JP7540877B2 - 免疫グロブリン単一可変ドメインの生成方法 - Google Patents
免疫グロブリン単一可変ドメインの生成方法 Download PDFInfo
- Publication number
- JP7540877B2 JP7540877B2 JP2018542263A JP2018542263A JP7540877B2 JP 7540877 B2 JP7540877 B2 JP 7540877B2 JP 2018542263 A JP2018542263 A JP 2018542263A JP 2018542263 A JP2018542263 A JP 2018542263A JP 7540877 B2 JP7540877 B2 JP 7540877B2
- Authority
- JP
- Japan
- Prior art keywords
- nanobody
- expression
- nucleic acid
- seq
- single variable
- 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
- 108060003951 Immunoglobulin Proteins 0.000 title claims description 315
- 102000018358 immunoglobulin Human genes 0.000 title claims description 315
- 238000000034 method Methods 0.000 title claims description 166
- 108090000623 proteins and genes Proteins 0.000 claims description 251
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 246
- 102000004169 proteins and genes Human genes 0.000 claims description 222
- 235000018102 proteins Nutrition 0.000 claims description 221
- 230000014509 gene expression Effects 0.000 claims description 195
- 241000235648 Pichia Species 0.000 claims description 189
- 150000007523 nucleic acids Chemical class 0.000 claims description 142
- 108020004707 nucleic acids Proteins 0.000 claims description 139
- 102000039446 nucleic acids Human genes 0.000 claims description 139
- 101000664600 Homo sapiens Tripartite motif-containing protein 3 Proteins 0.000 claims description 127
- 102100038798 Tripartite motif-containing protein 3 Human genes 0.000 claims description 127
- 230000002068 genetic effect Effects 0.000 claims description 78
- 241000235058 Komagataella pastoris Species 0.000 claims description 67
- 230000027455 binding Effects 0.000 claims description 52
- 108010003723 Single-Domain Antibodies Proteins 0.000 claims description 49
- 150000001413 amino acids Chemical class 0.000 claims description 45
- 238000004519 manufacturing process Methods 0.000 claims description 44
- 210000000349 chromosome Anatomy 0.000 claims description 24
- 235000001014 amino acid Nutrition 0.000 claims description 19
- 101100203200 Danio rerio shha gene Proteins 0.000 claims description 18
- 102000008100 Human Serum Albumin Human genes 0.000 claims description 18
- 108091006905 Human Serum Albumin Proteins 0.000 claims description 18
- 238000013518 transcription Methods 0.000 claims description 18
- 230000035897 transcription Effects 0.000 claims description 18
- 210000004899 c-terminal region Anatomy 0.000 claims description 15
- 230000002708 enhancing effect Effects 0.000 claims description 15
- 108010047041 Complementarity Determining Regions Proteins 0.000 claims description 14
- -1 Kar2p Proteins 0.000 claims description 9
- 102100040881 60S acidic ribosomal protein P0 Human genes 0.000 claims description 6
- 150000001875 compounds Chemical class 0.000 claims description 6
- 210000002966 serum Anatomy 0.000 claims description 6
- 102000007562 Serum Albumin Human genes 0.000 claims description 5
- 108010071390 Serum Albumin Proteins 0.000 claims description 5
- 239000000872 buffer Substances 0.000 claims description 4
- 235000018417 cysteine Nutrition 0.000 claims description 4
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 4
- 239000008194 pharmaceutical composition Substances 0.000 claims description 2
- 101000609814 Dictyostelium discoideum Protein disulfide-isomerase 1 Proteins 0.000 claims 5
- 101000673456 Homo sapiens 60S acidic ribosomal protein P0 Proteins 0.000 claims 5
- 101001114059 Homo sapiens Protein-arginine deiminase type-1 Proteins 0.000 claims 5
- 102100023222 Protein-arginine deiminase type-1 Human genes 0.000 claims 5
- 102000004196 processed proteins & peptides Human genes 0.000 description 244
- 229920001184 polypeptide Polymers 0.000 description 242
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 58
- 102000006010 Protein Disulfide-Isomerase Human genes 0.000 description 38
- 108020003519 protein disulfide isomerase Proteins 0.000 description 38
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 30
- 108010034467 ribosomal protein P0 Proteins 0.000 description 28
- 210000004027 cell Anatomy 0.000 description 27
- 239000012634 fragment Substances 0.000 description 27
- 125000003729 nucleotide group Chemical group 0.000 description 26
