ES2874077T3 - Métodos y compuestos mejorados para eliminar respuestas inmunitarias a agentes terapéuticos - Google Patents
Métodos y compuestos mejorados para eliminar respuestas inmunitarias a agentes terapéuticos Download PDFInfo
- Publication number
- ES2874077T3 ES2874077T3 ES16778714T ES16778714T ES2874077T3 ES 2874077 T3 ES2874077 T3 ES 2874077T3 ES 16778714 T ES16778714 T ES 16778714T ES 16778714 T ES16778714 T ES 16778714T ES 2874077 T3 ES2874077 T3 ES 2874077T3
- Authority
- ES
- Spain
- Prior art keywords
- epitope
- sequence
- protein
- seq
- peptide
- 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.)
- Active
Links
- 230000028993 immune response Effects 0.000 title claims abstract description 32
- 239000003814 drug Substances 0.000 title claims description 25
- 238000000034 method Methods 0.000 title claims description 23
- 229940124597 therapeutic agent Drugs 0.000 title description 18
- 150000001875 compounds Chemical class 0.000 title description 7
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 203
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 186
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 181
- 210000001744 T-lymphocyte Anatomy 0.000 claims abstract description 161
- 150000001413 amino acids Chemical class 0.000 claims abstract description 100
- 230000001225 therapeutic effect Effects 0.000 claims abstract description 76
- 102000043131 MHC class II family Human genes 0.000 claims abstract description 70
- 108091054438 MHC class II family Proteins 0.000 claims abstract description 70
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 58
- 239000013603 viral vector Substances 0.000 claims abstract description 51
- 108090000854 Oxidoreductases Proteins 0.000 claims abstract description 31
- 102000004316 Oxidoreductases Human genes 0.000 claims abstract description 31
- 229920001184 polypeptide Polymers 0.000 claims abstract description 23
- 239000013604 expression vector Substances 0.000 claims abstract description 20
- 230000004927 fusion Effects 0.000 claims abstract description 16
- 102000040430 polynucleotide Human genes 0.000 claims abstract description 13
- 108091033319 polynucleotide Proteins 0.000 claims abstract description 13
- 239000002157 polynucleotide Substances 0.000 claims abstract description 13
- 108020001507 fusion proteins Proteins 0.000 claims description 21
- 102000037865 fusion proteins Human genes 0.000 claims description 21
- 239000013598 vector Substances 0.000 claims description 19
- 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 description 7
- 108010093013 HLA-DR1 Antigen Proteins 0.000 claims description 6
- 241000700605 Viruses Species 0.000 claims description 4
- 230000003612 virological effect Effects 0.000 claims description 3
- 230000012743 protein tagging Effects 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 162
- 229940024606 amino acid Drugs 0.000 description 87
- 235000001014 amino acid Nutrition 0.000 description 86
- 239000000427 antigen Substances 0.000 description 33
- 108091007433 antigens Proteins 0.000 description 33
- 102000036639 antigens Human genes 0.000 description 33
- 210000004027 cell Anatomy 0.000 description 33
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 31
- 102400001295 Class-II-associated invariant chain peptide Human genes 0.000 description 27
- 101800001887 Class-II-associated invariant chain peptide Proteins 0.000 description 27
- 238000002255 vaccination Methods 0.000 description 26
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 20
- 102000003951 Erythropoietin Human genes 0.000 description 18
- 108090000394 Erythropoietin Proteins 0.000 description 18
- 229940105423 erythropoietin Drugs 0.000 description 18
- 230000001461 cytolytic effect Effects 0.000 description 14
- 238000001415 gene therapy Methods 0.000 description 13
- 241000282414 Homo sapiens Species 0.000 description 11
- 230000000890 antigenic effect Effects 0.000 description 11
- 230000001603 reducing effect Effects 0.000 description 11
- 230000014509 gene expression Effects 0.000 description 9
- 108700028369 Alleles Proteins 0.000 description 8
- 108020004414 DNA Proteins 0.000 description 8
- 102000005840 alpha-Galactosidase Human genes 0.000 description 8
- 108010030291 alpha-Galactosidase Proteins 0.000 description 8
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 8
- 230000004048 modification Effects 0.000 description 8
- 238000012986 modification Methods 0.000 description 8
- 238000010647 peptide synthesis reaction Methods 0.000 description 8
- 125000003275 alpha amino acid group Chemical group 0.000 description 7
- 210000000612 antigen-presenting cell Anatomy 0.000 description 6
- 239000003795 chemical substances by application Substances 0.000 description 6
- 239000012634 fragment Substances 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- 238000003780 insertion Methods 0.000 description 6
- 230000037431 insertion Effects 0.000 description 6
- 102000039446 nucleic acids Human genes 0.000 description 6
- 108020004707 nucleic acids Proteins 0.000 description 6
