBXVTEAMEQO-UHFFFAOYSA-N acetic acid Substances CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 9
- 231100000433 cytotoxic Toxicity 0.000 description 9
- 230000034994 death Effects 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 230000009257 reactivity Effects 0.000 description 9
- 230000002829 reductive effect Effects 0.000 description 9
- KILNVBDSWZSGLL-KXQOOQHDSA-N 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCCCCCCCCC KILNVBDSWZSGLL-KXQOOQHDSA-N 0.000 description 8
- 101001057504 Homo sapiens Interferon-stimulated gene 20 kDa protein Proteins 0.000 description 8
- 101001055144 Homo sapiens Interleukin-2 receptor subunit alpha Proteins 0.000 description 8
- 102100027268 Interferon-stimulated gene 20 kDa protein Human genes 0.000 description 8
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 8
- 238000001516 cell proliferation assay Methods 0.000 description 8
- 238000004128 high performance liquid chromatography Methods 0.000 description 8
- 239000013642 negative control Substances 0.000 description 8
- 108090000623 proteins and genes Proteins 0.000 description 8
- 238000012360 testing method Methods 0.000 description 8
- 239000002691 unilamellar liposome Substances 0.000 description 8
- 108010065805 Interleukin-12 Proteins 0.000 description 7
- 208000009956 adenocarcinoma Diseases 0.000 description 7
- 239000003795 chemical substances by application Substances 0.000 description 7
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 7
- 230000028993 immune response Effects 0.000 description 7
- 238000004519 manufacturing process Methods 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 235000018102 proteins Nutrition 0.000 description 7
- 102000004169 proteins and genes Human genes 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 6
- JVJGCCBAOOWGEO-RUTPOYCXSA-N (2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-4-amino-2-[[(2s,3s)-2-[[(2s,3s)-2-[[(2s)-2-azaniumyl-3-hydroxypropanoyl]amino]-3-methylpentanoyl]amino]-3-methylpentanoyl]amino]-4-oxobutanoyl]amino]-3-phenylpropanoyl]amino]-4-carboxylatobutanoyl]amino]-6-azaniumy Chemical compound OC[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(O)=O)CC1=CC=CC=C1 JVJGCCBAOOWGEO-RUTPOYCXSA-N 0.000 description 6
- 102100034763 Peroxiredoxin-2 Human genes 0.000 description 6
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 6
- 239000002253 acid Substances 0.000 description 6
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 6
- 210000004443 dendritic cell Anatomy 0.000 description 6
- 230000036039 immunity Effects 0.000 description 6
- 230000001965 increasing effect Effects 0.000 description 6
- 210000003071 memory t lymphocyte Anatomy 0.000 description 6
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 6
- 230000035755 proliferation Effects 0.000 description 6
- 238000011160 research Methods 0.000 description 6
- 239000007790 solid phase Substances 0.000 description 6
- 241000283707 Capra Species 0.000 description 5
- 241000725303 Human immunodeficiency virus Species 0.000 description 5
- 108010002586 Interleukin-7 Proteins 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 239000004698 Polyethylene Substances 0.000 description 5
- 229920002684 Sepharose Polymers 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 5
- 238000013459 approach Methods 0.000 description 5
- 238000004113 cell culture Methods 0.000 description 5
- 230000016396 cytokine production Effects 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 238000010828 elution Methods 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- 238000009169 immunotherapy Methods 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 206010022000 influenza Diseases 0.000 description 5
- 238000002955 isolation Methods 0.000 description 5
- 229960004857 mitomycin Drugs 0.000 description 5
- 239000002245 particle Substances 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- 239000013641 positive control Substances 0.000 description 5
- 238000012163 sequencing technique Methods 0.000 description 5
- 210000002966 serum Anatomy 0.000 description 5
- 238000010186 staining Methods 0.000 description 5
- 230000004936 stimulating effect Effects 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- -1 CD45R0 Proteins 0.000 description 4
- 238000012286 ELISA Assay Methods 0.000 description 4
- 101001133056 Homo sapiens Mucin-1 Proteins 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- 239000004677 Nylon Substances 0.000 description 4
- 102000003992 Peroxidases Human genes 0.000 description 4
- 230000006044 T cell activation Effects 0.000 description 4
- 230000006052 T cell proliferation Effects 0.000 description 4
- 230000001464 adherent effect Effects 0.000 description 4
- 239000012491 analyte Substances 0.000 description 4
- 230000000903 blocking effect Effects 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 230000008859 change Effects 0.000 description 4
- 239000012228 culture supernatant Substances 0.000 description 4
- 238000011026 diafiltration Methods 0.000 description 4
- 239000012636 effector Substances 0.000 description 4
- 238000000684 flow cytometry Methods 0.000 description 4
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 4
- 230000005847 immunogenicity Effects 0.000 description 4
- 238000010348 incorporation Methods 0.000 description 4
- 239000003446 ligand Substances 0.000 description 4
- 229920001778 nylon Polymers 0.000 description 4
- 230000020477 pH reduction Effects 0.000 description 4
- 244000045947 parasite Species 0.000 description 4
- 108040007629 peroxidase activity proteins Proteins 0.000 description 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
- 230000002062 proliferating effect Effects 0.000 description 4
- 230000035945 sensitivity Effects 0.000 description 4
- 230000002269 spontaneous effect Effects 0.000 description 4
- 229960005486 vaccine Drugs 0.000 description 4
- 201000009030 Carcinoma Diseases 0.000 description 3
- 102000008949 Histocompatibility Antigens Class I Human genes 0.000 description 3
- 108010002352 Interleukin-1 Proteins 0.000 description 3
- 102000000589 Interleukin-1 Human genes 0.000 description 3
- 102000043131 MHC class II family Human genes 0.000 description 3
- 108091054438 MHC class II family Proteins 0.000 description 3
- 108010063954 Mucins Proteins 0.000 description 3
- 102000015728 Mucins Human genes 0.000 description 3
- 229930040373 Paraformaldehyde Natural products 0.000 description 3
- 239000012980 RPMI-1640 medium Substances 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- 241001417495 Serranidae Species 0.000 description 3
- 108010090804 Streptavidin Proteins 0.000 description 3
- 108091008874 T cell receptors Proteins 0.000 description 3
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 3
- 208000036142 Viral infection Diseases 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- ATBOMIWRCZXYSZ-XZBBILGWSA-N [1-[2,3-dihydroxypropoxy(hydroxy)phosphoryl]oxy-3-hexadecanoyloxypropan-2-yl] (9e,12e)-octadeca-9,12-dienoate Chemical compound CCCCCCCCCCCCCCCC(=O)OCC(COP(O)(=O)OCC(O)CO)OC(=O)CCCCCCC\C=C\C\C=C\CCCCC ATBOMIWRCZXYSZ-XZBBILGWSA-N 0.000 description 3
- AWUCVROLDVIAJX-UHFFFAOYSA-N alpha-glycerophosphate Natural products OCC(O)COP(O)(O)=O AWUCVROLDVIAJX-UHFFFAOYSA-N 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 229960002685 biotin Drugs 0.000 description 3
- 235000020958 biotin Nutrition 0.000 description 3
- 239000011616 biotin Substances 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 235000014633 carbohydrates Nutrition 0.000 description 3
- 125000002091 cationic group Chemical group 0.000 description 3
- 235000012000 cholesterol Nutrition 0.000 description 3
- 210000004748 cultured cell Anatomy 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 238000005538 encapsulation Methods 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 239000006166 lysate Substances 0.000 description 3
- 210000002540 macrophage Anatomy 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 230000011278 mitosis Effects 0.000 description 3
- 210000000865 mononuclear phagocyte system Anatomy 0.000 description 3
- 229920002866 paraformaldehyde Polymers 0.000 description 3
- 244000052769 pathogen Species 0.000 description 3
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 3
- 230000003389 potentiating effect Effects 0.000 description 3
- 230000037452 priming Effects 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000010183 spectrum analysis Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 238000002560 therapeutic procedure Methods 0.000 description 3
- 238000011282 treatment Methods 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- 230000009385 viral infection Effects 0.000 description 3
- 239000011534 wash buffer Substances 0.000 description 3
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 2
- 108010039627 Aprotinin Proteins 0.000 description 2
- MJJIHRWNWSQTOI-VEVYYDQMSA-N Asp-Thr-Arg Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H]([C@H](O)C)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O MJJIHRWNWSQTOI-VEVYYDQMSA-N 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 108010022366 Carcinoembryonic Antigen Proteins 0.000 description 2
- 102100025475 Carcinoembryonic antigen-related cell adhesion molecule 5 Human genes 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 2
- 102000002068 Glycopeptides Human genes 0.000 description 2
- 108010015899 Glycopeptides Proteins 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 2
- 108010074328 Interferon-gamma Proteins 0.000 description 2
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 2
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 2
- 102000015696 Interleukins Human genes 0.000 description 2
- 108010063738 Interleukins Proteins 0.000 description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- 229930182816 L-glutamine Natural products 0.000 description 2
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 2
- 108010037255 Member 7 Tumor Necrosis Factor Receptor Superfamily Proteins 0.000 description 2
- 108010058846 Ovalbumin Proteins 0.000 description 2
- 241000223960 Plasmodium falciparum Species 0.000 description 2
- 102100033762 Proheparin-binding EGF-like growth factor Human genes 0.000 description 2
- 102000007066 Prostate-Specific Antigen Human genes 0.000 description 2
- 108010072866 Prostate-Specific Antigen Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 241000287433 Turdus Species 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 125000000129 anionic group Chemical group 0.000 description 2
- 230000007503 antigenic stimulation Effects 0.000 description 2
- 229960004405 aprotinin Drugs 0.000 description 2
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 150000001719 carbohydrate derivatives Chemical class 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 230000022131 cell cycle Effects 0.000 description 2
- 238000009172 cell transfer therapy Methods 0.000 description 2
- 229940030156 cell vaccine Drugs 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 230000002596 correlated effect Effects 0.000 description 2
- 230000000139 costimulatory effect Effects 0.000 description 2
- 238000004163 cytometry Methods 0.000 description 2
- 230000007402 cytotoxic response Effects 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 239000003599 detergent Substances 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 2
- 239000003085 diluting agent Substances 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000000132 electrospray ionisation Methods 0.000 description 2
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 2
- 239000012149 elution buffer Substances 0.000 description 2
- 230000012202 endocytosis Effects 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 239000012467 final product Substances 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- IPCSVZSSVZVIGE-UHFFFAOYSA-N hexadecanoic acid Chemical compound CCCCCCCCCCCCCCCC(O)=O IPCSVZSSVZVIGE-UHFFFAOYSA-N 0.000 description 2
- VBZWSGALLODQNC-UHFFFAOYSA-N hexafluoroacetone Chemical compound FC(F)(F)C(=O)C(F)(F)F VBZWSGALLODQNC-UHFFFAOYSA-N 0.000 description 2
- 230000003308 immunostimulating effect Effects 0.000 description 2
- 230000001024 immunotherapeutic effect Effects 0.000 description 2
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 108010052968 leupeptin Proteins 0.000 description 2
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 210000004698 lymphocyte Anatomy 0.000 description 2
- 238000002794 lymphocyte assay Methods 0.000 description 2
- 239000012139 lysis buffer Substances 0.000 description 2
- 201000004792 malaria Diseases 0.000 description 2
- 238000001819 mass spectrum Methods 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 230000003278 mimic effect Effects 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 229940092253 ovalbumin Drugs 0.000 description 2
- 230000000242 pagocytic effect Effects 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 210000005259 peripheral blood Anatomy 0.000 description 2
- 239000011886 peripheral blood Substances 0.000 description 2
- 235000020030 perry Nutrition 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 230000005855 radiation Effects 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 125000006853 reporter group Chemical group 0.000 description 2
- 230000000284 resting effect Effects 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 238000010532 solid phase synthesis reaction Methods 0.000 description 2
- 230000003595 spectral effect Effects 0.000 description 2
- 230000001954 sterilising effect Effects 0.000 description 2
- 238000004659 sterilization and disinfection Methods 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 239000003643 water by type Substances 0.000 description 2
- CJDRUOGAGYHKKD-XMTJACRCSA-N (+)-Ajmaline Natural products O[C@H]1[C@@H](CC)[C@@H]2[C@@H]3[C@H](O)[C@@]45[C@@H](N(C)c6c4cccc6)[C@@H](N1[C@H]3C5)C2 CJDRUOGAGYHKKD-XMTJACRCSA-N 0.000 description 1
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- DQJCDTNMLBYVAY-ZXXIYAEKSA-N (2S,5R,10R,13R)-16-{[(2R,3S,4R,5R)-3-{[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy}-5-(ethylamino)-6-hydroxy-2-(hydroxymethyl)oxan-4-yl]oxy}-5-(4-aminobutyl)-10-carbamoyl-2,13-dimethyl-4,7,12,15-tetraoxo-3,6,11,14-tetraazaheptadecan-1-oic acid Chemical compound NCCCC[C@H](C(=O)N[C@@H](C)C(O)=O)NC(=O)CC[C@H](C(N)=O)NC(=O)[C@@H](C)NC(=O)C(C)O[C@@H]1[C@@H](NCC)C(O)O[C@H](CO)[C@H]1O[C@H]1[C@H](NC(C)=O)[C@@H](O)[C@H](O)[C@@H](CO)O1 DQJCDTNMLBYVAY-ZXXIYAEKSA-N 0.000 description 1
- TWLQEIBUXHHZPI-UPPQRMANSA-N (2s)-1-[(2s)-4-amino-2-[[(2s)-2-[[(2s)-4-amino-2-[[(2s)-1-[(2s)-4-amino-2-[[(2s)-2-[[(2s)-4-amino-2-[[(2s)-1-[(2s)-4-amino-2-[[(2s)-2-[[(2s)-2,4-diamino-4-oxobutanoyl]amino]propanoyl]amino]-4-oxobutanoyl]pyrrolidine-2-carbonyl]amino]-4-oxobutanoyl]amino]p Chemical compound NC(=O)C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N1[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N2[C@@H](CCC2)C(O)=O)CCC1 TWLQEIBUXHHZPI-UPPQRMANSA-N 0.000 description 1
- SJTPYAOZAPSOLO-REOHCLBHSA-N (2s)-2-hydrazinyl-3-hydroxypropanoic acid Chemical group NN[C@@H](CO)C(O)=O SJTPYAOZAPSOLO-REOHCLBHSA-N 0.000 description 1
- 108010004200 (asparaginyl-alanyl-asparaginyl-proline)3 Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 102100035526 B melanoma antigen 1 Human genes 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 102100032912 CD44 antigen Human genes 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- YVGGHNCTFXOJCH-UHFFFAOYSA-N DDT Chemical compound C1=CC(Cl)=CC=C1C(C(Cl)(Cl)Cl)C1=CC=C(Cl)C=C1 YVGGHNCTFXOJCH-UHFFFAOYSA-N 0.000 description 1
- 206010011968 Decreased immune responsiveness Diseases 0.000 description 1
- 102100025012 Dipeptidyl peptidase 4 Human genes 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 238000011510 Elispot assay Methods 0.000 description 1
- 101710146739 Enterotoxin Proteins 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- 108091006027 G proteins Proteins 0.000 description 1
- 230000035519 G0 Phase Effects 0.000 description 1
- 230000010190 G1 phase Effects 0.000 description 1
- 230000010337 G2 phase Effects 0.000 description 1
- 102000030782 GTP binding Human genes 0.000 description 1
- 108091000058 GTP-Binding Proteins 0.000 description 1
- 229930186217 Glycolipid Natural products 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 108010078851 HIV Reverse Transcriptase Proteins 0.000 description 1
- 102100036242 HLA class II histocompatibility antigen, DQ alpha 2 chain Human genes 0.000 description 1
- 102000025850 HLA-A2 Antigen Human genes 0.000 description 1
- 108010074032 HLA-A2 Antigen Proteins 0.000 description 1
- 101710121697 Heat-stable enterotoxin Proteins 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 208000009889 Herpes Simplex Diseases 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000874316 Homo sapiens B melanoma antigen 1 Proteins 0.000 description 1
- 101000868273 Homo sapiens CD44 antigen Proteins 0.000 description 1
- 101000908391 Homo sapiens Dipeptidyl peptidase 4 Proteins 0.000 description 1
- 101000930801 Homo sapiens HLA class II histocompatibility antigen, DQ alpha 2 chain Proteins 0.000 description 1
- 101000935043 Homo sapiens Integrin beta-1 Proteins 0.000 description 1
- 101001063392 Homo sapiens Lymphocyte function-associated antigen 3 Proteins 0.000 description 1
- 101000946889 Homo sapiens Monocyte differentiation antigen CD14 Proteins 0.000 description 1
- 101000738771 Homo sapiens Receptor-type tyrosine-protein phosphatase C Proteins 0.000 description 1
- 206010062016 Immunosuppression Diseases 0.000 description 1
- 102100025304 Integrin beta-1 Human genes 0.000 description 1
- 102100025390 Integrin beta-2 Human genes 0.000 description 1
- 102000015271 Intercellular Adhesion Molecule-1 Human genes 0.000 description 1
- 108010064593 Intercellular Adhesion Molecule-1 Proteins 0.000 description 1
- 102100037850 Interferon gamma Human genes 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108090000176 Interleukin-13 Proteins 0.000 description 1