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 25
- 239000002773 nucleotide Substances 0.000 description 25
- 239000013598 vector Substances 0.000 description 25
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 24
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 21
- 239000000427 antigen Substances 0.000 description 18
- 108091007433 antigens Proteins 0.000 description 18
- 102000036639 antigens Human genes 0.000 description 18
- 230000001965 increasing effect Effects 0.000 description 18
- 229940024606 amino acid Drugs 0.000 description 17
- 239000013612 plasmid Substances 0.000 description 17
- 230000009466 transformation Effects 0.000 description 17
- 239000013604 expression vector Substances 0.000 description 15
- 239000000047 product Substances 0.000 description 15
- 239000002609 medium Substances 0.000 description 13
- 235000002198 Annona diversifolia Nutrition 0.000 description 12
- 108020004414 DNA Proteins 0.000 description 12
- 238000011002 quantification Methods 0.000 description 12
- 230000028327 secretion Effects 0.000 description 12
- 108010076504 Protein Sorting Signals Proteins 0.000 description 11
- 239000001963 growth medium Substances 0.000 description 11
- 108010025188 Alcohol oxidase Proteins 0.000 description 9
- 125000000539 amino acid group Chemical group 0.000 description 9
- 230000000875 corresponding effect Effects 0.000 description 9
- 229940072221 immunoglobulins Drugs 0.000 description 9
- 230000001939 inductive effect Effects 0.000 description 9
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 9
- 244000303258 Annona diversifolia Species 0.000 description 8
- 101100070241 Mus musculus Hcn2 gene Proteins 0.000 description 8
- 101100314583 Mus musculus Trim3 gene Proteins 0.000 description 8
- 241000282836 Camelus dromedarius Species 0.000 description 7
- 108091026890 Coding region Proteins 0.000 description 7
- 241000588724 Escherichia coli Species 0.000 description 7
- 230000001976 improved effect Effects 0.000 description 7
- 239000003550 marker Substances 0.000 description 7
- 230000001105 regulatory effect Effects 0.000 description 7
- 241000282414 Homo sapiens Species 0.000 description 6
- 241000320412 Ogataea angusta Species 0.000 description 6
- 241000235070 Saccharomyces Species 0.000 description 6
- 239000000203 mixture Substances 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 5
- 241001452677 Ogataea methanolica Species 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 238000012258 culturing Methods 0.000 description 5
- 238000000855 fermentation Methods 0.000 description 5
- 230000004151 fermentation Effects 0.000 description 5
- 230000004927 fusion Effects 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 102000004506 Blood Proteins Human genes 0.000 description 4
- 108010017384 Blood Proteins Proteins 0.000 description 4
- 241000282832 Camelidae Species 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 4
- 108010067193 Formaldehyde transketolase Proteins 0.000 description 4
- 108090000698 Formate Dehydrogenases Proteins 0.000 description 4
- 241000282838 Lama Species 0.000 description 4
- 241000222124 [Candida] boidinii Species 0.000 description 4
- 230000004186 co-expression Effects 0.000 description 4
- 230000001276 controlling effect Effects 0.000 description 4
- 239000012228 culture supernatant Substances 0.000 description 4
- 238000011156 evaluation Methods 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 4
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 239000006152 selective media Substances 0.000 description 4
- 241000894007 species Species 0.000 description 4
- 238000010561 standard procedure Methods 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 3
- 102100032919 Chromobox protein homolog 1 Human genes 0.000 description 3
- 108091035707 Consensus sequence Proteins 0.000 description 3
- 101000616562 Danio rerio Sonic hedgehog protein A Proteins 0.000 description 3
- 101000797584 Homo sapiens Chromobox protein homolog 1 Proteins 0.000 description 3
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 3
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 3
- 241001099157 Komagataella Species 0.000 description 3
- 108700008625 Reporter Genes Proteins 0.000 description 3