- 150000007523 nucleic acids Chemical class 0.000 description 6
- 235000018417 cysteine Nutrition 0.000 description 5
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 238000002649 immunization Methods 0.000 description 5
- 230000003053 immunization Effects 0.000 description 5
- 238000002347 injection Methods 0.000 description 5
- 239000007924 injection Substances 0.000 description 5
- 108020003175 receptors Proteins 0.000 description 5
- 102000005962 receptors Human genes 0.000 description 5
- 238000009256 replacement therapy Methods 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 238000003786 synthesis reaction Methods 0.000 description 5
- 238000002560 therapeutic procedure Methods 0.000 description 5
- 238000011282 treatment Methods 0.000 description 5
- 229960005486 vaccine Drugs 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 208000024720 Fabry Disease Diseases 0.000 description 4
- 102000004877 Insulin Human genes 0.000 description 4
- 108090001061 Insulin Proteins 0.000 description 4
- 125000000539 amino acid group Chemical group 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 229940125396 insulin Drugs 0.000 description 4
- 238000012423 maintenance Methods 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 150000002894 organic compounds Chemical class 0.000 description 4
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 3
- 239000004475 Arginine Substances 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 3
- 108010054218 Factor VIII Proteins 0.000 description 3
- 102000001690 Factor VIII Human genes 0.000 description 3
- 102100040485 HLA class II histocompatibility antigen, DRB1 beta chain Human genes 0.000 description 3
- 108010039343 HLA-DRB1 Chains Proteins 0.000 description 3
- 108010027412 Histocompatibility Antigens Class II Proteins 0.000 description 3
- 102000018713 Histocompatibility Antigens Class II Human genes 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 3
- 102000007079 Peptide Fragments Human genes 0.000 description 3
- 108010033276 Peptide Fragments Proteins 0.000 description 3
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 3
- 230000006907 apoptotic process Effects 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 3
- 230000006329 citrullination Effects 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 150000001945 cysteines Chemical class 0.000 description 3
- 231100000433 cytotoxic Toxicity 0.000 description 3
- 230000001472 cytotoxic effect Effects 0.000 description 3
- 210000004443 dendritic cell Anatomy 0.000 description 3
- 229960000301 factor viii Drugs 0.000 description 3
- 125000003630 glycyl group Chemical class [H]N([H])C([H])([H])C(*)=O 0.000 description 3
- 125000001165 hydrophobic group Chemical group 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 230000001965 increasing effect Effects 0.000 description 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 3
- 238000009163 protein therapy Methods 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- 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 2
- KDRNOBUWMVLVFH-UHFFFAOYSA-N 2-methyl-n-(2,2,6,6-tetramethylpiperidin-4-yl)prop-2-enamide Chemical compound CC(=C)C(=O)NC1CC(C)(C)NC(C)(C)C1 KDRNOBUWMVLVFH-UHFFFAOYSA-N 0.000 description 2
- BYXHQQCXAJARLQ-ZLUOBGJFSA-N Ala-Ala-Ala Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(O)=O BYXHQQCXAJARLQ-ZLUOBGJFSA-N 0.000 description 2
- 102100022641 Coagulation factor IX Human genes 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 150000008574 D-amino acids Chemical class 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- 108010076282 Factor IX Proteins 0.000 description 2
- 108010058597 HLA-DR Antigens Proteins 0.000 description 2
- 102000006354 HLA-DR Antigens Human genes 0.000 description 2
- 208000009292 Hemophilia A Diseases 0.000 description 2
- 241000711549 Hepacivirus C Species 0.000 description 2
- 101000740112 Homo sapiens Membrane-associated transporter protein Proteins 0.000 description 2
- 206010021143 Hypoxia Diseases 0.000 description 2
- 102100033448 Lysosomal alpha-glucosidase Human genes 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 102100037258 Membrane-associated transporter protein Human genes 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 208000015914 Non-Hodgkin lymphomas Diseases 0.000 description 2
- 102000006010 Protein Disulfide-Isomerase Human genes 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 208000001647 Renal Insufficiency Diseases 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 2
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 2
- 108700019146 Transgenes Proteins 0.000 description 2
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 2
- 108010067390 Viral Proteins Proteins 0.000 description 2
- 230000021736 acetylation Effects 0.000 description 2
- 238000006640 acetylation reaction Methods 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 230000000961 alloantigen Effects 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 238000007385 chemical modification Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 108010057085 cytokine receptors Proteins 0.000 description 2
