NO321984B1 - Konjugat, fremstilling, samt anvendelse derav - Google Patents
Konjugat, fremstilling, samt anvendelse derav Download PDFInfo
- Publication number
- NO321984B1 NO321984B1 NO19975435A NO975435A NO321984B1 NO 321984 B1 NO321984 B1 NO 321984B1 NO 19975435 A NO19975435 A NO 19975435A NO 975435 A NO975435 A NO 975435A NO 321984 B1 NO321984 B1 NO 321984B1
- Authority
- NO
- Norway
- Prior art keywords
- superantigen
- see
- sea
- amino acid
- binding
- Prior art date
Links
- 238000002360 preparation method Methods 0.000 title claims description 6
- 231100000617 superantigen Toxicity 0.000 claims description 130
- 101000686985 Mouse mammary tumor virus (strain C3H) Protein PR73 Proteins 0.000 claims description 83
- 210000004027 cell Anatomy 0.000 claims description 63
- 108091054438 MHC class II family Proteins 0.000 claims description 53
- 102000043131 MHC class II family Human genes 0.000 claims description 52
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 43
- 108091008874 T cell receptors Proteins 0.000 claims description 37
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 claims description 37
- 125000000539 amino acid group Chemical group 0.000 claims description 29
- 230000003013 cytotoxicity Effects 0.000 claims description 26
- 231100000135 cytotoxicity Toxicity 0.000 claims description 26
- 230000035772 mutation Effects 0.000 claims description 24
- 230000008685 targeting Effects 0.000 claims description 21
- 239000000427 antigen Substances 0.000 claims description 18
- 108091007433 antigens Proteins 0.000 claims description 18
- 102000036639 antigens Human genes 0.000 claims description 18
- 201000010099 disease Diseases 0.000 claims description 18
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 18
- 239000000203 mixture Substances 0.000 claims description 18
- 238000006467 substitution reaction Methods 0.000 claims description 16
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 14
- 206010028980 Neoplasm Diseases 0.000 claims description 13
- 230000002829 reductive effect Effects 0.000 claims description 11
- 201000011510 cancer Diseases 0.000 claims description 10
- 230000004927 fusion Effects 0.000 claims description 9
- 230000006044 T cell activation Effects 0.000 claims description 8
- 241000124008 Mammalia Species 0.000 claims description 6
- 239000003814 drug Substances 0.000 claims description 5
- 230000001976 improved effect Effects 0.000 claims description 5
- 208000023275 Autoimmune disease Diseases 0.000 claims description 4
- 208000030852 Parasitic disease Diseases 0.000 claims description 4
- 208000036142 Viral infection Diseases 0.000 claims description 4
- 230000003213 activating effect Effects 0.000 claims description 4
- 229940079593 drug Drugs 0.000 claims description 4
- 230000009385 viral infection Effects 0.000 claims description 4
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 3
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 3
- 210000000987 immune system Anatomy 0.000 claims description 3
- 230000001939 inductive effect Effects 0.000 claims description 3
- 102200097287 rs199473486 Human genes 0.000 claims description 3
- 102220011740 rs386833408 Human genes 0.000 claims description 3
- 102220046159 rs587782693 Human genes 0.000 claims description 3
- 230000000694 effects Effects 0.000 description 29
- 108090000623 proteins and genes Proteins 0.000 description 18
- 230000001419 dependent effect Effects 0.000 description 16
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 15
- 231100000655 enterotoxin Toxicity 0.000 description 15
- 238000003556 assay Methods 0.000 description 14
- 108020001507 fusion proteins Proteins 0.000 description 14
- 102000037865 fusion proteins Human genes 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 14
- 235000001014 amino acid Nutrition 0.000 description 13
- 235000018102 proteins Nutrition 0.000 description 12
- 239000012636 effector Substances 0.000 description 11
- 239000012634 fragment Substances 0.000 description 10
- 241001529936 Murinae Species 0.000 description 9
- 210000004408 hybridoma Anatomy 0.000 description 9
- 230000003993 interaction Effects 0.000 description 9
- 230000005889 cellular cytotoxicity Effects 0.000 description 8
- 238000000034 method Methods 0.000 description 8
- 238000012986 modification Methods 0.000 description 8
- 230000004048 modification Effects 0.000 description 8