- 101000616493 Xenopus laevis Sonic hedgehog protein Proteins 0.000 description 3
- 230000008827 biological function Effects 0.000 description 3
- 229960000074 biopharmaceutical Drugs 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 238000010217 densitometric analysis Methods 0.000 description 3
- 238000003391 densitometric scan Methods 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 3
- 238000010195 expression analysis Methods 0.000 description 3
- 238000012239 gene modification Methods 0.000 description 3
- 230000005017 genetic modification Effects 0.000 description 3
- 235000013617 genetically modified food Nutrition 0.000 description 3
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Chemical compound O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 3
- 230000010354 integration Effects 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 230000002018 overexpression Effects 0.000 description 3
- 239000000825 pharmaceutical preparation Substances 0.000 description 3
- NLKNQRATVPKPDG-UHFFFAOYSA-M potassium iodide Chemical compound [K+].[I-] NLKNQRATVPKPDG-UHFFFAOYSA-M 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 238000001542 size-exclusion chromatography Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 230000005026 transcription initiation Effects 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
- SBKVPJHMSUXZTA-MEJXFZFPSA-N (2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-5-amino-2-[[2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoyl]amino]-5-oxopentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]amino]-4-methylsulfanylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoic acid Chemical group C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 SBKVPJHMSUXZTA-MEJXFZFPSA-N 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 2
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 241000251730 Chondrichthyes Species 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 108060001084 Luciferase Proteins 0.000 description 2
- 239000005089 Luciferase Substances 0.000 description 2
- 108010038049 Mating Factor Proteins 0.000 description 2
- BAVYZALUXZFZLV-UHFFFAOYSA-N Methylamine Chemical compound NC BAVYZALUXZFZLV-UHFFFAOYSA-N 0.000 description 2
- 101710141833 Peroxisomal biogenesis factor 8 Proteins 0.000 description 2
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 230000009824 affinity maturation Effects 0.000 description 2
- 239000000908 ammonium hydroxide Substances 0.000 description 2
- 108091008324 binding proteins Proteins 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- CRQQGFGUEAVUIL-UHFFFAOYSA-N chlorothalonil Chemical compound ClC1=C(Cl)C(C#N)=C(Cl)C(C#N)=C1Cl CRQQGFGUEAVUIL-UHFFFAOYSA-N 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 229910000365 copper sulfate Inorganic materials 0.000 description 2
- ARUVKPQLZAKDPS-UHFFFAOYSA-L copper(II) sulfate Chemical compound [Cu+2].[O-][S+2]([O-])([O-])[O-] ARUVKPQLZAKDPS-UHFFFAOYSA-L 0.000 description 2
- 230000002596 correlated effect Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 239000003623 enhancer Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 238000002744 homologous recombination Methods 0.000 description 2
- 230000006801 homologous recombination Effects 0.000 description 2
- 230000000977 initiatory effect Effects 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 238000004255 ion exchange chromatography Methods 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 210000001322 periplasm Anatomy 0.000 description 2
- 230000008092 positive effect Effects 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000011573 trace mineral Substances 0.000 description 2
- 235000013619 trace mineral Nutrition 0.000 description 2
- 230000032258 transport Effects 0.000 description 2
- 239000013603 viral vector Substances 0.000 description 2
- JIAARYAFYJHUJI-UHFFFAOYSA-L zinc dichloride Chemical compound [Cl-].[Cl-].[Zn+2] JIAARYAFYJHUJI-UHFFFAOYSA-L 0.000 description 2
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 1