- 102000003812 Interleukin-15 Human genes 0.000 description 1
- 108090000172 Interleukin-15 Proteins 0.000 description 1
- 108010002616 Interleukin-5 Proteins 0.000 description 1
- 108090001005 Interleukin-6 Proteins 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 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
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- 241000222722 Leishmania <genus> Species 0.000 description 1
- 241000222727 Leishmania donovani Species 0.000 description 1
- 241000222732 Leishmania major Species 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 108010064548 Lymphocyte Function-Associated Antigen-1 Proteins 0.000 description 1
- 102100030984 Lymphocyte function-associated antigen 3 Human genes 0.000 description 1
- 102000008072 Lymphokines Human genes 0.000 description 1
- 108010074338 Lymphokines Proteins 0.000 description 1
- 108700018351 Major Histocompatibility Complex Proteins 0.000 description 1
- 102000007557 Melanoma-Specific Antigens Human genes 0.000 description 1
- 108010071463 Melanoma-Specific Antigens Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102100035877 Monocyte differentiation antigen CD14 Human genes 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101001133053 Mus musculus Mucin-1 Proteins 0.000 description 1
- 101001095260 Mus musculus Prolyl endopeptidase Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 102000011931 Nucleoproteins Human genes 0.000 description 1
- 108010061100 Nucleoproteins Proteins 0.000 description 1
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 1
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 1
- 101710160107 Outer membrane protein A Proteins 0.000 description 1
- 235000021314 Palmitic acid Nutrition 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 102100037422 Receptor-type tyrosine-protein phosphatase C Human genes 0.000 description 1
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 1
- 230000018199 S phase Effects 0.000 description 1
- 108010024818 Schistosoma mansoni 28-kilodalton glutathione S-transferase antigen Proteins 0.000 description 1
- 241000607760 Shigella sonnei Species 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 241000223997 Toxoplasma gondii Species 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 1
- 238000011467 adoptive cell therapy Methods 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 230000000712 assembly Effects 0.000 description 1
- 238000000429 assembly Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 201000008680 babesiosis Diseases 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 210000004900 c-terminal fragment Anatomy 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000011712 cell development Effects 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000006957 competitive inhibition Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 230000000875 corresponding effect Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 230000006806 disease prevention Effects 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 238000012137 double-staining Methods 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 230000002121 endocytic effect Effects 0.000 description 1
- 210000001163 endosome Anatomy 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 239000000147 enterotoxin Substances 0.000 description 1
- 231100000655 enterotoxin Toxicity 0.000 description 1
- 238000003114 enzyme-linked immunosorbent spot assay Methods 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 238000001125 extrusion Methods 0.000 description 1
- 239000000706 filtrate 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
- 238000000799 fluorescence microscopy Methods 0.000 description 1
- 235000015244 frankfurter Nutrition 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 229940044627 gamma-interferon Drugs 0.000 description 1
- 238000004817 gas chromatography Methods 0.000 description 1
- 102000054766 genetic haplotypes Human genes 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000007773 growth pattern Effects 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 210000002443 helper t lymphocyte Anatomy 0.000 description 1
- 239000000185 hemagglutinin Substances 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 229920006158 high molecular weight polymer Polymers 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 210000005104 human peripheral blood lymphocyte Anatomy 0.000 description 1
- 230000008348 humoral response Effects 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 238000003125 immunofluorescent labeling Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 229940047122 interleukins Drugs 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- GZQKNULLWNGMCW-PWQABINMSA-N lipid A (E. coli) Chemical compound O1[C@H](CO)[C@@H](OP(O)(O)=O)[C@H](OC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCCCC)[C@@H](NC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCC)[C@@H]1OC[C@@H]1[C@@H](O)[C@H](OC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](NC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](OP(O)(O)=O)O1 GZQKNULLWNGMCW-PWQABINMSA-N 0.000 description 1
- 230000000527 lymphocytic effect Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000012737 microarray-based gene expression Methods 0.000 description 1
- 239000003607 modifier Substances 0.000 description 1
- 229940051875 mucins Drugs 0.000 description 1
- 238000012243 multiplex automated genomic engineering Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- WQEPLUUGTLDZJY-UHFFFAOYSA-N n-Pentadecanoic acid Natural products CCCCCCCCCCCCCCC(O)=O WQEPLUUGTLDZJY-UHFFFAOYSA-N 0.000 description 1
- 210000004898 n-terminal fragment Anatomy 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 108010028895 oncolipin Proteins 0.000 description 1
- GSSMIHQEWAQUPM-AOLPDKKJSA-N ovalbumin peptide Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)[C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C1=CN=CN1 GSSMIHQEWAQUPM-AOLPDKKJSA-N 0.000 description 1
- 230000002611 ovarian Effects 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 210000004986 primary T-cell Anatomy 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000002250 progressing effect Effects 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 230000010349 pulsation Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- QEVHRUUCFGRFIF-MDEJGZGSSA-N reserpine Chemical compound O([C@H]1[C@@H]([C@H]([C@H]2C[C@@H]3C4=C(C5=CC=C(OC)C=C5N4)CCN3C[C@H]2C1)C(=O)OC)OC)C(=O)C1=CC(OC)=C(OC)C(OC)=C1 QEVHRUUCFGRFIF-MDEJGZGSSA-N 0.000 description 1
- 230000004043 responsiveness Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 201000004409 schistosomiasis Diseases 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 229940115939 shigella sonnei Drugs 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 238000005728 strengthening Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 108010066082 tartrate-sensitive acid phosphatase Proteins 0.000 description 1
- TUNFSRHWOTWDNC-HKGQFRNVSA-N tetradecanoic acid Chemical compound CCCCCCCCCCCCC[14C](O)=O TUNFSRHWOTWDNC-HKGQFRNVSA-N 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 201000002311 trypanosomiasis Diseases 0.000 description 1
- 201000008827 tuberculosis Diseases 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 241000712461 unidentified influenza virus Species 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 229940125575 vaccine candidate Drugs 0.000 description 1
- 238000009834 vaporization Methods 0.000 description 1
- 230000008016 vaporization Effects 0.000 description 1
- 230000003442 weekly effect Effects 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
- C07K14/435—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
- C07K14/4727—Mucins, e.g. human intestinal mucin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/10—Cellular immunotherapy characterised by the cell type used
- A61K40/11—T-cells, e.g. tumour infiltrating lymphocytes [TIL] or regulatory T [Treg] cells; Lymphokine-activated killer [LAK] cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/40—Cellular immunotherapy characterised by antigens that are targeted or presented by cells of the immune system
- A61K40/41—Vertebrate antigens
- A61K40/42—Cancer antigens
- A61K40/4256—Tumor associated carbohydrates
- A61K40/4257—Mucins, e.g. MUC-1
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
- A61K2039/55511—Organic adjuvants
- A61K2039/55555—Liposomes; Vesicles, e.g. nanoparticles; Spheres, e.g. nanospheres; Polymers
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Organic Chemistry (AREA)
- Epidemiology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Toxicology (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicinal Preparation (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US4594997P | 1997-05-08 | 1997-05-08 | |
| US45949P | 1997-05-08 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2357960T3 true ES2357960T3 (es) | 2011-05-04 |
Family
ID=21940709
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES05076809T Expired - Lifetime ES2357960T3 (es) | 1997-05-08 | 1998-05-07 | Procedimiento para generar células t activadas y células presentadoras de antígenos pulsadas con antígenos. |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US6600012B1 (enExample) |
| EP (3) | EP1634949B1 (enExample) |
| JP (1) | JP4480800B2 (enExample) |
| AT (2) | ATE491465T1 (enExample) |
| AU (1) | AU727863B2 (enExample) |
| CA (1) | CA2289742C (enExample) |
| DE (2) | DE69839443D1 (enExample) |
| DK (1) | DK1634949T3 (enExample) |
| ES (1) | ES2357960T3 (enExample) |
| WO (1) | WO1998050527A1 (enExample) |
Families Citing this family (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE19906744A1 (de) * | 1999-02-18 | 2000-08-24 | Martin Roecken | Verfahren zur Herstellung antitumoraler Th1-Zellen |
| CA2368967A1 (en) * | 1999-04-09 | 2000-10-19 | Biomira, Inc. | Telomerase-specific cancer vaccine |
| DE19917195B4 (de) * | 1999-04-16 | 2006-09-28 | Immatics Biotechnologies Gmbh | Peptid zur Auslösung einer Immunreaktion gegen Tumorzellen, diese enthaltende pharmzeutische Zusammensetzungen, dessen Verwendungen, dafür codierende Nukleinsäure und diese Nukleinsäure enthaltender Expressionsvektor |
| WO2001018035A2 (en) | 1999-09-08 | 2001-03-15 | Transgene S.A. | Muc-1 derived peptides |
| GB9921337D0 (en) * | 1999-09-09 | 1999-11-10 | Axis Genetics Plc | Modified plant viruses |
| GB0007150D0 (en) * | 2000-03-24 | 2000-05-17 | Lamellar Therapeutics Limited | Immunotherapeutic methods and compositions |
| EP1377275B1 (en) * | 2001-03-27 | 2006-10-25 | Biomira, Inc. | Vaccine for modulating between t1 and t2 immune responses |
| EP1499347A2 (en) | 2002-03-15 | 2005-01-26 | Department of Veterans Affairs, Rehabilitation R&D Service | Methods and compositions using cellular asialodeterminants and glycoconjugates for targeting cells to tissues and organs |
| CA2482477A1 (en) * | 2002-04-15 | 2003-10-30 | Biomira, Inc. | Synthetic glyco-lipo-peptides as vaccines |
| US20060142546A1 (en) * | 2002-09-05 | 2006-06-29 | Franz-Georg Hanisch | Immunogenic muc1 glycopeptides |
| WO2004033667A2 (en) * | 2002-10-10 | 2004-04-22 | Department Of Veterans Affairs | Detection, localization and staging of tumors using labeled activated lymphocytes directed to a tumor specific epitope |
| US20050045205A1 (en) * | 2003-08-29 | 2005-03-03 | Stach Steven R. | Apparatus and method for cleaning printed circuit boards |
| GB0322448D0 (en) | 2003-09-25 | 2003-10-29 | Lamellar Therapeutics Ltd | Using lamellar bodies to modify linear biological macro molecules |
| EP1697399B1 (en) | 2003-12-12 | 2016-11-23 | GOVERNMENT OF THE UNITED STATES OF AMERICA, as repr. by THE SECR. OF THE DEPT. OF HEALTH AND HUMAN SERVICES AND HIS SUCCESSORS | A human cytotoxic t-lymphocyte epitope and its agonist epitope from the non-variable number of tandem repeat sequence of muc-1 |
| TW201204410A (en) | 2004-04-01 | 2012-02-01 | Oncothyreon Inc | Mucinous glycoprotein (MUC-1) vaccine |
| EP1812052A1 (en) * | 2004-11-02 | 2007-08-01 | Biomedical Research Models, Inc. | Methods of cancer treatment/prevention using cancer cell-specific surface antigens |
| TW201615208A (zh) * | 2005-06-28 | 2016-05-01 | 安柯席爾伊恩股份有限公司 | 以黏液性糖蛋白（ｍｕｃ-１）疫苗治療病人之方法 |
| WO2010002478A2 (en) | 2008-07-03 | 2010-01-07 | University Of Georgia Research Foundation, Inc. | Glycopeptide and uses thereof |
| EP2025762A3 (en) | 2006-01-17 | 2009-09-30 | Health Research Inc. | Heteroduplex tracking assay |
| RU2377994C1 (ru) * | 2008-05-21 | 2010-01-10 | Леонид Валентинович Загребин | Способ иммунореабилитации онкозаболеваний |
| US20100059084A1 (en) * | 2008-09-10 | 2010-03-11 | Austin American Technology Corporation | Cleaning and testing ionic cleanliness of electronic assemblies |
| US9597392B2 (en) | 2010-05-10 | 2017-03-21 | Ascend Biopharmaceuticals Pty Ltd. | Use of high molecular weight mannan for inducing and/or enhancing an immune response |
| BR112013021779A2 (pt) | 2011-02-24 | 2017-09-19 | Oncothyreon Inc | vacina de glicolipopeptídeo baseada em muc1 com adjuvante. |
| EP2800762B1 (en) | 2012-01-03 | 2018-01-03 | The United States of America, as represented by the Secretary, Department of Health and Human Services | Native and agonist ctl epitopes of the muc1 tumor antigen |
| BR112015028252A2 (pt) | 2013-05-14 | 2017-07-25 | Merck Patent Gmbh | método de tratamento de câncer de pulmão por vacinação com lipopeptídeo muc-1 |
| WO2015058831A1 (en) | 2013-10-25 | 2015-04-30 | Merck Patent Gmbh | Elevated biomarker expression in lung cancer patients responding to treatment with muc-1 lipopeptide vaccines |
| IL303806B2 (en) | 2016-12-22 | 2024-05-01 | Cue Biopharma Inc | Multimeric polypeptides modulate T cells and methods for their use |
| WO2018129474A1 (en) | 2017-01-09 | 2018-07-12 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| WO2018170168A1 (en) | 2017-03-15 | 2018-09-20 | Cue Biopharma, Inc. | Methods for modulating an immune response |
| GB201812647D0 (en) | 2018-08-03 | 2018-09-19 | Chancellor Masters And Scholars Of The Univ Of Oxford | Viral vectors and methods for the prevention or treatment of cancer |
| WO2020257191A1 (en) * | 2019-06-19 | 2020-12-24 | Cue Biopharma, Inc. | Multimeric t-cell modulatory polypeptides and methods of use thereof |
| IL296209A (en) | 2020-05-12 | 2022-11-01 | Cue Biopharma Inc | Multimeric t-cell modulatory polypeptides and methods of using them |
| JP2023541366A (ja) | 2020-09-09 | 2023-10-02 | キュー バイオファーマ， インコーポレイテッド | １型真性糖尿病（ｔ１ｄ）を治療するためのｍｈｃクラスｉｉ ｔ細胞調節多量体ポリペプチド及びその使用方法 |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE69511410T2 (de) | 1994-06-13 | 1999-12-16 | Unilever N.V., Rotterdam | Bleichaktivierung |
| CA2192655A1 (en) * | 1994-06-14 | 1995-12-21 | Edgar G. Engleman | Methods for in vivo t cell activation by antigen-pulsed dendritic cells |
| AU5849796A (en) * | 1994-12-27 | 1996-08-07 | United Biomedical Inc. | Peptide ratchet libraries for ctl-inducing vaccines and therapeutics |
| AU6330896A (en) * | 1995-06-07 | 1996-12-30 | Governors Of The University Of Alberta, The | A method for eliciting a th1-specific immune response |
| WO1998037095A2 (en) | 1997-02-24 | 1998-08-27 | Therion Biologics Corporation | Recombinant pox virus for immunization against muc1 tumor-associated antigen |
-
1998
- 1998-05-07 JP JP54847798A patent/JP4480800B2/ja not_active Expired - Fee Related
- 1998-05-07 DK DK05076809.2T patent/DK1634949T3/da active
- 1998-05-07 EP EP05076809A patent/EP1634949B1/en not_active Expired - Lifetime
- 1998-05-07 ES ES05076809T patent/ES2357960T3/es not_active Expired - Lifetime
- 1998-05-07 CA CA2289742A patent/CA2289742C/en not_active Expired - Fee Related
- 1998-05-07 DE DE69839443T patent/DE69839443D1/de not_active Expired - Lifetime
- 1998-05-07 AU AU73712/98A patent/AU727863B2/en not_active Ceased
- 1998-05-07 AT AT05076809T patent/ATE491465T1/de active
- 1998-05-07 AT AT98921011T patent/ATE394474T1/de not_active IP Right Cessation
- 1998-05-07 WO PCT/US1998/009288 patent/WO1998050527A1/en not_active Ceased
- 1998-05-07 EP EP98921011A patent/EP0986636B1/en not_active Expired - Lifetime
- 1998-05-07 EP EP10180388.0A patent/EP2341072A3/en not_active Withdrawn
- 1998-05-07 DE DE69842060T patent/DE69842060D1/de not_active Expired - Lifetime
-
2000
- 2000-02-03 US US09/497,232 patent/US6600012B1/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| US6600012B1 (en) | 2003-07-29 |
| CA2289742C (en) | 2013-07-16 |
| EP0986636A1 (en) | 2000-03-22 |
| JP4480800B2 (ja) | 2010-06-16 |
| EP2341072A3 (en) | 2013-10-30 |
| EP1634949A1 (en) | 2006-03-15 |
| ATE394474T1 (de) | 2008-05-15 |
| DE69839443D1 (de) | 2008-06-19 |
| DK1634949T3 (da) | 2011-03-28 |
| AU727863B2 (en) | 2001-01-04 |
| ATE491465T1 (de) | 2011-01-15 |
| EP0986636B1 (en) | 2008-05-07 |
| JP2001525668A (ja) | 2001-12-11 |
| AU7371298A (en) | 1998-11-27 |
| CA2289742A1 (en) | 1998-11-12 |
| EP2341072A2 (en) | 2011-07-06 |
| WO1998050527A1 (en) | 1998-11-12 |
| EP1634949B1 (en) | 2010-12-15 |
| DE69842060D1 (de) | 2011-01-27 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2357960T3 (es) | Procedimiento para generar células t activadas y células presentadoras de antígenos pulsadas con antígenos. | |
| US8552145B2 (en) | Vaccine for modulating between T1 and T2 immune responses | |
| TW514530B (en) | Tumor vaccines and methods for their production | |
| Agrawal et al. | Rapid induction of primary human CD4+ and CD8+ T cell responses against cancer-associated MUC1 peptide epitopes. | |
| EP4045150A1 (en) | Immunogenic compounds for treatment of adrenal cancer | |
| JP4592702B2 (ja) | ＮＹ−ＥＳＯ−１とアジュバントのｉｎｖｉｖｏ有効性 | |
| JP2002541811A (ja) | テロメラーゼ特異的癌ワクチン | |
| AU2002309141A1 (en) | Vaccine for modulating between T1 and T2 immune responses | |
| US20020018806A1 (en) | Lipopeptide adjuvants | |
| US20210283237A1 (en) | Vaccine compositions | |
| EP1852126A2 (en) | Vaccine for modulating between T1 and T2 immune responses | |
| AU4111999A (en) | Induction of anti-tumor cytotoxic T lymphocytes in humans using synthetic peptide epitopes |