UA79235C2 - Il-18 mutant polypeptide, extracted dna coded il-18 mutant polypeptide, vector and pharmaceutical composition - Google Patents
Il-18 mutant polypeptide, extracted dna coded il-18 mutant polypeptide, vector and pharmaceutical composition Download PDFInfo
- Publication number
- UA79235C2 UA79235C2 UA2003109084A UA2003109084A UA79235C2 UA 79235 C2 UA79235 C2 UA 79235C2 UA 2003109084 A UA2003109084 A UA 2003109084A UA 2003109084 A UA2003109084 A UA 2003109084A UA 79235 C2 UA79235 C2 UA 79235C2
- Authority
- UA
- Ukraine
- Prior art keywords
- avr
- cells
- bek
- biu
- iem
- Prior art date
Links
- 239000013598 vector Substances 0.000 title abstract description 19
- 108090000765 processed proteins & peptides Proteins 0.000 title abstract description 13
- 229920001184 polypeptide Polymers 0.000 title abstract description 10
- 102000004196 processed proteins & peptides Human genes 0.000 title abstract description 10
- 239000008194 pharmaceutical composition Substances 0.000 title abstract description 6
- 230000035772 mutation Effects 0.000 abstract description 23
- 239000002299 complementary DNA Substances 0.000 abstract description 12
- 230000003993 interaction Effects 0.000 abstract description 4
- 238000006467 substitution reaction Methods 0.000 abstract description 4
- 102000003810 Interleukin-18 Human genes 0.000 abstract description 3
- 108090000171 Interleukin-18 Proteins 0.000 abstract description 3
- 125000000539 amino acid group Chemical group 0.000 abstract description 2
- 102000044166 interleukin-18 binding protein Human genes 0.000 abstract 1
- 108010070145 interleukin-18 binding protein Proteins 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 56
- 108090000623 proteins and genes Proteins 0.000 description 41
- 102000004169 proteins and genes Human genes 0.000 description 34
- 235000018102 proteins Nutrition 0.000 description 32
- 102220554136 APC membrane recruitment protein 1_E42A_mutation Human genes 0.000 description 28
- 108020004414 DNA Proteins 0.000 description 26
- 238000006243 chemical reaction Methods 0.000 description 24
- 206010028980 Neoplasm Diseases 0.000 description 20
- 239000002243 precursor Substances 0.000 description 16
- 230000000694 effects Effects 0.000 description 14
- 238000004519 manufacturing process Methods 0.000 description 14
- 102000004127 Cytokines Human genes 0.000 description 13
- 108090000695 Cytokines Proteins 0.000 description 13
- 150000001413 amino acids Chemical group 0.000 description 13
- 108010074860 Factor Xa Proteins 0.000 description 12
- 108010076504 Protein Sorting Signals Proteins 0.000 description 12
- 238000003776 cleavage reaction Methods 0.000 description 12
- 230000014509 gene expression Effects 0.000 description 11
- 230000007017 scission Effects 0.000 description 11
- 239000012634 fragment Substances 0.000 description 10
- 235000010469 Glycine max Nutrition 0.000 description 9
- 235000001014 amino acid Nutrition 0.000 description 9
- 229940024606 amino acid Drugs 0.000 description 9
- 102220553782 APC membrane recruitment protein 1_K89A_mutation Human genes 0.000 description 8
- 244000068988 Glycine max Species 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 8
- 230000006698 induction Effects 0.000 description 8
- 230000001939 inductive effect Effects 0.000 description 8
- 241000699666 Mus <mouse, genus> Species 0.000 description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 description 7
- 239000011159 matrix material Substances 0.000 description 7
- 238000006386 neutralization reaction Methods 0.000 description 7
- 230000004044 response Effects 0.000 description 7
- 230000002441 reversible effect Effects 0.000 description 7
- 230000009471 action Effects 0.000 description 6
- 241000699670 Mus sp. Species 0.000 description 5
- 208000027697 autoimmune lymphoproliferative syndrome due to CTLA4 haploinsuffiency Diseases 0.000 description 5
- 230000004071 biological effect Effects 0.000 description 5
- 201000011510 cancer Diseases 0.000 description 5
- 210000004443 dendritic cell Anatomy 0.000 description 5
- 235000014304 histidine Nutrition 0.000 description 5
- 230000001965 increasing effect Effects 0.000 description 5
- 238000000034 method Methods 0.000 description 5
- 239000013612 plasmid Substances 0.000 description 5
- 230000028327 secretion Effects 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 4
- 230000000735 allogeneic effect Effects 0.000 description 4
- 239000000427 antigen Substances 0.000 description 4
- 102000036639 antigens Human genes 0.000 description 4
- 108091007433 antigens Proteins 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 239000002158 endotoxin Substances 0.000 description 4
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 4
- 201000001441 melanoma Diseases 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 230000000638 stimulation Effects 0.000 description 4
- 238000002054 transplantation Methods 0.000 description 4
- 230000003612 virological effect Effects 0.000 description 4
- IJJWOSAXNHWBPR-HUBLWGQQSA-N 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-n-(6-hydrazinyl-6-oxohexyl)pentanamide Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)NCCCCCC(=O)NN)SC[C@@H]21 IJJWOSAXNHWBPR-HUBLWGQQSA-N 0.000 description 3
- 102000002265 Human Growth Hormone Human genes 0.000 description 3
- 108010000521 Human Growth Hormone Proteins 0.000 description 3
- 239000000854 Human Growth Hormone Substances 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- 241001529936 Murinae Species 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 230000003321 amplification Effects 0.000 description 3
- 230000000259 anti-tumor effect Effects 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 239000000411 inducer Substances 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 210000004185 liver Anatomy 0.000 description 3
- PKAHQJNJPDVTDP-UHFFFAOYSA-N methyl cyclopropanecarboxylate Chemical compound COC(=O)C1CC1 PKAHQJNJPDVTDP-UHFFFAOYSA-N 0.000 description 3
- 238000012544 monitoring process Methods 0.000 description 3
- 230000003472 neutralizing effect Effects 0.000 description 3
- 238000003199 nucleic acid amplification method Methods 0.000 description 3
- 102000005962 receptors Human genes 0.000 description 3
- 108020003175 receptors Proteins 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 108090000669 Annexin A4 Proteins 0.000 description 2
- 102100034612 Annexin A4 Human genes 0.000 description 2
- 108090000426 Caspase-1 Proteins 0.000 description 2
- 102100035904 Caspase-1 Human genes 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 108091035707 Consensus sequence Proteins 0.000 description 2
- 230000004544 DNA amplification Effects 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 108010051696 Growth Hormone Proteins 0.000 description 2
- 102000008300 Mutant Proteins Human genes 0.000 description 2
- 108010021466 Mutant Proteins Proteins 0.000 description 2
- 102000001708 Protein Isoforms Human genes 0.000 description 2
- 108010029485 Protein Isoforms Proteins 0.000 description 2
- 238000007792 addition Methods 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 238000007664 blowing Methods 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 102000003675 cytokine receptors Human genes 0.000 description 2
- 108010057085 cytokine receptors Proteins 0.000 description 2