- QRBLKGHRWFGINE-UGWAGOLRSA-N 2-[2-[2-[[2-[[4-[[2-[[6-amino-2-[3-amino-1-[(2,3-diamino-3-oxopropyl)amino]-3-oxopropyl]-5-methylpyrimidine-4-carbonyl]amino]-3-[(2r,3s,4s,5s,6s)-3-[(2s,3r,4r,5s)-4-carbamoyl-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)- Chemical compound N=1C(C=2SC=C(N=2)C(N)=O)CSC=1CCNC(=O)C(C(C)=O)NC(=O)C(C)C(O)C(C)NC(=O)C(C(O[C@H]1[C@@]([C@@H](O)[C@H](O)[C@H](CO)O1)(C)O[C@H]1[C@@H]([C@](O)([C@@H](O)C(CO)O1)C(N)=O)O)C=1NC=NC=1)NC(=O)C1=NC(C(CC(N)=O)NCC(N)C(N)=O)=NC(N)=C1C QRBLKGHRWFGINE-UGWAGOLRSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 108020003589 5' Untranslated Regions Proteins 0.000 description 1
- 108050002744 60S acidic ribosomal protein P0 Proteins 0.000 description 1
- 102000013563 Acid Phosphatase Human genes 0.000 description 1
- 108010051457 Acid Phosphatase Proteins 0.000 description 1
- 101100437118 Arabidopsis thaliana AUG1 gene Proteins 0.000 description 1
- 101100407148 Arabidopsis thaliana PBL3 gene Proteins 0.000 description 1
- 101100083253 Caenorhabditis elegans pho-1 gene Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 241000238154 Carcinus maenas Species 0.000 description 1
- 244000062995 Cassia occidentalis Species 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 230000006820 DNA synthesis Effects 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 101100234413 Dictyostelium discoideum kif9 gene Proteins 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 101000893906 Fowl adenovirus A serotype 1 (strain CELO / Phelps) Protein GAM-1 Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000799554 Homo sapiens Protein AATF Proteins 0.000 description 1
- 108050008546 Hyperglycemic hormone Proteins 0.000 description 1
- 241000376403 Hyphopichia Species 0.000 description 1
- 102000004195 Isomerases Human genes 0.000 description 1
- 108090000769 Isomerases Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-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
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 241000577979 Peromyscus spicilegus Species 0.000 description 1
- LTQCLFMNABRKSH-UHFFFAOYSA-N Phleomycin Natural products N=1C(C=2SC=C(N=2)C(N)=O)CSC=1CCNC(=O)C(C(O)C)NC(=O)C(C)C(O)C(C)NC(=O)C(C(OC1C(C(O)C(O)C(CO)O1)OC1C(C(OC(N)=O)C(O)C(CO)O1)O)C=1NC=NC=1)NC(=O)C1=NC(C(CC(N)=O)NCC(N)C(N)=O)=NC(N)=C1C LTQCLFMNABRKSH-UHFFFAOYSA-N 0.000 description 1
- 108010035235 Phleomycins Proteins 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 1
- 102100034180 Protein AATF Human genes 0.000 description 1
- 230000004570 RNA-binding Effects 0.000 description 1
- 238000011529 RT qPCR Methods 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 241000235344 Saccharomycetaceae Species 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- 240000007591 Tilia tomentosa Species 0.000 description 1
- 108091023040 Transcription factor Proteins 0.000 description 1
- 102000040945 Transcription factor Human genes 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 108010084455 Zeocin Proteins 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000011681 asexual reproduction Effects 0.000 description 1
- 238000013465 asexual reproduction Methods 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 108010051210 beta-Fructofuranosidase 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
- 229930189065 blasticidin Natural products 0.000 description 1
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- PASHVRUKOFIRIK-UHFFFAOYSA-L calcium sulfate dihydrate Chemical compound O.O.[Ca+2].[O-]S([O-])(=O)=O PASHVRUKOFIRIK-UHFFFAOYSA-L 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 230000034303 cell budding Effects 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 125000003636 chemical group Chemical group 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000012136 culture method Methods 0.000 description 1
- 239000007933 dermal patch Substances 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 108091006047 fluorescent proteins Proteins 0.000 description 1
- 102000034287 fluorescent proteins Human genes 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 238000012268 genome sequencing Methods 0.000 description 1
- LXJXRIRHZLFYRP-UHFFFAOYSA-N glyceraldehyde 3-phosphate Chemical compound O=CC(O)COP(O)(O)=O LXJXRIRHZLFYRP-UHFFFAOYSA-N 0.000 description 1
- XLYOFNOQVPJJNP-ZSJDYOACSA-N heavy water Substances [2H]O[2H] XLYOFNOQVPJJNP-ZSJDYOACSA-N 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 102000028557 immunoglobulin binding proteins Human genes 0.000 description 1