- 102000003675 cytokine receptors Human genes 0.000 description 2
- 230000007812 deficiency Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 230000010437 erythropoiesis Effects 0.000 description 2
- 229960004222 factor ix Drugs 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 230000007954 hypoxia Effects 0.000 description 2
- 238000002650 immunosuppressive therapy Methods 0.000 description 2
- 238000000126 in silico method Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 108010028930 invariant chain Proteins 0.000 description 2
- 201000006370 kidney failure Diseases 0.000 description 2
- -1 linker compound Chemical class 0.000 description 2
- 230000010534 mechanism of action Effects 0.000 description 2
- 102000035118 modified proteins Human genes 0.000 description 2
- 108091005573 modified proteins Proteins 0.000 description 2
- 230000003472 neutralizing effect Effects 0.000 description 2
- 210000005259 peripheral blood Anatomy 0.000 description 2
- 239000011886 peripheral blood Substances 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 125000006239 protecting group Chemical group 0.000 description 2
- 108020003519 protein disulfide isomerase Proteins 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 206010039073 rheumatoid arthritis Diseases 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 230000019635 sulfation Effects 0.000 description 2
- 238000005670 sulfation reaction Methods 0.000 description 2
- 125000005931 tert-butyloxycarbonyl group Chemical group [H]C([H])([H])C(OC(*)=O)(C([H])([H])[H])C([H])([H])[H] 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- 150000003573 thiols Chemical class 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 229960000187 tissue plasminogen activator Drugs 0.000 description 2
- 208000035408 type 1 diabetes mellitus 1 Diseases 0.000 description 2
- 210000004340 zona pellucida Anatomy 0.000 description 2
- DVQCNGKZAMNXCR-BYPYZUCNSA-N (2s)-3-methyl-2-(sulfanylamino)butanoic acid Chemical compound CC(C)[C@H](NS)C(O)=O DVQCNGKZAMNXCR-BYPYZUCNSA-N 0.000 description 1
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- SLXKOJJOQWFEFD-UHFFFAOYSA-N 6-aminohexanoic acid Chemical compound NCCCCCC(O)=O SLXKOJJOQWFEFD-UHFFFAOYSA-N 0.000 description 1
- 102000006991 Apolipoprotein B-100 Human genes 0.000 description 1
- 108010008150 Apolipoprotein B-100 Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 102100022005 B-lymphocyte antigen CD20 Human genes 0.000 description 1
- 102100027314 Beta-2-microglobulin Human genes 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 108010041397 CD4 Antigens Proteins 0.000 description 1
- 102100023804 Coagulation factor VII Human genes 0.000 description 1
- 102100026735 Coagulation factor VIII Human genes 0.000 description 1
- 206010053567 Coagulopathies Diseases 0.000 description 1
- 208000015943 Coeliac disease Diseases 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 241000701022 Cytomegalovirus Species 0.000 description 1
- QNAYBMKLOCPYGJ-UWTATZPHSA-N D-alanine Chemical compound C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 238000011238 DNA vaccination Methods 0.000 description 1
- 241000450599 DNA viruses Species 0.000 description 1
- 241000702421 Dependoparvovirus Species 0.000 description 1
- 101710106383 Disulfide bond formation protein B Proteins 0.000 description 1
- 206010013883 Dwarfism Diseases 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000620209 Escherichia coli DH5[alpha] Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 108010023321 Factor VII Proteins 0.000 description 1
- 201000003542 Factor VIII deficiency Diseases 0.000 description 1
- 108010014173 Factor X Proteins 0.000 description 1
- 241001663880 Gammaretrovirus Species 0.000 description 1
- 208000015872 Gaucher disease Diseases 0.000 description 1
- 208000020322 Gaucher disease type I Diseases 0.000 description 1
- 208000032007 Glycogen storage disease due to acid maltase deficiency Diseases 0.000 description 1
- 206010053185 Glycogen storage disease type II Diseases 0.000 description 1
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 description 1
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 102000018997 Growth Hormone Human genes 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 108091006013 HA-tagged proteins Proteins 0.000 description 1
- 102100029966 HLA class II histocompatibility antigen, DP alpha 1 chain Human genes 0.000 description 1
- 102100040505 HLA class II histocompatibility antigen, DR alpha chain Human genes 0.000 description 1
- 108010067802 HLA-DR alpha-Chains Proteins 0.000 description 1
- 108700037339 HLA-DR13 antigen Proteins 0.000 description 1
- 108010063970 HLA-DR15 antigen Proteins 0.000 description 1
- 108010064885 HLA-DR3 Antigen Proteins 0.000 description 1
- 108010001041 HLA-DR7 Antigen Proteins 0.000 description 1
- 108010086066 HLA-DR8 antigen Proteins 0.000 description 1
- 102210049236 HLA-DRB1*03:01 Human genes 0.000 description 1
- 108010047214 HLA-DRB1*03:01 antigen Proteins 0.000 description 1
- 108010029657 HLA-DRB1*04:01 antigen Proteins 0.000 description 1