- 238000003752 polymerase chain reaction Methods 0.000 description 8
- 238000004519 manufacturing process Methods 0.000 description 7
- 238000010276 construction Methods 0.000 description 6
- 230000035755 proliferation Effects 0.000 description 6
- 230000004044 response Effects 0.000 description 6
- 101000914484 Homo sapiens T-lymphocyte activation antigen CD80 Proteins 0.000 description 5
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 5
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 5
- 102000000588 Interleukin-2 Human genes 0.000 description 5
- 108010002350 Interleukin-2 Proteins 0.000 description 5
- 102100027222 T-lymphocyte activation antigen CD80 Human genes 0.000 description 5
- 150000001413 amino acids Chemical class 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 239000000147 enterotoxin Substances 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 210000002966 serum Anatomy 0.000 description 5
- 238000002560 therapeutic procedure Methods 0.000 description 5
- 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 4
- 102000004127 Cytokines Human genes 0.000 description 4
- 108090000695 Cytokines Proteins 0.000 description 4
- 102000018713 Histocompatibility Antigens Class II Human genes 0.000 description 4
- 230000004913 activation Effects 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000008859 change Effects 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 3
- 108010027412 Histocompatibility Antigens Class II Proteins 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- 101710192266 Tegument protein VP22 Proteins 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 230000009089 cytolysis Effects 0.000 description 3
- 231100000433 cytotoxic Toxicity 0.000 description 3
- 230000001472 cytotoxic effect Effects 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 230000003472 neutralizing effect Effects 0.000 description 3
- 239000008194 pharmaceutical composition Substances 0.000 description 3
- 102220032372 rs104895229 Human genes 0.000 description 3
- 102200090720 rs137852501 Human genes 0.000 description 3
- 102220038736 rs532961259 Human genes 0.000 description 3
- 102220014798 rs56204273 Human genes 0.000 description 3
- 102200131361 rs57793737 Human genes 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 229940104230 thymidine Drugs 0.000 description 3
- 206010057248 Cell death Diseases 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- 101710146739 Enterotoxin Proteins 0.000 description 2
- 101710204426 Enterotoxin type A Proteins 0.000 description 2
- 101000867232 Escherichia coli Heat-stable enterotoxin II Proteins 0.000 description 2
- 102100040837 Galactoside alpha-(1,2)-fucosyltransferase 2 Human genes 0.000 description 2
- 101000893710 Homo sapiens Galactoside alpha-(1,2)-fucosyltransferase 2 Proteins 0.000 description 2
- 101001018111 Infectious salmon anemia virus (isolate Atlantic salmon/Norway/810/9/99) Matrix protein 1 Proteins 0.000 description 2
- 125000000415 L-cysteinyl group Chemical group O=C([*])[C@@](N([H])[H])([H])C([H])([H])S[H] 0.000 description 2
- 241000713333 Mouse mammary tumor virus Species 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 101000882406 Staphylococcus aureus Enterotoxin type C-1 Proteins 0.000 description 2
- 101000882403 Staphylococcus aureus Enterotoxin type C-2 Proteins 0.000 description 2
- 101000794214 Staphylococcus aureus Toxic shock syndrome toxin-1 Proteins 0.000 description 2
- 230000006052 T cell proliferation Effects 0.000 description 2
- 101710101607 Toxic shock syndrome toxin-1 Proteins 0.000 description 2
- 101710120037 Toxin CcdB Proteins 0.000 description 2
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
- PTFCDOFLOPIGGS-UHFFFAOYSA-N Zinc dication Chemical compound [Zn+2] PTFCDOFLOPIGGS-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 238000001516 cell proliferation assay Methods 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 230000007402 cytotoxic response Effects 0.000 description 2
- 238000002784 cytotoxicity assay Methods 0.000 description 2
- 231100000263 cytotoxicity test Toxicity 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 108010022946 erythrogenic toxin Proteins 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 125000001165 hydrophobic group Chemical group 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 230000004073 interleukin-2 production Effects 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 238000011275 oncology therapy Methods 0.000 description 2
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000002062 proliferating effect Effects 0.000 description 2
- 238000010188 recombinant method Methods 0.000 description 2
- 230000000284 resting effect Effects 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- DAEPDZWVDSPTHF-UHFFFAOYSA-M sodium pyruvate Chemical compound [Na+].CC(=O)C([O-])=O DAEPDZWVDSPTHF-UHFFFAOYSA-M 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 239000003053 toxin Substances 0.000 description 2
- 231100000765 toxin Toxicity 0.000 description 2
- 108700012359 toxins Proteins 0.000 description 2
- 230000005909 tumor killing Effects 0.000 description 2
- 102000003390 tumor necrosis factor Human genes 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-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
- KHOITXIGCFIULA-UHFFFAOYSA-N Alophen Chemical compound C1=CC(OC(=O)C)=CC=C1C(C=1N=CC=CC=1)C1=CC=C(OC(C)=O)C=C1 KHOITXIGCFIULA-UHFFFAOYSA-N 0.000 description 1
- 208000003950 B-cell lymphoma Diseases 0.000 description 1
- 108010077805 Bacterial Proteins Proteins 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 102220617552 Caspase-1_D70A_mutation Human genes 0.000 description 1
- 241001112695 Clostridiales Species 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 241001646716 Escherichia coli K-12 Species 0.000 description 1
- 241000027294 Fusi Species 0.000 description 1
- 229930182566 Gentamicin Natural products 0.000 description 1
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 1
- BUEFQXUHTUZXHR-LURJTMIESA-N Gly-Gly-Pro zwitterion Chemical compound NCC(=O)NCC(=O)N1CCC[C@H]1C(O)=O BUEFQXUHTUZXHR-LURJTMIESA-N 0.000 description 1
- 101100005713 Homo sapiens CD4 gene Proteins 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 101710194492 SET-binding protein Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 101001057112 Staphylococcus aureus Enterotoxin type D Proteins 0.000 description 1
- 108700037929 Streptococcus pyogenes SpeA Proteins 0.000 description 1
- 231100000650 Toxic shock syndrome Toxicity 0.000 description 1
- 206010044250 Toxic shock syndrome staphylococcal Diseases 0.000 description 1
- 102000005918 Ubiquitin Thiolesterase Human genes 0.000 description 1
- 108010005656 Ubiquitin Thiolesterase Proteins 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 238000009098 adjuvant therapy Methods 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 102000006707 alpha-beta T-Cell Antigen Receptors Human genes 0.000 description 1
- 108010087408 alpha-beta T-Cell Antigen Receptors Proteins 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 239000003708 ampul Substances 0.000 description 1
- 230000003092 anti-cytokine Effects 0.000 description 1
- 230000001754 anti-pyretic effect Effects 0.000 description 1
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 239000002221 antipyretic Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000008365 aqueous carrier Substances 0.000 description 1
- 230000002917 arthritic effect Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 238000002619 cancer immunotherapy Methods 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 239000012876 carrier material Substances 0.000 description 1
- 230000022534 cell killing Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 230000005859 cell recognition Effects 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000012937 correction 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
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 210000001198 duodenum Anatomy 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 239000012997 ficoll-paque Substances 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 108010051307 glycyl-glycyl-proline Proteins 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 210000002443 helper t lymphocyte Anatomy 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 230000005934 immune activation Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 229940047122 interleukins Drugs 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 238000001361 intraarterial administration Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 230000001788 irregular Effects 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000011344 liquid material Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 201000005202 lung cancer Diseases 0.000 description 1
- 208000020816 lung neoplasm Diseases 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000002483 medication Methods 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- 230000000869 mutational effect Effects 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
- 210000000496 pancreas Anatomy 0.000 description 1
- 229960005489 paracetamol Drugs 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 239000011236 particulate material Substances 0.000 description 1
- 230000007030 peptide scission Effects 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 210000003800 pharynx Anatomy 0.000 description 1
- 102000054765 polymorphisms of proteins Human genes 0.000 description 1
- 210000004896 polypeptide structure Anatomy 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000009696 proliferative response Effects 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 102220228223 rs1064796013 Human genes 0.000 description 1
- 102200067541 rs281864846 Human genes 0.000 description 1
- 102220065891 rs57793737 Human genes 0.000 description 1
- 102200058377 rs61755804 Human genes 0.000 description 1
- 102220068439 rs781650198 Human genes 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 210000002356 skeleton Anatomy 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 229940054269 sodium pyruvate Drugs 0.000 description 1
- 239000011343 solid material Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 208000017756 staphylococcal toxic-shock syndrome Diseases 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 108010010318 streptococcal M protein Proteins 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000012134 supernatant fraction Substances 0.000 description 1
- 238000011477 surgical intervention Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 231100000057 systemic toxicity Toxicity 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 150000003568 thioethers Chemical class 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 150000003573 thiols Chemical class 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 229960005486 vaccine Drugs 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
- C07K16/3023—Lung
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
-
- 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
- A61P33/00—Antiparasitic agents
-
- 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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/305—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F)
- C07K14/31—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
- C07K16/3046—Stomach, Intestines
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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)
- Immunology (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Cell Biology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Epidemiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Communicable Diseases (AREA)
- Virology (AREA)
- Oncology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Peptides Or Proteins (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Catalysts (AREA)
- Addition Polymer Or Copolymer, Post-Treatments, Or Chemical Modifications (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE9601245A SE9601245D0 (sv) | 1996-03-29 | 1996-03-29 | Chimeric superantigens and their use |
| US08/695,692 US6514498B1 (en) | 1996-03-19 | 1996-08-12 | Modified/chimeric superantigens and their use |
| PCT/SE1997/000537 WO1997036932A1 (en) | 1996-03-29 | 1997-03-26 | Modified/chimeric superantigens and their use |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO975435D0 NO975435D0 (no) | 1997-11-26 |
| NO975435L NO975435L (no) | 1998-01-29 |
| NO321984B1 true NO321984B1 (no) | 2006-07-31 |
Family
ID=26662565
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO19975435A NO321984B1 (no) | 1996-03-29 | 1997-11-26 | Konjugat, fremstilling, samt anvendelse derav |
Country Status (20)
| Country | Link |
|---|---|
| US (1) | US7226595B2 (es) |
| EP (1) | EP0835266B1 (es) |
| JP (1) | JP4114951B2 (es) |
| AT (1) | ATE294818T1 (es) |
| AU (1) | AU707827B2 (es) |
| BR (1) | BR9702179A (es) |
| CA (1) | CA2222757C (es) |
| CZ (1) | CZ294475B6 (es) |
| DE (1) | DE69733179T2 (es) |
| ES (1) | ES2242222T3 (es) |
| HU (1) | HU228185B1 (es) |
| ID (1) | ID16512A (es) |
| IL (1) | IL122211A (es) |
| MX (1) | MX9709265A (es) |
| NO (1) | NO321984B1 (es) |
| NZ (1) | NZ329145A (es) |
| PL (1) | PL189696B1 (es) |
| PT (1) | PT835266E (es) |
| TW (1) | TW517061B (es) |
| WO (1) | WO1997036932A1 (es) |
Families Citing this family (50)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE9402430L (sv) * | 1994-07-11 | 1996-01-12 | Pharmacia Ab | Konjugat mellan modifierat superantigen och en målsökande förening samt användning av konjugaten |
| TW517061B (en) | 1996-03-29 | 2003-01-11 | Pharmacia & Amp Upjohn Ab | Modified/chimeric superantigens and their use |
| US7276488B2 (en) | 1997-06-04 | 2007-10-02 | Oxford Biomedica (Uk) Limited | Vector system |
| EP1012259B1 (en) | 1997-06-04 | 2009-09-30 | Oxford Biomedica (UK) Limited | Tumor targeted vector |
| US6713284B2 (en) | 1997-06-25 | 2004-03-30 | The United States Of America As Represented By The Secretary Of The Army | Bacterial superantigen vaccines |
| US7087235B2 (en) | 1997-06-25 | 2006-08-08 | The United States Of America As Represented By The Secretary Of The Army | Fusion protein of streptococcal pyrogenic exotoxins |
| EA002688B1 (ru) * | 1997-07-21 | 2002-08-29 | Фармациа Энд Апджон Аб | Способы инактивации клеток-мишеней, агенты и композиции, вызывающие цитолиз, и соединения, используемые для получения этих агентов |
| US6872394B1 (en) | 1997-12-02 | 2005-03-29 | Idaho Research Foundation, Inc. | Non-toxic immune stimulating enterotoxin compositions |
| WO1999027889A2 (en) * | 1997-12-02 | 1999-06-10 | Idaho Research Foundation, Inc. | Non-toxic immune stimulating enterotoxin compositions |
| AU762813B2 (en) * | 1998-08-13 | 2003-07-03 | Walter Reed Army Institute Of Research | Bacterial superantigen vaccines |
| US7491402B2 (en) * | 1998-12-24 | 2009-02-17 | Auckland Uniservices Limited | Superantigens SMEZ-2, SPE-G, SPE-H and SPE-J and uses thereof |
| EP1242456B1 (en) | 1999-11-18 | 2008-10-15 | Oxford Biomedica (UK) Limited | Scfv antibodies against disease associated molecules |
| US20030124142A1 (en) * | 2000-12-04 | 2003-07-03 | Fraser John David | Immunomodulatory constructs and their uses |
| SE0102327D0 (sv) * | 2001-06-28 | 2001-06-28 | Active Biotech Ab | A novel engineered superantigen for human therapy |
| WO2003095481A1 (en) * | 2002-05-09 | 2003-11-20 | Auckland Uniservices Limited | Streptococcal superantigens spe-l and spe-m |
| NZ519371A (en) * | 2002-06-04 | 2004-11-26 | Auckland Uniservices Ltd | Immunomodulatory constructs and their uses |
| US8025873B2 (en) | 2002-06-20 | 2011-09-27 | Paladin Labs, Inc. | Chimeric antigens for eliciting an immune response |
| US8029803B2 (en) | 2002-06-20 | 2011-10-04 | Paladin Labs, Inc. | Chimeric antigens for eliciting an immune response |
| GB0315450D0 (en) | 2003-07-01 | 2003-08-06 | Celltech R&D Ltd | Biological products |
| GB0315457D0 (en) * | 2003-07-01 | 2003-08-06 | Celltech R&D Ltd | Biological products |
| US8007805B2 (en) | 2003-08-08 | 2011-08-30 | Paladin Labs, Inc. | Chimeric antigens for breaking host tolerance to foreign antigens |
| SE0402025D0 (sv) * | 2004-08-13 | 2004-08-13 | Active Biotech Ab | Treatment of hyperproliferative disease with superantigens in combination with another anticancer agent |
| JP2008520227A (ja) * | 2004-11-18 | 2008-06-19 | メディジーン リミテッド | 可溶性二官能性タンパク質 |
| WO2006105168A2 (en) * | 2005-03-29 | 2006-10-05 | Regents Of The University Of Minnesota | Enhancing immune responses with bacterial exotoxins |
| US20070178113A1 (en) * | 2005-11-22 | 2007-08-02 | Backstrom B T | Superantigen conjugate |
| CA2755640C (en) * | 2009-03-20 | 2018-05-22 | Genentech, Inc. | Bispecific antibody with a single antigen-binding domain specific for both her3 and egfr |
| CA2807552A1 (en) | 2010-08-06 | 2012-02-09 | Moderna Therapeutics, Inc. | Engineered nucleic acids and methods of use thereof |
| EP3431485B1 (en) | 2010-10-01 | 2020-12-30 | ModernaTX, Inc. | Engineered nucleic acids and methods of use thereof |
| WO2012135805A2 (en) | 2011-03-31 | 2012-10-04 | modeRNA Therapeutics | Delivery and formulation of engineered nucleic acids |
| US9464124B2 (en) | 2011-09-12 | 2016-10-11 | Moderna Therapeutics, Inc. | Engineered nucleic acids and methods of use thereof |
| AU2012318752B2 (en) | 2011-10-03 | 2017-08-31 | Modernatx, Inc. | Modified nucleosides, nucleotides, and nucleic acids, and uses thereof |
| CN104114572A (zh) | 2011-12-16 | 2014-10-22 | 现代治疗公司 | 经修饰的核苷、核苷酸和核酸组合物 |
| US9572897B2 (en) | 2012-04-02 | 2017-02-21 | Modernatx, Inc. | Modified polynucleotides for the production of cytoplasmic and cytoskeletal proteins |
| EP2833923A4 (en) | 2012-04-02 | 2016-02-24 | Moderna Therapeutics Inc | MODIFIED POLYNUCLEOTIDES FOR THE PRODUCTION OF PROTEINS |
| US9283287B2 (en) | 2012-04-02 | 2016-03-15 | Moderna Therapeutics, Inc. | Modified polynucleotides for the production of nuclear proteins |
| US10501512B2 (en) | 2012-04-02 | 2019-12-10 | Modernatx, Inc. | Modified polynucleotides |
| US9597380B2 (en) | 2012-11-26 | 2017-03-21 | Modernatx, Inc. | Terminally modified RNA |
| US8980864B2 (en) | 2013-03-15 | 2015-03-17 | Moderna Therapeutics, Inc. | Compositions and methods of altering cholesterol levels |
| EP3010535B1 (en) * | 2013-06-19 | 2019-08-14 | Integrated Biotherapeutics, Inc. | Toxoid peptides derived from phenol soluble modulin, delta toxin, superantigens, and fusions thereof |
| BR112016004355A2 (pt) * | 2013-08-30 | 2017-10-17 | Aprilbio Co Ltd | constructo de fusão de parte efetora de fab anti-soroalbumina e método de preparação do mesmo |
| WO2015048744A2 (en) | 2013-09-30 | 2015-04-02 | Moderna Therapeutics, Inc. | Polynucleotides encoding immune modulating polypeptides |
| JP2016538829A (ja) | 2013-10-03 | 2016-12-15 | モデルナ セラピューティクス インコーポレイテッドＭｏｄｅｒｎａ Ｔｈｅｒａｐｅｕｔｉｃｓ，Ｉｎｃ． | 低密度リポタンパク質受容体をコードするポリヌクレオチド |
| WO2017122098A2 (en) | 2016-01-10 | 2017-07-20 | Neotx Therapeutics Ltd. | Methods and compositions for enhancing the potency of superantigen mediated cancer immunotherapy. |
| CN110996993B (zh) | 2017-07-27 | 2024-05-31 | Ab疫苗公司 | 包含源自超抗原类毒素的融合肽的免疫原性组合物 |
| JPWO2020162203A1 (es) * | 2019-02-08 | 2020-08-13 | ||
| EA202193121A1 (ru) | 2019-05-15 | 2022-02-21 | Неоткс Терапьютикс Лтд. | Лечение рака |
| KR20210095781A (ko) | 2020-01-24 | 2021-08-03 | 주식회사 에이프릴바이오 | 항원결합 단편 및 생리활성 이펙터 모이어티로 구성된 융합 컨스트럭트를 포함하는 다중결합항체 및 이를 포함하는 약학조성물 |
| AU2021357520A1 (en) | 2020-03-05 | 2022-09-29 | Neotx Therapeutics Ltd. | Methods and compositions for treating cancer with immune cells |
| WO2023215560A1 (en) | 2022-05-05 | 2023-11-09 | Atoosa Corporation | Tumor cell/immune cell multivalent receptor engager – bio-nanoparticle (timre-bnp) |
| WO2024077066A1 (en) * | 2022-10-05 | 2024-04-11 | Musc Foundation For Research Development | Superantigen vaccine conjugate for the treatment of cancer |
Family Cites Families (50)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3627644A (en) * | 1968-03-01 | 1971-12-14 | Hajime Okamoto | Process for the cultivation of hemolytic streptococci |
| US3903262A (en) * | 1972-03-13 | 1975-09-02 | Cutter Lab | Pharmaceutical compositions comprising intravenously injectable modified serum globulin, its production and use |
| US4237224A (en) * | 1974-11-04 | 1980-12-02 | Board Of Trustees Of The Leland Stanford Jr. University | Process for producing biologically functional molecular chimeras |
| GB1587244A (en) | 1977-07-01 | 1981-04-01 | Memm Spa | Streptococcal antigen pharmaceutical compositions containing it and its use in medical diagnosis and treatment |
| US4268434A (en) * | 1979-01-09 | 1981-05-19 | Higerd Thomas B | Immunosuppressive extracellular product from oral bacteria |
| US5091091A (en) * | 1981-11-06 | 1992-02-25 | Terman David S | Protein A perfusion and post perfusion drug infusion |
| US4699783A (en) * | 1983-03-11 | 1987-10-13 | Terman David S | Products and methods for treatment of cancer |
| US4681870A (en) * | 1985-01-11 | 1987-07-21 | Imre Corporation | Protein A-silica immunoadsorbent and process for its production |
| FR2589267B1 (fr) | 1985-10-25 | 1991-05-31 | Bertin & Cie | Procede de traitement d'images, notamment dans une installation de tri postal |
| US4980160A (en) | 1986-10-16 | 1990-12-25 | Biogen, Inc. | Combinations of tumor necrosis factors and anti-inflammatory agents and methods for treating malignant and non-malignant diseases |
| EP0336562B1 (en) | 1988-03-04 | 1995-06-14 | Cancer Research Campaign Technology Ltd. | Improvements relating to antigens |
| DE68907388T2 (de) | 1988-07-22 | 1994-01-05 | Imre Corp | Gereinigte Protein A-Zusammensetzungen und Verfahren zu ihrer Herstellung. |
| DE3921211C1 (es) | 1989-06-28 | 1990-11-29 | Idt Ag Fuer In Vivo Diagnostik Und Therapie, Zuerich, Ch | |
| US6042837A (en) * | 1989-09-20 | 2000-03-28 | Kalland; Terje | Methods of staphylococcal enterotoxin directed cell-mediated cytotoxicity (SDCC) |
| SE8903100D0 (sv) | 1989-09-20 | 1989-09-20 | Pharmacia Ab | New pharmaceutical agent |
| US6126945A (en) * | 1989-10-03 | 2000-10-03 | Pharmacia Ab | Tumor killing effects of enterotoxins, superantigens, and related compounds |
| US5728388A (en) * | 1989-10-03 | 1998-03-17 | Terman; David S. | Method of cancer treatment |
| DE69133485T2 (de) | 1990-01-17 | 2006-06-22 | Terman, David S., Pebble Beach | Verwendung von Staphylococcus Enterotoxin Homologe für Krebs-Therapie |
| SE465328B (sv) | 1990-02-19 | 1991-08-26 | Duotech Innovation Ab | Kompensationsventil |
| KR100189024B1 (ko) | 1990-07-20 | 1999-06-01 | 존 해던쉬트롬 | 항체 및 초항원을 포함하는 가용성 항체 결합체 및 그 제조방법 |
| US6197299B1 (en) * | 1990-07-20 | 2001-03-06 | Pharmacia & Upjohn Ab | Antibody conjugates |
| US5858363A (en) * | 1990-07-20 | 1999-01-12 | Pharmacia & Upjohn Ab | Target specific antibody-superantigen conjugates and their preparation |
| WO1993024136A1 (en) | 1991-01-17 | 1993-12-09 | Terman David S | Tumor killing effects of enterotoxins, superantigens, and related compounds |
| US6090914A (en) * | 1991-06-27 | 2000-07-18 | Bristol-Myers Squibb Company | CTLA4/CD28Ig hybrid fusion proteins and uses thereof |
| SE9102074D0 (sv) | 1991-07-03 | 1991-07-03 | Kabi Pharmacia Ab | Tomour antigen specific antibody |
| EP0626805A4 (en) | 1992-01-28 | 1995-12-06 | Nat Jewish Ct Immun & Respirat | Protective effects of mutated superantigens. |
| US5545716A (en) * | 1992-09-08 | 1996-08-13 | University Of Florida | Superantigen agonist and antagonist peptides |
| US5519114A (en) * | 1993-10-29 | 1996-05-21 | University Of Florida Research Foundation, Inc. | Retroviral superantigens, superantigen peptides, and methods of use |
| SE9402430L (sv) * | 1994-07-11 | 1996-01-12 | Pharmacia Ab | Konjugat mellan modifierat superantigen och en målsökande förening samt användning av konjugaten |
| US5541087A (en) * | 1994-09-14 | 1996-07-30 | Fuji Immunopharmaceuticals Corporation | Expression and export technology of proteins as immunofusins |
| AU723116B2 (en) * | 1995-06-07 | 2000-08-17 | Regents Of The University Of Minnesota | Mutants of streptococcal toxin A and methods of use |
| SE9601245D0 (sv) * | 1996-03-29 | 1996-03-29 | Pharmacia Ab | Chimeric superantigens and their use |
| TW517061B (en) | 1996-03-29 | 2003-01-11 | Pharmacia & Amp Upjohn Ab | Modified/chimeric superantigens and their use |
| WO1997036614A1 (en) * | 1996-03-29 | 1997-10-09 | Terman David S | Polymerized staphylococcal protein a for treatment of diseases |
| US6774218B2 (en) * | 1996-12-06 | 2004-08-10 | Regents Of The University Of Minnesota | Mutants of streptococcal toxin C and methods of use |
| EP0946730B1 (en) * | 1996-12-06 | 2006-03-08 | Regents Of The University Of Minnesota | Mutants of streptococcal toxin c and methods of use |
| WO1998024911A2 (en) * | 1996-12-06 | 1998-06-11 | Regents Of The University Of Minnesota | Mutants of streptococcal toxin a and methods of use |
| WO1998026747A2 (en) * | 1996-12-17 | 1998-06-25 | Terman David S | Superantigen based methods and compositions for treatment of diseases |
| IL119938A (en) * | 1996-12-30 | 2005-08-31 | Yissum Res Dev Co | Peptides capable of eliciting protective immunity against toxic shock induced by pyrogenic exotoxins or of antagonizing toxin-mediated activation of t cells |
| US6713284B2 (en) * | 1997-06-25 | 2004-03-30 | The United States Of America As Represented By The Secretary Of The Army | Bacterial superantigen vaccines |
| US7087235B2 (en) * | 1997-06-25 | 2006-08-08 | The United States Of America As Represented By The Secretary Of The Army | Fusion protein of streptococcal pyrogenic exotoxins |
| WO1999036433A2 (en) * | 1998-01-14 | 1999-07-22 | Morphogenesis, Inc. | Materials and methods for treating oncological disease |
| EP1097212B1 (en) * | 1998-07-10 | 2008-12-24 | U.S. Medical Research Institute of Infectious Diseases | Anthrax vaccine |
| US20020177551A1 (en) * | 2000-05-31 | 2002-11-28 | Terman David S. | Compositions and methods for treatment of neoplastic disease |
| US20030157113A1 (en) * | 1999-12-28 | 2003-08-21 | Terman David S. | Compositions and methods for treatment of neoplastic disease |
| US20010046501A1 (en) * | 2000-03-14 | 2001-11-29 | Johnson Howard M. | Superantigen enhancement of specific immune responses |
| JP4283430B2 (ja) * | 2000-09-26 | 2009-06-24 | 株式会社カネカ | エンテロトキシンの吸着材、吸着除去方法および吸着器 |
| US20030124142A1 (en) * | 2000-12-04 | 2003-07-03 | Fraser John David | Immunomodulatory constructs and their uses |
| CN1369550A (zh) * | 2001-02-16 | 2002-09-18 | 沈阳协合集团有限公司 | 一种金黄色葡萄球菌的培养物及其制备方法 |
| SE0102327D0 (sv) * | 2001-06-28 | 2001-06-28 | Active Biotech Ab | A novel engineered superantigen for human therapy |
-
1997
- 1997-03-24 TW TW086103689A patent/TW517061B/zh not_active IP Right Cessation
- 1997-03-26 PT PT97916693T patent/PT835266E/pt unknown
- 1997-03-26 EP EP97916693A patent/EP0835266B1/en not_active Expired - Lifetime
- 1997-03-26 DE DE69733179T patent/DE69733179T2/de not_active Expired - Lifetime
- 1997-03-26 AU AU25251/97A patent/AU707827B2/en not_active Ceased
- 1997-03-26 PL PL97323626A patent/PL189696B1/pl not_active IP Right Cessation
- 1997-03-26 BR BR9702179A patent/BR9702179A/pt not_active Application Discontinuation
- 1997-03-26 IL IL122211A patent/IL122211A/en not_active IP Right Cessation
- 1997-03-26 ES ES97916693T patent/ES2242222T3/es not_active Expired - Lifetime
- 1997-03-26 CA CA2222757A patent/CA2222757C/en not_active Expired - Fee Related
- 1997-03-26 HU HU9903444A patent/HU228185B1/hu not_active IP Right Cessation
- 1997-03-26 CZ CZ19973712A patent/CZ294475B6/cs unknown
- 1997-03-26 MX MX9709265A patent/MX9709265A/es not_active IP Right Cessation
- 1997-03-26 JP JP53519897A patent/JP4114951B2/ja not_active Expired - Fee Related
- 1997-03-26 WO PCT/SE1997/000537 patent/WO1997036932A1/en active IP Right Grant
- 1997-03-26 NZ NZ329145A patent/NZ329145A/en not_active IP Right Cessation
- 1997-03-26 AT AT97916693T patent/ATE294818T1/de active
- 1997-03-27 ID IDP971022A patent/ID16512A/id unknown
- 1997-11-26 NO NO19975435A patent/NO321984B1/no not_active IP Right Cessation
-
2002
- 2002-10-30 US US10/283,838 patent/US7226595B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| JP2002502363A (ja) | 2002-01-22 |
| CZ294475B6 (cs) | 2005-01-12 |
| DE69733179T2 (de) | 2005-10-06 |
| WO1997036932A1 (en) | 1997-10-09 |
| CZ371297A3 (cs) | 1998-05-13 |
| ES2242222T3 (es) | 2005-11-01 |
| HUP9903444A3 (en) | 2003-08-28 |
| TW517061B (en) | 2003-01-11 |
| ATE294818T1 (de) | 2005-05-15 |
| HU228185B1 (en) | 2013-01-28 |
| IL122211A0 (en) | 1998-04-05 |
| BR9702179A (pt) | 1999-03-16 |
| EP0835266A1 (en) | 1998-04-15 |
| PT835266E (pt) | 2005-07-29 |
| DE69733179D1 (de) | 2005-06-09 |
| ID16512A (id) | 1997-10-02 |
| HUP9903444A2 (hu) | 2000-02-28 |
| NZ329145A (en) | 2000-06-23 |
| MX9709265A (es) | 1998-03-31 |
| CA2222757A1 (en) | 1997-10-09 |
| CA2222757C (en) | 2011-07-26 |
| PL189696B1 (pl) | 2005-09-30 |
| AU2525197A (en) | 1997-10-22 |
| NO975435L (no) | 1998-01-29 |
| US20030092894A1 (en) | 2003-05-15 |
| EP0835266B1 (en) | 2005-05-04 |
| US7226595B2 (en) | 2007-06-05 |
| PL323626A1 (en) | 1998-04-14 |
| JP4114951B2 (ja) | 2008-07-09 |
| IL122211A (en) | 2009-07-20 |
| AU707827B2 (en) | 1999-07-22 |
| NO975435D0 (no) | 1997-11-26 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| NO321984B1 (no) | Konjugat, fremstilling, samt anvendelse derav | |
| US6514498B1 (en) | Modified/chimeric superantigens and their use | |
| CN112300269B (zh) | Kras突变特异性t细胞受体筛选及抗肿瘤用途 | |
| EP3505535A1 (en) | Anti-pd1 monoclonal antibody, pharmaceutical composition thereof and use thereof | |
| US7074909B2 (en) | Antibodies | |
| JP2019107018A (ja) | 抗ｃｔｌａ４モノクローナル抗体またはその抗原結合断片、医薬組成物および使用 | |
| AU2013271428B2 (en) | Human bispecific EGFRvIII antibody engaging molecules | |
| NO320151B1 (no) | Konjugat mellom en biospesifikk affinitetsmotpart og et peptid avledet fra et superantigen som er kovalent bundet til hverandre | |
| US20180362659A1 (en) | Certain Improved Human Bispecific EGFRvIII Antibody Engaging Molecules | |
| Antonsson et al. | Functional characterization of the interaction between the superantigen staphylococcal enterotoxin A and the TCR. | |
| US20070161080A1 (en) | Antibodies | |
| EP3999106A1 (en) | Self-assembled vaccines and combination therapies for treating cancer | |
| CN115304680A (zh) | 基于Pep42构建的双特异性细胞接合器分子的制备及其应用 | |
| WO2024051223A1 (zh) | 药物组合及用途 | |
| CN113005088B (zh) | 工程改造的t细胞、其制备及应用 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM1K | Lapsed by not paying the annual fees |