- 108091009323 immunoglobulin binding proteins Proteins 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 230000007154 intracellular accumulation Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 235000011073 invertase Nutrition 0.000 description 1
- 239000001573 invertase Substances 0.000 description 1
- SURQXAFEQWPFPV-UHFFFAOYSA-L iron(2+) sulfate heptahydrate Chemical compound O.O.O.O.O.O.O.[Fe+2].[O-]S([O-])(=O)=O SURQXAFEQWPFPV-UHFFFAOYSA-L 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000318 kanamycin Drugs 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
- 229930182823 kanamycin A Natural products 0.000 description 1
- 101150083025 kin-2 gene Proteins 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- WRUGWIBCXHJTDG-UHFFFAOYSA-L magnesium sulfate heptahydrate Chemical compound O.O.O.O.O.O.O.[Mg+2].[O-]S([O-])(=O)=O WRUGWIBCXHJTDG-UHFFFAOYSA-L 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 229940099596 manganese sulfate Drugs 0.000 description 1
- 239000011702 manganese sulphate Substances 0.000 description 1
- 235000007079 manganese sulphate Nutrition 0.000 description 1
- SQQMAOCOWKFBNP-UHFFFAOYSA-L manganese(II) sulfate Chemical compound [Mn+2].[O-]S([O-])(=O)=O SQQMAOCOWKFBNP-UHFFFAOYSA-L 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000001450 methanotrophic effect Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- CWCMIVBLVUHDHK-ZSNHEYEWSA-N phleomycin D1 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC[C@@H](N=1)C=1SC=C(N=1)C(=O)NCCCCNC(N)=N)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C CWCMIVBLVUHDHK-ZSNHEYEWSA-N 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 235000011007 phosphoric acid Nutrition 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- OTYBMLCTZGSZBG-UHFFFAOYSA-L potassium sulfate Chemical compound [K+].[K+].[O-]S([O-])(=O)=O OTYBMLCTZGSZBG-UHFFFAOYSA-L 0.000 description 1
- 229910052939 potassium sulfate Inorganic materials 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000012562 protein A resin Substances 0.000 description 1
- 230000012846 protein folding Effects 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 239000012429 reaction media Substances 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000009962 secretion pathway Effects 0.000 description 1
- 230000014639 sexual reproduction Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000011684 sodium molybdate Substances 0.000 description 1
- TVXXNOYZHKPKGW-UHFFFAOYSA-N sodium molybdate (anhydrous) Chemical compound [Na+].[Na+].[O-][Mo]([O-])(=O)=O TVXXNOYZHKPKGW-UHFFFAOYSA-N 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 108010067930 structure-specific endonuclease I Proteins 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-N sulfuric acid Substances OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 229940126585 therapeutic drug Drugs 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000009452 underexpressoin Effects 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000011592 zinc chloride Substances 0.000 description 1
- 235000005074 zinc chloride Nutrition 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/37—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi
- C07K14/39—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi from yeasts
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/10—Immunoglobulins specific features characterized by their source of isolation or production
- C07K2317/14—Specific host cells or culture conditions, e.g. components, pH or temperature
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/35—Valency
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/569—Single domain, e.g. dAb, sdAb, VHH, VNAR or nanobody®
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Mycology (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- Immunology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- General Chemical & Material Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2024038103A JP2024073531A (ja) | 2016-02-12 | 2024-03-12 | 免疫グロブリン単一可変ドメインの生成方法 |
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201662294470P | 2016-02-12 | 2016-02-12 | |
| US62/294,470 | 2016-02-12 | ||