- 102210029654 HLA-DRB1*07:01 Human genes 0.000 description 1
- 102210026614 HLA-DRB1*13:01 Human genes 0.000 description 1
- 206010019280 Heart failures Diseases 0.000 description 1
- 208000031220 Hemophilia Diseases 0.000 description 1
- 208000005176 Hepatitis C Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 108091006054 His-tagged proteins Proteins 0.000 description 1
- 102000008949 Histocompatibility Antigens Class I Human genes 0.000 description 1
- 101000897405 Homo sapiens B-lymphocyte antigen CD20 Proteins 0.000 description 1
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 description 1
- 101000987586 Homo sapiens Eosinophil peroxidase Proteins 0.000 description 1
- 101000864089 Homo sapiens HLA class II histocompatibility antigen, DP alpha 1 chain Proteins 0.000 description 1
- 101000930802 Homo sapiens HLA class II histocompatibility antigen, DQ alpha 1 chain Proteins 0.000 description 1
- 101000968032 Homo sapiens HLA class II histocompatibility antigen, DR beta 3 chain Proteins 0.000 description 1
- 101000610605 Homo sapiens Tumor necrosis factor receptor superfamily member 10A Proteins 0.000 description 1
- 102000004157 Hydrolases Human genes 0.000 description 1
- 108090000604 Hydrolases Proteins 0.000 description 1
- 206010061216 Infarction Diseases 0.000 description 1
- 102000006992 Interferon-alpha Human genes 0.000 description 1
- 108010047761 Interferon-alpha Proteins 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102000010781 Interleukin-6 Receptors Human genes 0.000 description 1
- 108010038501 Interleukin-6 Receptors Proteins 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- RHGKLRLOHDJJDR-BYPYZUCNSA-N L-citrulline Chemical group NC(=O)NCCC[C@H]([NH3+])C([O-])=O RHGKLRLOHDJJDR-BYPYZUCNSA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- FFFHZYDWPBMWHY-VKHMYHEASA-N L-homocysteine Chemical compound OC(=O)[C@@H](N)CCS FFFHZYDWPBMWHY-VKHMYHEASA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 241000713666 Lentivirus Species 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 208000015439 Lysosomal storage disease Diseases 0.000 description 1
- 108091054437 MHC class I family Proteins 0.000 description 1
- 201000005505 Measles Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 108091061960 Naked DNA Proteins 0.000 description 1
- RHGKLRLOHDJJDR-UHFFFAOYSA-N Ndelta-carbamoyl-DL-ornithine Natural products OC(=O)C(N)CCCNC(N)=O RHGKLRLOHDJJDR-UHFFFAOYSA-N 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 101710116318 Probable disulfide formation protein Proteins 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 101710145796 Staphylokinase Proteins 0.000 description 1
- 108010055044 Tetanus Toxin Proteins 0.000 description 1
- 108060008225 Thiolase Proteins 0.000 description 1
- 102000002933 Thioredoxin Human genes 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 102000014384 Type C Phospholipases Human genes 0.000 description 1
- 108010079194 Type C Phospholipases Proteins 0.000 description 1
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 1
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 1
- 210000001766 X chromosome Anatomy 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 229960000548 alemtuzumab Drugs 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- 108010028144 alpha-Glucosidases Proteins 0.000 description 1
- 229960002684 aminocaproic acid 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
- 229960000723 ampicillin Drugs 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000004873 anchoring Methods 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
- 230000003092 anti-cytokine Effects 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000000599 auto-anti-genic effect Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 108010081355 beta 2-Microglobulin Proteins 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 210000000234 capsid Anatomy 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000000747 cardiac effect Effects 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000000423 cell based assay Methods 0.000 description 1
- 230000011712 cell development Effects 0.000 description 1
- 230000005859 cell recognition Effects 0.000 description 1
- 238000002659 cell therapy Methods 0.000 description 1
- 229940106189 ceramide Drugs 0.000 description 1
- 150000001783 ceramides Chemical class 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 210000000038 chest Anatomy 0.000 description 1
- 229960002173 citrulline Drugs 0.000 description 1
- 235000013477 citrulline Nutrition 0.000 description 1
- 230000009852 coagulant defect Effects 0.000 description 1
- 238000002648 combination therapy Methods 0.000 description 1
- 239000003433 contraceptive agent Substances 0.000 description 1
- 230000002254 contraceptive 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
- 238000011461 current therapy Methods 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000006240 deamidation Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 241001493065 dsRNA viruses Species 0.000 description 1