- 230000007123 defense Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- 238000009169 immunotherapy Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 231100000518 lethal Toxicity 0.000 description 2
- 230000001665 lethal effect Effects 0.000 description 2
- 208000032839 leukemia Diseases 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 229920006008 lipopolysaccharide Polymers 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- SYSZENVIJHPFNL-UHFFFAOYSA-N (alpha-D-mannosyl)7-beta-D-mannosyl-diacetylchitobiosyl-L-asparagine, isoform B (protein) Chemical compound COC1=CC=C(I)C=C1 SYSZENVIJHPFNL-UHFFFAOYSA-N 0.000 description 1
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- PXFBZOLANLWPMH-UHFFFAOYSA-N 16-Epiaffinine Natural products C1C(C2=CC=CC=C2N2)=C2C(=O)CC2C(=CC)CN(C)C1C2CO PXFBZOLANLWPMH-UHFFFAOYSA-N 0.000 description 1
- RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 241000534414 Anotopterus nikparini Species 0.000 description 1
- 241000726103 Atta Species 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 101100454194 Caenorhabditis elegans mei-1 gene Proteins 0.000 description 1
- 101100401100 Caenorhabditis elegans mes-1 gene Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 238000011238 DNA vaccination Methods 0.000 description 1
- 241000887108 Dicoma Species 0.000 description 1
- 101100163433 Drosophila melanogaster armi gene Proteins 0.000 description 1
- 101100536354 Drosophila melanogaster tant gene Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 101710134987 Esterase 6 Proteins 0.000 description 1
- UOACKFBJUYNSLK-XRKIENNPSA-N Estradiol Cypionate Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H](C4=CC=C(O)C=C4CC3)CC[C@@]21C)C(=O)CCC1CCCC1 UOACKFBJUYNSLK-XRKIENNPSA-N 0.000 description 1
- 102000018997 Growth Hormone Human genes 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 241001562081 Ikeda Species 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000013462 Interleukin-12 Human genes 0.000 description 1
- 108010065805 Interleukin-12 Proteins 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 1
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 206010027455 Metastases to kidney Diseases 0.000 description 1
- 101100460719 Mus musculus Noto gene Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 241001387976 Pera Species 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 108010093965 Polymyxin B Proteins 0.000 description 1
- 108010040201 Polymyxins Proteins 0.000 description 1
- 208000037062 Polyps Diseases 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 208000006265 Renal cell carcinoma Diseases 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 241000710209 Theiler's encephalomyelitis virus Species 0.000 description 1
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 1
- 241000533793 Tipuana tipu Species 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 101100187345 Xenopus laevis noto gene Proteins 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 238000011224 anti-cancer immunotherapy Methods 0.000 description 1
- 230000000947 anti-immunosuppressive effect Effects 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 201000008275 breast carcinoma Diseases 0.000 description 1
- 238000002619 cancer immunotherapy Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000004939 coking Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 230000035622 drinking Effects 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000010304 firing Methods 0.000 description 1
- -1 for example Proteins 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 238000012239 gene modification Methods 0.000 description 1
- 230000005017 genetic modification Effects 0.000 description 1
- 235000013617 genetically modified food Nutrition 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 210000002443 helper t lymphocyte Anatomy 0.000 description 1
- 150000002411 histidines Chemical class 0.000 description 1
- 230000007124 immune defense Effects 0.000 description 1
- 208000026278 immune system disease Diseases 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 229940117681 interleukin-12 Drugs 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000001865 kupffer cell Anatomy 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 108020001756 ligand binding domains Proteins 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 235000019988 mead Nutrition 0.000 description 1
- 230000010534 mechanism of action Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 230000001400 myeloablative effect Effects 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 150000007523 nucleic acids Chemical group 0.000 description 1
- 231100000590 oncogenic Toxicity 0.000 description 1
- 230000002246 oncogenic effect Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 210000002997 osteoclast Anatomy 0.000 description 1
- BVURVTVDNWSNFN-UHFFFAOYSA-N pepap Chemical compound C1CC(OC(=O)C)(C=2C=CC=CC=2)CCN1CCC1=CC=CC=C1 BVURVTVDNWSNFN-UHFFFAOYSA-N 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 210000004976 peripheral blood cell Anatomy 0.000 description 1
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 229920000024 polymyxin B Polymers 0.000 description 1
- 229960005266 polymyxin b Drugs 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 238000011155 quantitative monitoring Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 235000002020 sage Nutrition 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000007910 systemic administration Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000002110 toxicologic effect Effects 0.000 description 1
- 231100000027 toxicology Toxicity 0.000 description 1
- 238000009966 trimming Methods 0.000 description 1
- 210000002700 urine Anatomy 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- 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
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- 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)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Virology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US27432701P | 2001-03-08 | 2001-03-08 | |
PCT/IB2002/002344 WO2002101049A2 (en) | 2001-03-08 | 2002-03-08 | Interleukin-18 mutants, their production and use |
Publications (1)
Publication Number | Publication Date |
---|---|
UA79235C2 true UA79235C2 (en) | 2007-06-11 |
Family
ID=23047735
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
UA2003109084A UA79235C2 (en) | 2001-03-08 | 2002-08-03 | Il-18 mutant polypeptide, extracted dna coded il-18 mutant polypeptide, vector and pharmaceutical composition |
Country Status (19)
Country | Link |
---|---|
US (2) | US7524488B2 (pt) |
EP (1) | EP1392830B1 (pt) |
JP (1) | JP2004530432A (pt) |
KR (1) | KR100862136B1 (pt) |
CN (1) | CN100503829C (pt) |
AT (1) | ATE315647T1 (pt) |
AU (1) | AU2002324249B2 (pt) |
BR (1) | BRPI0207933B8 (pt) |
CA (1) | CA2438851C (pt) |
DE (1) | DE60208692T2 (pt) |
DK (1) | DK1392830T3 (pt) |
EA (1) | EA005769B1 (pt) |
ES (1) | ES2251610T3 (pt) |
HK (1) | HK1084151A1 (pt) |
IL (2) | IL157800A0 (pt) |
MX (1) | MXPA03008110A (pt) |
SI (1) | SI1392830T1 (pt) |
UA (1) | UA79235C2 (pt) |
WO (1) | WO2002101049A2 (pt) |
Families Citing this family (23)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE602004031341D1 (de) | 2003-07-21 | 2011-03-24 | Transgene Sa | Multifunktionelle cytokine |
CA2531773A1 (en) | 2003-07-21 | 2005-02-17 | Transgene S.A. | Novel multifunctional cytokines |
JP4741504B2 (ja) * | 2003-11-05 | 2011-08-03 | アレス トレーディング ソシエテ アノニム | Il−18結合タンパク質の精製方法 |
US7557084B2 (en) * | 2004-03-31 | 2009-07-07 | Regeneron Pharmaceuticals, Inc. | IL-18 specific polypeptides and therapeutic uses thereof |
SI2267024T1 (sl) | 2005-06-03 | 2012-09-28 | Ares Trading Sa | Proizvodnja rekombinantnega IL-18 vezavnega proteina |
ES2375831T3 (es) | 2005-06-10 | 2012-03-06 | Ares Trading S.A. | Procedimiento para la purificación de prote�?nas de unión a il-18. |
CN101177454B (zh) * | 2007-05-09 | 2010-09-22 | 郑骏年 | Il-18突变体多肽及制备及用途 |
WO2012078936A2 (en) * | 2010-12-10 | 2012-06-14 | Glaxosmithkline Llc | Methods to produce a purified peptide chain fraction |
CN111315395A (zh) * | 2017-09-06 | 2020-06-19 | 耶鲁大学 | 白细胞介素-18变体和使用方法 |
US12029778B2 (en) | 2019-05-13 | 2024-07-09 | Yale University | Interleukin-18 mimics and methods of use |
JP2021170968A (ja) * | 2020-04-22 | 2021-11-01 | 国立大学法人 長崎大学 | マウスil−18の製造方法及びそのための組換えdna |
US20220056091A1 (en) * | 2020-08-19 | 2022-02-24 | Bright Peak Therapeutics Ag | Modified il-18 polypeptides and uses thereof |
WO2022094473A1 (en) | 2020-11-02 | 2022-05-05 | Simcha IL-18, Inc. | Interleukin-18 variants and methods of use |
US20240150421A1 (en) * | 2021-02-10 | 2024-05-09 | Nagasaki University | Novel human interleukin-18 variant and use thereof |
WO2023010021A1 (en) | 2021-07-27 | 2023-02-02 | Xencor, Inc. | Il-18-fc fusion proteins |
JP2023024168A (ja) | 2021-08-06 | 2023-02-16 | 国立大学法人 長崎大学 | がんの治療剤 |
WO2023056193A2 (en) * | 2021-09-29 | 2023-04-06 | Chimera Bioengineering, Inc. | Il-18 variants and uses thereof |
WO2023118497A1 (en) * | 2021-12-22 | 2023-06-29 | Pieris Pharmaceuticals Gmbh | Novel il-18 variants |
WO2023161853A1 (en) | 2022-02-23 | 2023-08-31 | Bright Peak Therapeutics Ag | Activatable il-18 polypeptides |
WO2023161856A1 (en) * | 2022-02-23 | 2023-08-31 | Bright Peak Therapeutics Ag | Modified il-18 polypeptides |
US20230355795A1 (en) * | 2022-02-23 | 2023-11-09 | Bright Peak Therapeutics Ag | Immune antigen specific il-18 immunocytokines and uses thereof |
WO2024044780A1 (en) * | 2022-08-26 | 2024-02-29 | Sutro Biopharma, Inc. | Interleukin-18 variants and uses thereof |
US20240166705A1 (en) | 2022-11-07 | 2024-05-23 | Xencor, Inc. | Il18-fc fusion proteins |
Family Cites Families (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP4024366B2 (ja) * | 1996-11-29 | 2007-12-19 | 株式会社林原生物化学研究所 | ポリペプチド |
TWI227136B (en) * | 1998-05-21 | 2005-02-01 | Smithkline Beecham Corp | Novel pharmaceutical composition for the prevention and/or treatment of cancer |
IL129427A0 (en) | 1999-04-13 | 2000-02-17 | Yeda Res & Dev | Preparation of biologically active molecules |
-
2002
- 2002-03-08 IL IL15780002A patent/IL157800A0/xx unknown
- 2002-03-08 DE DE60208692T patent/DE60208692T2/de not_active Expired - Lifetime
- 2002-03-08 MX MXPA03008110A patent/MXPA03008110A/es active IP Right Grant
- 2002-03-08 AT AT02758668T patent/ATE315647T1/de active
- 2002-03-08 CA CA2438851A patent/CA2438851C/en not_active Expired - Lifetime
- 2002-03-08 US US10/094,153 patent/US7524488B2/en not_active Expired - Lifetime
- 2002-03-08 EA EA200300987A patent/EA005769B1/ru not_active IP Right Cessation
- 2002-03-08 SI SI200230280T patent/SI1392830T1/sl unknown
- 2002-03-08 JP JP2003503799A patent/JP2004530432A/ja active Pending
- 2002-03-08 ES ES02758668T patent/ES2251610T3/es not_active Expired - Lifetime
- 2002-03-08 DK DK02758668T patent/DK1392830T3/da active
- 2002-03-08 CN CNB02809803XA patent/CN100503829C/zh not_active Expired - Lifetime
- 2002-03-08 AU AU2002324249A patent/AU2002324249B2/en not_active Expired
- 2002-03-08 BR BR0207933-0 patent/BRPI0207933B8/pt not_active IP Right Cessation
- 2002-03-08 KR KR1020037011581A patent/KR100862136B1/ko active IP Right Grant
- 2002-03-08 WO PCT/IB2002/002344 patent/WO2002101049A2/en active IP Right Grant
- 2002-03-08 EP EP02758668A patent/EP1392830B1/en not_active Expired - Lifetime
- 2002-08-03 UA UA2003109084A patent/UA79235C2/uk unknown
-
2003
- 2003-09-08 IL IL157800A patent/IL157800A/en unknown
-
2006
- 2006-06-06 HK HK06106439.0A patent/HK1084151A1/xx not_active IP Right Cessation
-
2009
- 2009-03-16 US US12/404,458 patent/US7875709B2/en not_active Expired - Fee Related
Also Published As
Publication number | Publication date |
---|---|
DE60208692D1 (de) | 2006-04-06 |
BRPI0207933B8 (pt) | 2021-05-25 |
MXPA03008110A (es) | 2003-12-12 |
US20090286855A1 (en) | 2009-11-19 |
EP1392830A2 (en) | 2004-03-03 |
CN1764723A (zh) | 2006-04-26 |
EA200300987A1 (ru) | 2004-02-26 |
US7875709B2 (en) | 2011-01-25 |
HK1084151A1 (en) | 2006-07-21 |
CA2438851A1 (en) | 2002-12-19 |
BRPI0207933B1 (pt) | 2020-11-24 |
WO2002101049A2 (en) | 2002-12-19 |
DE60208692T2 (de) | 2006-07-13 |
CN100503829C (zh) | 2009-06-24 |
ATE315647T1 (de) | 2006-02-15 |
US7524488B2 (en) | 2009-04-28 |
IL157800A0 (en) | 2004-03-28 |
DK1392830T3 (da) | 2006-05-08 |
EA005769B1 (ru) | 2005-06-30 |
KR20030088448A (ko) | 2003-11-19 |
EP1392830B1 (en) | 2006-01-11 |
BR0207933A (pt) | 2004-03-02 |
SI1392830T1 (sl) | 2006-06-30 |
CA2438851C (en) | 2011-07-26 |
AU2002324249B2 (en) | 2007-04-05 |
ES2251610T3 (es) | 2006-05-01 |
IL157800A (en) | 2009-08-03 |
US20020169291A1 (en) | 2002-11-14 |
JP2004530432A (ja) | 2004-10-07 |
KR100862136B1 (ko) | 2008-10-09 |
WO2002101049A3 (en) | 2003-12-18 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
UA79235C2 (en) | Il-18 mutant polypeptide, extracted dna coded il-18 mutant polypeptide, vector and pharmaceutical composition | |
Chen et al. | T-cell immunity to the joining region of p210BCR-ABL protein. | |
Morgan et al. | Recognition of glioma stem cells by genetically modified T cells targeting EGFRvIII and development of adoptive cell therapy for glioma | |
CA2906587C (en) | Compositions and methods for use of recombinant t cell receptors for direct recognition of tumor antigen | |
CN108504668A (zh) | 靶向cd19和cd22嵌合抗原受体及其用途 | |
EP3842051A1 (en) | Therapeutic agent comprising nucleic acid and car-modified immune cell and application thereof | |
CN101835892A (zh) | Cdca1肽和包含cdca1肽的药剂 | |
CN109320615A (zh) | 靶向新型bcma的嵌合抗原受体及其用途 | |
Valencia et al. | Interleukin-2 as immunotherapeutic in the autoimmune diseases | |
CN113727720A (zh) | 用于治疗表达cldn6的癌症的嵌合抗原受体修饰的细胞 | |
US20080125390A1 (en) | Methods for Modulating Immune and Inflammatory Responses | |
CN109423495A (zh) | 一种双靶向嵌合抗原受体及其用途 | |
CA3119472A1 (en) | Split interleukin mimetics and their use | |
CN108866088A (zh) | 靶向cll-1嵌合抗原受体及其用途 | |
US11098283B2 (en) | T cells modified to overexpress c-Myb | |
AU2006327514B2 (en) | DNA vaccine for cancer therapy | |
Fujii et al. | Cancer immunotherapy using artificial adjuvant vector cells to deliver NY‐ESO‐1 antigen to dendritic cells in situ | |
CN116970058B (zh) | 针对tp53基因r249s突变的肿瘤新抗原多肽及其应用 | |
Xu et al. | Interleukins in the treatment of melanoma | |
US20240018213A1 (en) | Modulators of notch signaling and methods of use thereof | |
KR20220052987A (ko) | Ebv 유래 항원에 특이적인 tcr 작제물 | |
EP3683229A1 (en) | Specific t cell receptors against epitopes of mutant myd88l265p protein for adoptive t cell therapy | |
US20240009239A1 (en) | Therapeutic targeting of mesothelin in acute myeloid leukemia with chimeric antigen receptor t cell therapy | |
CN108424458A (zh) | 靶向ny-eso-1的嵌合抗原受体及其用途 | |
CN108864276A (zh) | 靶向ny-eso-1的t细胞受体联合表达pd1抗体可变区及其用途 |