| PCT/EP2017/053034 WO2017137579A1 (en) | 2016-02-12 | 2017-02-10 | Method for the production of immunoglobulin single variable domains |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2024038103A Division JP2024073531A (ja) | 2016-02-12 | 2024-03-12 | 免疫グロブリン単一可変ドメインの生成方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2019507748A JP2019507748A (ja) | 2019-03-22 |
| JP7540877B2 true JP7540877B2 (ja) | 2024-08-27 |
Family
ID=58018106
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2018542263A Active JP7540877B2 (ja) | 2016-02-12 | 2017-02-10 | 免疫グロブリン単一可変ドメインの生成方法 |
| JP2024038103A Pending JP2024073531A (ja) | 2016-02-12 | 2024-03-12 | 免疫グロブリン単一可変ドメインの生成方法 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2024038103A Pending JP2024073531A (ja) | 2016-02-12 | 2024-03-12 | 免疫グロブリン単一可変ドメインの生成方法 |
Country Status (7)
| Country | Link |
|---|---|
| US (2) | US10975141B2 (enExample) |
| EP (1) | EP3414268A1 (enExample) |
| JP (2) | JP7540877B2 (enExample) |
| CN (1) | CN108699151B (enExample) |
| AU (2) | AU2017216864B2 (enExample) |
| CA (1) | CA3014443A1 (enExample) |
| WO (1) | WO2017137579A1 (enExample) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NO2768984T3 (enExample) * | 2015-11-12 | 2018-06-09 | ||
| EP3414268A1 (en) | 2016-02-12 | 2018-12-19 | Ablynx NV | Method for the production of immunoglobulin single variable domains |
| WO2019187911A1 (ja) * | 2018-03-26 | 2019-10-03 | 国立大学法人神戸大学 | 新規細胞及びそれを用いた目的タンパク質の製造方法 |
| CN114981300B (zh) * | 2019-12-06 | 2025-10-31 | 艾伯霖克斯公司 | 包含靶向TNFα和IL-23的免疫球蛋白单个可变结构域的多肽 |
| CN110964113B (zh) * | 2019-12-24 | 2021-09-03 | 北京纽安博生物技术有限公司 | 介导结合免疫球蛋白的单域抗体、由其构建的双功能抗体及其应用 |
| WO2021187560A1 (ja) * | 2020-03-19 | 2021-09-23 | 国立大学法人神戸大学 | 内在性遺伝子の発現が増強された遺伝子組換え細胞の製造方法 |
| EP4126971A1 (en) | 2020-03-30 | 2023-02-08 | Ablynx N.V. | Method for the production and purification of multivalent immunoglobulin single variable domains |
| FR3120866B1 (fr) | 2021-03-19 | 2025-02-28 | Univ Toulouse 3 Paul Sabatier | Molécule hybride comprenant un peptide citrulliné dérivé de la fibrine et un anticorps ou fragment d’anticorps se liant à CD38 et/ou CD138, et ses utilisations |
| FR3120877B1 (fr) | 2021-03-19 | 2025-03-14 | Univ Toulouse 3 Paul Sabatier | Cellule immunitaire comprenant un récepteur Fc à sa surface, et sur lequel est greffé une molécule hybride comprenant un fragment Fc d’anticorps et au moins un peptide citrulliné dérivé de la fibrine, et ses utilisations |
| FR3120865B1 (fr) | 2021-03-19 | 2025-02-28 | Univ Toulouse 3 Paul Sabatier | Molécule hybride comprenant un fragment Fc d’anticorps et au moins un peptide citrulliné dérivé de la fibrine, et ses utilisations |
| CN114920839B (zh) * | 2022-06-17 | 2023-03-10 | 天津大学 | 特异性结合il-23的纳米抗体及其用途 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007132949A1 (ja) | 2006-05-16 | 2007-11-22 | National Institute Of Advanced Industrial Science And Technology | タンパク質の高分泌生産方法 |
| WO2011161266A1 (en) | 2010-06-25 | 2011-12-29 | Ablynx Nv | Improved immunoglobulin single variable domains and constructs thereof directed against cxcr4 |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9212226B2 (en) | 2008-05-16 | 2015-12-15 | Ablynx N.V. | Amino acid sequences directed against CXCR4 and other GPCRs and compounds comprising the same |
| DK2982690T3 (da) | 2009-04-30 | 2021-04-12 | Ablynx Nv | Fremgangsmåde til fremstilling af domæne-antistoffer |
| WO2010135678A1 (en) * | 2009-05-22 | 2010-11-25 | Research Corporation Technologies, Inc. | Nucleic acids of pichia pastoris and use thereof for recombinant production of proteins |
| US20150158948A9 (en) | 2011-03-28 | 2015-06-11 | Francis Descamps | Bispecific anti-cxcr7 immunoglobulin single variable domains |
| PT3248986T (pt) | 2014-05-16 | 2022-04-05 | Ablynx Nv | Domínios variáveis de imunoglobulina |
| EP3414268A1 (en) | 2016-02-12 | 2018-12-19 | Ablynx NV | Method for the production of immunoglobulin single variable domains |
-
2017
- 2017-02-10 EP EP17704752.9A patent/EP3414268A1/en active Pending
- 2017-02-10 AU AU2017216864A patent/AU2017216864B2/en active Active
- 2017-02-10 WO PCT/EP2017/053034 patent/WO2017137579A1/en not_active Ceased
- 2017-02-10 JP JP2018542263A patent/JP7540877B2/ja active Active
- 2017-02-10 US US16/076,314 patent/US10975141B2/en active Active
- 2017-02-10 CA CA3014443A patent/CA3014443A1/en active Pending
- 2017-02-10 CN CN201780010990.9A patent/CN108699151B/zh active Active
-
2020