- 230000005014 ectopic expression Effects 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 238000002641 enzyme replacement therapy Methods 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 210000003013 erythroid precursor cell Anatomy 0.000 description 1
- 229940012413 factor vii Drugs 0.000 description 1
- 229940012426 factor x Drugs 0.000 description 1
- 239000003527 fibrinolytic agent Substances 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 230000009395 genetic defect Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 102000054766 genetic haplotypes Human genes 0.000 description 1
- 210000004602 germ cell Anatomy 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 235000004554 glutamine Nutrition 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 201000004502 glycogen storage disease II Diseases 0.000 description 1
- 150000002339 glycosphingolipids Chemical class 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 210000002443 helper t lymphocyte Anatomy 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 235000014304 histidine Nutrition 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 102000044890 human EPO Human genes 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000006702 hypoxic induction Effects 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 238000012606 in vitro cell culture Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000007574 infarction Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 230000002132 lysosomal effect Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 108010087904 neutravidin Proteins 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000000813 peptide hormone Substances 0.000 description 1
- 210000004976 peripheral blood cell Anatomy 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 229940127557 pharmaceutical product Drugs 0.000 description 1
- 230000003285 pharmacodynamic effect Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 150000003906 phosphoinositides Chemical class 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 108060006632 protein arginine deiminase Proteins 0.000 description 1
- 102000001235 protein arginine deiminase Human genes 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 238000007921 solubility assay Methods 0.000 description 1
- 210000001082 somatic cell Anatomy 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 210000000225 synapse Anatomy 0.000 description 1
- 125000000999 tert-butyl group Chemical group [H]C([H])([H])C(*)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- 229960000814 tetanus toxoid Drugs 0.000 description 1
- 108060008226 thioredoxin Proteins 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 230000008733 trauma Effects 0.000 description 1
- 125000002221 trityl group Chemical group [H]C1=C([H])C([H])=C([H])C([H])=C1C([*])(C1=C(C(=C(C(=C1[H])[H])[H])[H])[H])C1=C([H])C([H])=C([H])C([H])=C1[H] 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 210000005253 yeast cell 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
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70503—Immunoglobulin superfamily
- C07K14/70539—MHC-molecules, e.g. HLA-molecules
-
- 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
- A61K39/0005—Vertebrate antigens
- A61K39/001—Preparations to induce tolerance to non-self, e.g. prior to transplantation
-
- 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
- A61K39/39—Medicinal preparations containing antigens or antibodies characterised by the immunostimulating additives, e.g. chemical adjuvants
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
- A61K35/12—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells
- A61K2035/122—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells for inducing tolerance or supression of immune responses
-
- 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
- A61K2039/55505—Inorganic adjuvants
-
- 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
- A61K2039/55516—Proteins; Peptides
-
- 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
- A61K2039/57—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2
- A61K2039/572—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2 cytotoxic response
-
- 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
- A61K2039/62—Medicinal preparations containing antigens or antibodies characterised by the link between antigen and carrier
- A61K2039/627—Medicinal preparations containing antigens or antibodies characterised by the link between antigen and carrier characterised by the linker
-
- 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
- A61K2039/70—Multivalent vaccine
-
- 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
- C07K2319/00—Fusion polypeptide
- C07K2319/40—Fusion polypeptide containing a tag for immunodetection, or an epitope for immunisation
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Immunology (AREA)
- Microbiology (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Molecular Biology (AREA)
- Epidemiology (AREA)
- Mycology (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Transplantation (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cell Biology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP15186845 | 2015-09-25 | ||
| PCT/EP2016/072690 WO2017050966A1 (en) | 2015-09-25 | 2016-09-23 | Improved methods and compounds for eliminating immune responses to therapeutic agents |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2874077T3 true ES2874077T3 (es) | 2021-11-04 |
Family
ID=54251983
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES16778714T Active ES2874077T3 (es) | 2015-09-25 | 2016-09-23 | Métodos y compuestos mejorados para eliminar respuestas inmunitarias a agentes terapéuticos |
Country Status (8)
| Country | Link |
|---|---|
| US (2) | US11787849B2 (enExample) |
| EP (2) | EP3352782B1 (enExample) |
| JP (1) | JP7090335B2 (enExample) |
| CN (1) | CN108289941B (enExample) |
| AU (2) | AU2016328582B2 (enExample) |
| CA (1) | CA2995771A1 (enExample) |
| ES (1) | ES2874077T3 (enExample) |
| WO (1) | WO2017050966A1 (enExample) |
Families Citing this family (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| PT2476435T (pt) | 2006-08-11 | 2018-03-05 | Life Sciences Res Partners Vzw | Péptidos imunogénicos e a sua utilização em distúrbios imunitários |
| US8999346B2 (en) | 2008-02-14 | 2015-04-07 | Life Sciences Research Partners Vzw | Immunogenic control of tumours and tumour cells |
| CA2715611C (en) | 2008-02-14 | 2018-03-13 | Life Sciences Research Partners Vzw | Immunotherapy targeting intracellular pathogens |
| RU2615460C2 (ru) | 2010-11-25 | 2017-04-04 | Имнейт Сарл | Иммуногенные пептиды для применения в профилактике и/или лечении инфекционных заболеваний, аутоиммунных заболеваний, иммунных ответов на аллогенные факторы, аллергических заболеваний, опухолей, отторжения трансплантата и иммунных ответов против вирусных векторов. используемых для генной терапии или генной вакцинации |
| GB201201511D0 (en) | 2012-01-30 | 2012-03-14 | Univ Leuven Kath | Modified epitopes for boosting CD4+ T-cell responses |
| GB201309469D0 (en) | 2013-05-28 | 2013-07-10 | Imcyse Sa | Detection of CD4+ T lymphocytes |
| GB201418433D0 (en) | 2014-10-17 | 2014-12-03 | Imcyse Sa | Novel immunogenic peptides |
| US10729791B2 (en) | 2015-05-18 | 2020-08-04 | Imcyse Sa | Animal models for evaluating pharmaceutical compounds |
| EP3352782B1 (en) | 2015-09-25 | 2021-03-31 | ImCyse SA | Improved methods and compounds for eliminating immune responses to therapeutic agents |
| KR20240015731A (ko) | 2016-04-19 | 2024-02-05 | 임시스 에스에이 | 신규 면역원성 CD1d 결합 펩티드 |
| WO2020229703A1 (en) * | 2019-05-16 | 2020-11-19 | Imcyse Sa | Immunogenic peptides with an oxidoreductase motif comprising a modified cysteine |
| WO2021224403A1 (en) * | 2020-05-06 | 2021-11-11 | Imcyse Sa | Immunogenic peptides with new oxidoreductase motifs |
| CU20220066A7 (es) * | 2020-05-06 | 2023-06-13 | Imcyse Sa | Péptidos inmunogénicos útiles en el tratamiento de esclerosis múltiple |
| JP2023525276A (ja) * | 2020-05-06 | 2023-06-15 | アンシス・エスア | 延長された酸化還元酵素モチーフを有する免疫原性ペプチド |
| CN113621030B (zh) * | 2020-07-14 | 2023-05-26 | 上海科技大学 | 一种诱导蛋白质降解的多肽及其应用 |
Family Cites Families (61)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4599231A (en) | 1984-03-09 | 1986-07-08 | Scripps Clinic And Research Foundation | Synthetic hepatitis B virus vaccine including both T cell and B cell determinants |
| WO1985004103A1 (en) | 1984-03-09 | 1985-09-26 | Scripps Clinic And Research Foundation | Synthetic hepatitis b virus vaccine including both t cell anc b cell determinants |
| US4886782A (en) | 1987-02-26 | 1989-12-12 | The United States Of America As Represented By The Department Of Health And Human Services | Malarial immunogen |
| US5433948A (en) | 1990-02-13 | 1995-07-18 | Thomas; Wayne R. | Cloning and sequencing of allergens of dermatophagoides (house dust mite) |
| EP0550599B1 (en) | 1990-09-27 | 2003-04-23 | Tripep AB | Peptides for use in vaccination and induction of neutralizing antibodies against human immunodeficiency virus |
| EP0623168B1 (en) | 1991-10-16 | 2009-09-30 | Merck Patent GmbH | T cell epitopes of the major allergens from dermatophagoides (house dust mite) |
| US7252829B1 (en) | 1998-06-17 | 2007-08-07 | Idm Pharma, Inc. | HLA binding peptides and their uses |
| US5589582A (en) | 1992-10-27 | 1996-12-31 | Biotransplant, Inc. | Polynucleotides en coding porcine cytokines |
| US5633234A (en) | 1993-01-22 | 1997-05-27 | The Johns Hopkins University | Lysosomal targeting of immunogens |
| US5824315A (en) | 1993-10-25 | 1998-10-20 | Anergen, Inc. | Binding affinity of antigenic peptides for MHC molecules |
| US8791237B2 (en) | 1994-11-08 | 2014-07-29 | The Trustees Of The University Of Pennsylvania | Compositions and methods for treatment of non-hodgkins lymphoma |
| US7157089B1 (en) | 1996-11-26 | 2007-01-02 | Stressgen Biotechnologies Corporation | Immune responses using compositions containing stress proteins |
| AU1124499A (en) | 1997-10-28 | 1999-05-17 | Maxygen, Inc. | Human papillomavirus vectors |
| NO315238B1 (no) | 1998-05-08 | 2003-08-04 | Gemvax As | Peptider som stammer fra leserammeforskyvingsmutasjoner i TBF<beta>II- eller BAX-genet, og farmasöytiske sammensetninger inneholdende disse,nukleinsyresekvenser som koder for slike peptider, plasmider og virusvektoreromfattende slikenukleinsy |
| US20030152581A1 (en) | 1998-07-30 | 2003-08-14 | Jean-Marie Saint-Remy | Compound and method for the prevention and/or the treatment of allergy |
| AR020102A1 (es) | 1998-07-30 | 2002-04-10 | Ucb Sa | Compuesto para la prevencion y/o tratamiento de la alergia; composicion farmaceutica, composicion cosmetica, composicion en forma de bebida, alimento y/oalimento para animales domesticos que lo comprende y uso de dicho compuesto o dicha composicion farmaceutica para la fabricacion de un alimento |
| CA2350911A1 (en) | 1998-11-16 | 2000-05-25 | Board Of Regents, The University Of Texas System | Hiv-specific t-cell induction |
| GB0006437D0 (en) | 2000-03-17 | 2000-05-10 | Leuven Res & Dev Vzw | Compounds for the modulation of allergen sensitivity by antigens sharing T cell epitopes with allergens |
| AU2001254620A1 (en) * | 2000-04-28 | 2001-11-12 | Novozymes A/S | Lipolytic enzyme variant |
| AU2001272491A1 (en) | 2000-06-26 | 2002-01-08 | Smithkline Beecham Biologicals (S.A.) | Triple fusion proteins comprising ubiquitin fused between thioredoxin and a polypeptide of interest |
| US7049413B2 (en) | 2001-05-18 | 2006-05-23 | Ludwig Institute For Cancer Research | MAGE-A3 peptides presented by HLA class II molecules |
| US20040173778A1 (en) | 2001-05-30 | 2004-09-09 | Roncarolo Maria Grazia | Ex-vivo isolated cd25+cd4+ t cells with immunosuppressive activity and uses thereof |
| EP1432738B1 (en) | 2001-10-03 | 2009-03-04 | Unilever N.V. | Carbohydrate binding domain containing fusion proteins for delivery of therapeutic and other agents, and compositions containing them |
| WO2003072731A2 (en) | 2002-02-21 | 2003-09-04 | Apovia, Inc. | STABILIZED HBc CHIMER PARTICLES HAVING MENINGOCCOCAL IMMUNOGENS |
| US20100183652A1 (en) | 2002-02-21 | 2010-07-22 | Mark Page | STABILIZED HBc CHIMER PARTICLES AS THERAPEUTIC VACCINE FOR CHRONIC HEPATITIS |
| AU2003254950A1 (en) | 2002-08-26 | 2004-03-11 | Kirin Beer Kabushiki Kaisha | Peptides and drugs containing the same |
| CN103073620B (zh) | 2002-09-12 | 2014-12-10 | 肿瘤疗法科学股份有限公司 | Kdr肽和包括该肽的疫苗 |
| JP2004147649A (ja) | 2002-10-11 | 2004-05-27 | Kumamoto Technology & Industry Foundation | 頭頚部癌の抗原 |
| WO2005012502A2 (en) | 2003-03-28 | 2005-02-10 | Idm Pharma, Inc. | Methods of identifying optimal variants of peptide epitopes |
| US7651855B2 (en) | 2003-04-17 | 2010-01-26 | The Trustees Of The University Of Pennsylvania | Regulatory T cells and their use in immunotherapy and suppression of autoimmune responses |
| GB0324265D0 (en) | 2003-10-16 | 2003-11-19 | Medical Res Council | Peptide |
| WO2005042575A2 (en) * | 2003-10-30 | 2005-05-12 | Pharmexa A/S | Method for down-regulation of vegf |
| JP2008044848A (ja) | 2004-11-30 | 2008-02-28 | Univ Kurume | Ｈｌａ−ａ２４拘束性腫瘍抗原ペプチド |
| US8252893B2 (en) | 2005-01-31 | 2012-08-28 | Board Of Trustees Of The University Of Arkansas | CD8 T cell epitopes in HPV 16 E6 and E7 proteins and uses thereof |
| US10183986B2 (en) | 2005-12-15 | 2019-01-22 | Industrial Technology Research Institute | Trimeric collagen scaffold antibodies |
| GB0603081D0 (en) | 2006-02-15 | 2006-03-29 | Dynal Biotech Asa Oslo | Method |
| FR2898275B1 (fr) | 2006-03-10 | 2012-12-14 | Genethon | Cellules t regulatrices cd4+cd25+specifiques pour la greffe de cellules hematopoietiques et la tolerance immunitaire |
| WO2007135684A2 (en) | 2006-05-22 | 2007-11-29 | Hadasit Medical Research Services & Development Limited | Method of treatment of anti-cd4 autoimmunity |
| PT2476435T (pt) | 2006-08-11 | 2018-03-05 | Life Sciences Res Partners Vzw | Péptidos imunogénicos e a sua utilização em distúrbios imunitários |
| EP2158211B1 (en) | 2007-05-31 | 2016-08-10 | Medigene AG | Mutated structural protein of a parvovirus |
| CA2700618A1 (en) | 2007-09-27 | 2009-04-02 | The Board Of Trustees Of The University Of Arkansas | Inhibition of dendritic cell-driven regulatory t cell activation and potentiation of tumor antigen-specific t cell responses by interleukin-15 and map kinase inhibitor |
| WO2009101204A2 (en) | 2008-02-14 | 2009-08-20 | Life Sciences Research Partners Vzw | Elimination of immune responses to viral vectors |
| CA2715611C (en) | 2008-02-14 | 2018-03-13 | Life Sciences Research Partners Vzw | Immunotherapy targeting intracellular pathogens |
| AU2009214041A1 (en) | 2008-02-14 | 2009-08-20 | Katholieke Universiteit Leuven | CD4+ T-cells with cytolytic properties |
| WO2009101206A2 (en) | 2008-02-14 | 2009-08-20 | Life Sciences Research Partners Vzw | Strategies to prevent and/or treat immune responses to soluble allofactors |
| US8999346B2 (en) | 2008-02-14 | 2015-04-07 | Life Sciences Research Partners Vzw | Immunogenic control of tumours and tumour cells |
| US9248171B2 (en) | 2008-02-14 | 2016-02-02 | Imcyse Sa | Immunogenic peptides and their use in transplantation |
| WO2009106073A2 (en) | 2008-02-28 | 2009-09-03 | Dako Denmark A/S | Mhc multimers in borrelia diagnostics and disease |
| KR101022649B1 (ko) | 2008-08-07 | 2011-03-22 | 삼성모바일디스플레이주식회사 | 헤테로고리 화합물 및 이를 이용한 유기 전계 발광 장치 |
| US20110318380A1 (en) | 2008-10-01 | 2011-12-29 | Dako Denmark A/S | MHC Multimers in Cancer Vaccines and Immune Monitoring |
| CN103002909B (zh) | 2010-03-29 | 2016-06-29 | 国家科学研究中心 | 包含含有至少一个cxxc基序的多肽和异源抗原的药物组合物及其用途 |
| RU2615460C2 (ru) * | 2010-11-25 | 2017-04-04 | Имнейт Сарл | Иммуногенные пептиды для применения в профилактике и/или лечении инфекционных заболеваний, аутоиммунных заболеваний, иммунных ответов на аллогенные факторы, аллергических заболеваний, опухолей, отторжения трансплантата и иммунных ответов против вирусных векторов. используемых для генной терапии или генной вакцинации |
| GB201201511D0 (en) | 2012-01-30 | 2012-03-14 | Univ Leuven Kath | Modified epitopes for boosting CD4+ T-cell responses |
| CN104271148A (zh) | 2012-02-15 | 2015-01-07 | 洛桑聚合联合学院 | 红细胞结合性治疗剂 |
| GB201309469D0 (en) | 2013-05-28 | 2013-07-10 | Imcyse Sa | Detection of CD4+ T lymphocytes |
| GB201315946D0 (en) | 2013-09-06 | 2013-10-23 | Immune Targeting Systems Its Ltd | Oncology vaccine |
| GB201319160D0 (en) * | 2013-10-30 | 2013-12-11 | Imcyse Sa | Methods for induction of antigen-specific regulatory t cells |
| GB201418433D0 (en) | 2014-10-17 | 2014-12-03 | Imcyse Sa | Novel immunogenic peptides |
| US10729791B2 (en) | 2015-05-18 | 2020-08-04 | Imcyse Sa | Animal models for evaluating pharmaceutical compounds |
| EP3352782B1 (en) | 2015-09-25 | 2021-03-31 | ImCyse SA | Improved methods and compounds for eliminating immune responses to therapeutic agents |
| KR20240015731A (ko) | 2016-04-19 | 2024-02-05 | 임시스 에스에이 | 신규 면역원성 CD1d 결합 펩티드 |
-
2016
- 2016-09-23 EP EP16778714.2A patent/EP3352782B1/en active Active
- 2016-09-23 WO PCT/EP2016/072690 patent/WO2017050966A1/en not_active Ceased
- 2016-09-23 JP JP2018515566A patent/JP7090335B2/ja active Active
- 2016-09-23 CA CA2995771A patent/CA2995771A1/en active Pending
- 2016-09-23 ES ES16778714T patent/ES2874077T3/es active Active
- 2016-09-23 EP EP21164831.6A patent/EP3939606A3/en not_active Withdrawn
- 2016-09-23 AU AU2016328582A patent/AU2016328582B2/en not_active Ceased
- 2016-09-23 CN CN201680068767.5A patent/CN108289941B/zh not_active Expired - Fee Related
- 2016-09-23 US US15/761,223 patent/US11787849B2/en active Active
-
2023
- 2023-02-24 AU AU2023201135A patent/AU2023201135A1/en not_active Abandoned
- 2023-09-06 US US18/462,035 patent/US20240109951A1/en active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| EP3939606A3 (en) | 2022-04-20 |
| HK1252695A1 (en) | 2019-05-31 |
| JP7090335B2 (ja) | 2022-06-24 |
| WO2017050966A1 (en) | 2017-03-30 |
| AU2023201135A1 (en) | 2023-03-30 |
| CA2995771A1 (en) | 2017-03-30 |
| EP3352782A1 (en) | 2018-08-01 |
| AU2016328582B2 (en) | 2022-11-24 |
| AU2016328582A1 (en) | 2018-03-15 |
| US11787849B2 (en) | 2023-10-17 |
| EP3939606A2 (en) | 2022-01-19 |
| US20180258154A1 (en) | 2018-09-13 |
| JP2018528237A (ja) | 2018-09-27 |
| EP3352782B1 (en) | 2021-03-31 |
| CN108289941A (zh) | 2018-07-17 |
| US20240109951A1 (en) | 2024-04-04 |
| CN108289941B (zh) | 2022-06-21 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2874077T3 (es) | Métodos y compuestos mejorados para eliminar respuestas inmunitarias a agentes terapéuticos | |
| JP2025001671A (ja) | 個別化がんワクチンエピトープの選択 | |
| CA2747180C (en) | Use of flt3 ligand for enhancing immune responses in rna immunization | |
| ES2400249T3 (es) | Vacunas recombinantes y utilización de las mismas | |
| CA2724440C (en) | Strategies to prevent and/or treat immune responses to soluble allofactors | |
| EP2249855B1 (en) | Immunogenic peptides and their use in transplantation | |
| KR102228843B1 (ko) | Cd4+ t-세포 반응의 증강을 위한 변형된 에피토프 | |
| JP6789112B2 (ja) | Ｃｄ４＋ｔリンパ球の検出、調製および枯渇のための向上した方法 | |
| CN109310739A (zh) | 新抗原及其使用方法 | |
| JP7102430B2 (ja) | 糖尿病の治療のためのペプチド及び方法 | |
| RS61190B1 (sr) | Novi peptidi i kombinacija peptida za upotrebu u imunoterapiji protiv raka jajnika i drugih malignih tumora | |
| CN103180730A (zh) | 鉴定肿瘤特异性新抗原的组合物和方法 | |
| MXPA02000746A (es) | Proteinas de fusion fc para incrementar la inmunogenicidad de antigenos de proteina y peptido. | |
| EA029831B1 (ru) | Пептид, индуцирующий цитотоксические т-лимфоциты и стимулирующий антиопухолевые иммунные ответы | |
| JP2025500373A (ja) | Ｍｒｎａ治療用組成物 | |
| WO1995032731A2 (en) | Immunogenic pharmaceuticals | |
| JP2024535855A (ja) | Ｋｒａｓネオ抗原療法 | |
| ES2340357T3 (es) | Antigeno tumoral. | |
| HK40064028A (en) | Improved methods and compounds for eliminating immune responses to therapeutic agents | |
| Neal et al. | Hydrodynamic limb vein delivery of a xenogeneic DNA cancer vaccine effectively induces antitumor immunity | |
| HK1252695B (en) | Improved methods and compounds for eliminating immune responses to therapeutic agents | |
| ES2757604T3 (es) | Nucleasa efectora tal para la inactivación específica del correceptor del VIH CCR5 | |
| JP2010501160A (ja) | 無差別ＨＥＲ−２／ＮｅｕＣＤ４Ｔ細胞エピトープ | |
| EP3795593A1 (en) | Combination of immune-modulators with tumor specific neoantigens for use in prevention and treatment of tumors | |
| CN109069574A (zh) | 用于治疗黑色素瘤的方法和组合物 |