- 2020-07-30 US US16/943,022 patent/US11851480B2/en active Active
-
2023
- 2023-09-19 AU AU2023233070A patent/AU2023233070A1/en not_active Abandoned
-
2024
- 2024-03-12 JP JP2024038103A patent/JP2024073531A/ja active Pending
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007132949A1 (ja) | 2006-05-16 | 2007-11-22 | National Institute Of Advanced Industrial Science And Technology | タンパク質の高分泌生産方法 |
| WO2011161266A1 (en) | 2010-06-25 | 2011-12-29 | Ablynx Nv | Improved immunoglobulin single variable domains and constructs thereof directed against cxcr4 |
Non-Patent Citations (3)
| Title |
|---|
| Ｂｉｏｔｅｃｈｎｏｌ Ｂｉｏｅｎｇ，２００６ Ｍａｒ ２８，ｖｏｌ．９４，ｎｏ． ２，ｐｐ．３５３－３６１ |
| Ｍｉｃｒｏｂ Ｃｅｌｌ Ｆａｃｔ，２０１０ Ｊｕｎ ３０，ｖｏｌ．９，ａｒｔｉｃｌｅ ｎｏ．４９（ｐｐ．１－１２） |
| Ｔｒｅｎｄｓ Ｂｉｏｔｅｃｈｎｏｌ，２００３ Ｎｏｖ，ｖｏｌ．２１，ｎｏ．１１，ｐｐ．４８４－４９０ |
Also Published As
| Publication number | Publication date |
|---|---|
| AU2017216864A1 (en) | 2018-07-26 |
| CA3014443A1 (en) | 2017-08-17 |
| WO2017137579A1 (en) | 2017-08-17 |
| CN108699151B (zh) | 2022-08-12 |
| JP2019507748A (ja) | 2019-03-22 |
| AU2023233070A1 (en) | 2023-10-05 |
| US11851480B2 (en) | 2023-12-26 |
| US20210047392A1 (en) | 2021-02-18 |
| EP3414268A1 (en) | 2018-12-19 |
| CN108699151A (zh) | 2018-10-23 |
| JP2024073531A (ja) | 2024-05-29 |
| AU2017216864B2 (en) | 2023-06-22 |
| US10975141B2 (en) | 2021-04-13 |
| US20190194302A1 (en) | 2019-06-27 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP7540877B2 (ja) | 免疫グロブリン単一可変ドメインの生成方法 | |
| EP2707382B1 (en) | Method for the production of immunoglobulin single variable domains | |
| AU2013341049B2 (en) | Expression sequences | |
| EP2632946B1 (en) | Method for the production of immunoglobulin single variable domains | |
| JP6138788B2 (ja) | 形質転換した微生物、例えばピキア・パストリス中で抗体などのマルチサブユニットタンパク質を高濃度かつ高純度で生産するための多コピー法 | |
| US11225667B2 (en) | Multi-copy strategy for high-titer and high-purity production of multi-subunit proteins such as antibodies in transformed microbes such as Pichia pastoris | |
| EP2990485B1 (en) | Fd chain gene or l chain gene each capable of increasing secretion amount of fab-type antibody | |
| US12077794B2 (en) | Temperature shift for high yield expression of polypeptides in yeast and other transformed cells | |
| JP7266611B2 (ja) | ペプチドリンカーをコードする改良されたヌクレオチド配列 | |
| NZ621199B2 (en) | Multi-copy strategy for high-titer and high-purity production of multi-subunit proteins such as antibodies in transformed microbes such as pichia pastoris | |
| NZ721102B2 (en) | Multi-copy strategy for high-titer and high-purity production of multi-subunit proteins such as antibodies in transformed microbes such as pichia pastoris |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20200203 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20210323 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20210622 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20211026 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20220125 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20220517 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20220915 |
|
| C60 | Trial request (containing other claim documents, opposition documents) |
Free format text: JAPANESE INTERMEDIATE CODE: C60 Effective date: 20220915 |
|
| C11 | Written invitation by the commissioner to file amendments |
Free format text: JAPANESE INTERMEDIATE CODE: C11 Effective date: 20220927 |
|
| A911 | Transfer to examiner for re-examination before appeal (zenchi) |
Free format text: JAPANESE INTERMEDIATE CODE: A911 Effective date: 20221027 |
|
| C21 | Notice of transfer of a case for reconsideration by examiners before appeal proceedings |
Free format text: JAPANESE INTERMEDIATE CODE: C21 Effective date: 20221101 |
|
| A912 | Re-examination (zenchi) completed and case transferred to appeal board |
Free format text: JAPANESE INTERMEDIATE CODE: A912 Effective date: 20221209 |
|
| C211 | Notice of termination of reconsideration by examiners before appeal proceedings |
Free format text: JAPANESE INTERMEDIATE CODE: C211 Effective date: 20221213 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20240312 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20240815 |
|
| R150 | Certificate of patent or registration of utility model |
Ref document number: 7540877 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |