JP4312403B2 - （ポリ）ペプチド／タンパク質を、ジスルフィド結合を介してバクテリオファージ粒子に表示させる新規方法 - Google Patents
（ポリ）ペプチド／タンパク質を、ジスルフィド結合を介してバクテリオファージ粒子に表示させる新規方法 Download PDFInfo
- Publication number
- JP4312403B2 JP4312403B2 JP2001511164A JP2001511164A JP4312403B2 JP 4312403 B2 JP4312403 B2 JP 4312403B2 JP 2001511164 A JP2001511164 A JP 2001511164A JP 2001511164 A JP2001511164 A JP 2001511164A JP 4312403 B2 JP4312403 B2 JP 4312403B2
- Authority
- JP
- Japan
- Prior art keywords
- protein
- bacteriophage
- phage
- peptide
- coat
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 185
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 155
- 241001515965 unidentified phage Species 0.000 title claims abstract description 118
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 102
- 238000000034 method Methods 0.000 title claims abstract description 83
- 239000002245 particle Substances 0.000 title claims abstract description 79
- 235000018102 proteins Nutrition 0.000 claims description 148
- 239000013598 vector Substances 0.000 claims description 107
- 101710132601 Capsid protein Proteins 0.000 claims description 82
- 101710094648 Coat protein Proteins 0.000 claims description 82
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 claims description 82
- 101710125418 Major capsid protein Proteins 0.000 claims description 82
- 101710141454 Nucleoprotein Proteins 0.000 claims description 82
- 101710083689 Probable capsid protein Proteins 0.000 claims description 82
- 150000007523 nucleic acids Chemical group 0.000 claims description 50
- 235000001014 amino acid Nutrition 0.000 claims description 42
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 40
- 150000001413 amino acids Chemical class 0.000 claims description 33
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 29
- 230000027455 binding Effects 0.000 claims description 27
- 210000004777 protein coat Anatomy 0.000 claims description 25
- 239000012634 fragment Substances 0.000 claims description 24
- 235000018417 cysteine Nutrition 0.000 claims description 22
- 241000724791 Filamentous phage Species 0.000 claims description 19
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 19
- 238000004519 manufacturing process Methods 0.000 claims description 19
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 17
- 238000001514 detection method Methods 0.000 claims description 17
- 108020004707 nucleic acids Proteins 0.000 claims description 16
- 102000039446 nucleic acids Human genes 0.000 claims description 16
- 125000000539 amino acid group Chemical group 0.000 claims description 12
- 238000000746 purification Methods 0.000 claims description 12
- 108060003951 Immunoglobulin Proteins 0.000 claims description 9
- 102000018358 immunoglobulin Human genes 0.000 claims description 9
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims description 7
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims description 7
- 238000012216 screening Methods 0.000 claims description 7
- 230000015572 biosynthetic process Effects 0.000 claims description 6
- 108020001775 protein parts Proteins 0.000 claims 1
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 22
- 239000000427 antigen Substances 0.000 description 81
- 102000036639 antigens Human genes 0.000 description 79
- 108091007433 antigens Proteins 0.000 description 79
- 238000004091 panning Methods 0.000 description 49
- 210000004027 cell Anatomy 0.000 description 42
- 238000002965 ELISA Methods 0.000 description 32
- 238000002474 experimental method Methods 0.000 description 24
- 239000000758 substrate Substances 0.000 description 21
- 229920001213 Polysorbate 20 Polymers 0.000 description 19
- 235000013336 milk Nutrition 0.000 description 19
- 239000008267 milk Substances 0.000 description 19
- 210000004080 milk Anatomy 0.000 description 19
- 238000002823 phage display Methods 0.000 description 19
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 19
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 19
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 18
- 238000010561 standard procedure Methods 0.000 description 18
- UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 15
- 235000013861 fat-free Nutrition 0.000 description 14
- 102100034278 Annexin A6 Human genes 0.000 description 13
- 108090000656 Annexin A6 Proteins 0.000 description 13
- 208000015181 infectious disease Diseases 0.000 description 13
- 230000009870 specific binding Effects 0.000 description 13
- 108010076504 Protein Sorting Signals Proteins 0.000 description 11
- 239000000872 buffer Substances 0.000 description 11
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 11
- 239000013612 plasmid Substances 0.000 description 11
- 238000001262 western blot Methods 0.000 description 11
- 101000599852 Homo sapiens Intercellular adhesion molecule 1 Proteins 0.000 description 10
- 102100037877 Intercellular adhesion molecule 1 Human genes 0.000 description 10
- 239000003638 chemical reducing agent Substances 0.000 description 10
- 230000004927 fusion Effects 0.000 description 10
- 241000588724 Escherichia coli Species 0.000 description 9
- 238000007792 addition Methods 0.000 description 9
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 9
- 238000010790 dilution Methods 0.000 description 9
- 239000012895 dilution Substances 0.000 description 9
- 238000010828 elution Methods 0.000 description 9
- 239000013604 expression vector Substances 0.000 description 9
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 8
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 8
- 238000013459 approach Methods 0.000 description 8
- 210000004899 c-terminal region Anatomy 0.000 description 8
- 238000010367 cloning Methods 0.000 description 8
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 7
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 7
- 102000037865 fusion proteins Human genes 0.000 description 7
- 108020001507 fusion proteins Proteins 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- QRXMUCSWCMTJGU-UHFFFAOYSA-N 5-bromo-4-chloro-3-indolyl phosphate Chemical compound C1=C(Br)C(Cl)=C2C(OP(O)(=O)O)=CNC2=C1 QRXMUCSWCMTJGU-UHFFFAOYSA-N 0.000 description 6
- 101100112922 Candida albicans CDR3 gene Proteins 0.000 description 6
- 101001046686 Homo sapiens Integrin alpha-M Proteins 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 230000003993 interaction Effects 0.000 description 6
- 101100295756 Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81) omp38 gene Proteins 0.000 description 5
- 241000701959 Escherichia virus Lambda Species 0.000 description 5
- 101710155188 Hexon-interlacing protein Proteins 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- 101150042295 arfA gene Proteins 0.000 description 5
- 238000010276 construction Methods 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- 239000003550 marker Substances 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 5
- 101150087557 omcB gene Proteins 0.000 description 5
- 101150115693 ompA gene Proteins 0.000 description 5
- 239000000843 powder Substances 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 108010011170 Ala-Trp-Arg-His-Pro-Gln-Phe-Gly-Gly Proteins 0.000 description 4
- 241000196324 Embryophyta Species 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 239000011230 binding agent Substances 0.000 description 4
- 239000002299 complementary DNA Substances 0.000 description 4
- 239000000539 dimer Substances 0.000 description 4
- 230000002068 genetic effect Effects 0.000 description 4
- 238000003119 immunoblot Methods 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 108091005573 modified proteins Proteins 0.000 description 4
- 102000035118 modified proteins Human genes 0.000 description 4
- 238000011533 pre-incubation Methods 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 230000032258 transport Effects 0.000 description 4
- 108020004705 Codon Proteins 0.000 description 3
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 3
- 241001524679 Escherichia virus M13 Species 0.000 description 3
- 101710154606 Hemagglutinin Proteins 0.000 description 3
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 3
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 3
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 3
- 101710176177 Protein A56 Proteins 0.000 description 3
- 101100084022 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) lapA gene Proteins 0.000 description 3
- 239000007983 Tris buffer Substances 0.000 description 3
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 238000012512 characterization method Methods 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 150000001945 cysteines Chemical class 0.000 description 3
- 239000000185 hemagglutinin Substances 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 229930182817 methionine Natural products 0.000 description 3
- 108700010839 phage proteins Proteins 0.000 description 3
- 101150009573 phoA gene Proteins 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 108010039627 Aprotinin Proteins 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 2
- 235000014469 Bacillus subtilis Nutrition 0.000 description 2
- 241000233866 Fungi Species 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 108010090804 Streptavidin Proteins 0.000 description 2
- 108010028230 Trp-Ser- His-Pro-Gln-Phe-Glu-Lys Proteins 0.000 description 2
- BTKMJKKKZATLBU-UHFFFAOYSA-N [2-(1,3-benzothiazol-2-yl)-1,3-benzothiazol-6-yl] dihydrogen phosphate Chemical compound C1=CC=C2SC(C3=NC4=CC=C(C=C4S3)OP(O)(=O)O)=NC2=C1 BTKMJKKKZATLBU-UHFFFAOYSA-N 0.000 description 2
- 238000001261 affinity purification Methods 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 238000002224 dissection Methods 0.000 description 2
- 108010006205 fluorescein isothiocyanate bovine serum albumin Proteins 0.000 description 2
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 2
- 239000000833 heterodimer Substances 0.000 description 2
- 230000016784 immunoglobulin production Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 238000004806 packaging method and process Methods 0.000 description 2
- 210000001322 periplasm Anatomy 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 241000712461 unidentified influenza virus Species 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 101710145634 Antigen 1 Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102100021935 C-C motif chemokine 26 Human genes 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 241000702374 Enterobacteria phage fd Species 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 101000871768 Escherichia phage P2 Baseplate protein J Proteins 0.000 description 1
- 101000701698 Escherichia phage P2 Spike protein Proteins 0.000 description 1
- 108010020195 FLAG peptide Proteins 0.000 description 1
- XZWYTXMRWQJBGX-VXBMVYAYSA-N FLAG peptide Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(O)=O)CC1=CC=C(O)C=C1 XZWYTXMRWQJBGX-VXBMVYAYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000897493 Homo sapiens C-C motif chemokine 26 Proteins 0.000 description 1
- 101000979342 Homo sapiens Nuclear factor NF-kappa-B p105 subunit Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 101710135898 Myc proto-oncogene protein Proteins 0.000 description 1
- 102100038895 Myc proto-oncogene protein Human genes 0.000 description 1
- 238000005481 NMR spectroscopy Methods 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 102100023050 Nuclear factor NF-kappa-B p105 subunit Human genes 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 239000002033 PVDF binder Substances 0.000 description 1
- 108010067902 Peptide Library Proteins 0.000 description 1
- 101900205473 Plasmodium falciparum Circumsporozoite protein Proteins 0.000 description 1
- 241000350158 Prioria balsamifera Species 0.000 description 1
- 101710094223 Probable baseplate hub protein Proteins 0.000 description 1
- 101710150448 Transcriptional regulator Myc Proteins 0.000 description 1
- 241000499912 Trichoderma reesei Species 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000002730 additional effect Effects 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 230000019552 anatomical structure morphogenesis Effects 0.000 description 1
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 1
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
- 101150010487 are gene Proteins 0.000 description 1
- 238000003491 array Methods 0.000 description 1
- 238000013320 baculovirus expression vector system Methods 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 229960005156 digoxin Drugs 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 239000000710 homodimer Substances 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 102000047410 human NFKB1 Human genes 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000004001 molecular interaction Effects 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 229940051173 recombinant immunotoxin Drugs 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000002195 soluble material Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B40/00—Libraries per se, e.g. arrays, mixtures
- C40B40/02—Libraries contained in or displayed by microorganisms, e.g. bacteria or animal cells; Libraries contained in or displayed by vectors, e.g. plasmids; Libraries containing only microorganisms or vectors
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- 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
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
-
- 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
- C12N2795/00—Bacteriophages
- C12N2795/00011—Details
- C12N2795/10011—Details dsDNA Bacteriophages
- C12N2795/10022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Wood Science & Technology (AREA)
- Virology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Plant Pathology (AREA)
- Gastroenterology & Hepatology (AREA)
- Physics & Mathematics (AREA)
- Crystallography & Structural Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Processes Of Treating Macromolecular Substances (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP99114072.4 | 1999-07-20 | ||
| EP99114072 | 1999-07-20 | ||
| EP00103551.8 | 2000-02-18 | ||
| EP00103551 | 2000-02-18 | ||
| PCT/EP2000/006968 WO2001005950A2 (en) | 1999-07-20 | 2000-07-20 | Methods for displaying (poly)peptides/proteins on bacteriophage particles via disulfide bonds |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2003505025A JP2003505025A (ja) | 2003-02-12 |
| JP2003505025A5 JP2003505025A5 (enExample) | 2008-09-25 |
| JP4312403B2 true JP4312403B2 (ja) | 2009-08-12 |
Family
ID=26070571
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2001511164A Expired - Lifetime JP4312403B2 (ja) | 1999-07-20 | 2000-07-20 | （ポリ）ペプチド／タンパク質を、ジスルフィド結合を介してバクテリオファージ粒子に表示させる新規方法 |
Country Status (13)
| Country | Link |
|---|---|
| US (3) | US6753136B2 (enExample) |
| EP (2) | EP1144607B1 (enExample) |
| JP (1) | JP4312403B2 (enExample) |
| AT (1) | ATE417925T1 (enExample) |
| AU (1) | AU781396B2 (enExample) |
| CA (1) | CA2347973C (enExample) |
| DE (1) | DE60041119D1 (enExample) |
| DK (1) | DK1144607T5 (enExample) |
| ES (1) | ES2327382T3 (enExample) |
| IL (2) | IL142025A0 (enExample) |
| NO (1) | NO331199B1 (enExample) |
| PT (1) | PT1144607E (enExample) |
| WO (1) | WO2001005950A2 (enExample) |
Families Citing this family (136)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6472147B1 (en) * | 1999-05-25 | 2002-10-29 | The Scripps Research Institute | Methods for display of heterodimeric proteins on filamentous phage using pVII and pIX, compositions, vectors and combinatorial libraries |
| US7037706B1 (en) | 1999-09-29 | 2006-05-02 | Xenoport, Inc. | Compounds displayed on replicable genetic packages and methods of using same |
| EP1224327A4 (en) * | 1999-09-29 | 2004-09-08 | Xenoport Inc | COMPOSITIONS ON GENETICALLY REPLICABLE PRODUCTS AND METHODS FOR THEIR USE |
| US8288322B2 (en) | 2000-04-17 | 2012-10-16 | Dyax Corp. | Methods of constructing libraries comprising displayed and/or expressed members of a diverse family of peptides, polypeptides or proteins and the novel libraries |
| PT2308982E (pt) * | 2000-04-17 | 2015-03-04 | Dyax Corp | Métodos para construir bibliotecas de pacotes genéticos que representam os membros de uma família diversificada de péptidos |
| EP1360288B1 (en) | 2000-12-18 | 2011-02-16 | Dyax Corp. | Focused libraries of genetic packages |
| US7229757B2 (en) | 2001-03-21 | 2007-06-12 | Xenoport, Inc. | Compounds displayed on icosahedral phage and methods of using same |
| US6833441B2 (en) | 2001-08-01 | 2004-12-21 | Abmaxis, Inc. | Compositions and methods for generating chimeric heteromultimers |
| US7202045B2 (en) * | 2001-09-19 | 2007-04-10 | Regents Of The University Of Michigan | Detection and treatment of cancers of the lung |
| US7175983B2 (en) | 2001-11-02 | 2007-02-13 | Abmaxis, Inc. | Adapter-directed display systems |
| US8206977B2 (en) * | 2002-07-30 | 2012-06-26 | Morphosys Ag | Tricistronic vectors and uses therefor |
| US20040067532A1 (en) * | 2002-08-12 | 2004-04-08 | Genetastix Corporation | High throughput generation and affinity maturation of humanized antibody |
| NZ539226A (en) | 2002-11-09 | 2008-09-26 | Medigene Ltd | T cell receptor display |
| JP2007524348A (ja) | 2003-01-07 | 2007-08-30 | ダイアックス、コープ | クニッツドメインライブラリー |
| JP2008504013A (ja) | 2004-02-06 | 2008-02-14 | モルフォシス・アクチェンゲゼルシャフト | 抗ｃｄ３８ヒト抗体及びその用途 |
| MXPA06008700A (es) | 2004-02-06 | 2007-01-19 | Morphosys Ag | Anticuerpos anti-cd38 humanos y usos para los mismos. |
| US9200061B2 (en) | 2004-02-06 | 2015-12-01 | Morpho Sys AG | Generation and profiling of fully human HuCAL gold®-derived therapeutic antibodies specific for human CD3i |
| WO2006125640A2 (en) | 2005-05-24 | 2006-11-30 | Morphosys Ag | Generation and profiling of fully human hucal gold®-derived therapeutic antibodies specific for human cd38 |
| WO2006095345A2 (en) | 2005-03-08 | 2006-09-14 | Ramot At Tel-Aviv University Ltd. | Targeted drug-carrying bacteriophages |
| HUE058876T2 (hu) | 2005-05-18 | 2022-09-28 | Morphosys Ag | Anti-GM-CSF antitestek és felhasználásuk |
| US8114964B2 (en) | 2005-05-19 | 2012-02-14 | Centocor, Inc. | Anti-MCP-1 antibodies, compositions, methods and uses |
| HUE035250T2 (hu) | 2005-10-12 | 2018-05-02 | Morphosys Ag | Humán CD38-ra specifikus teljesen humán HuCAL GOLD-eredetû terápiás ellenanyagok létrehozása és profilozása |
| DE502005009389D1 (de) | 2005-11-09 | 2010-05-20 | Morphosys Ag | Identifizierung und charakterisierung von funktionsblockierenden anti-ed-b-fibronektin antikörpern |
| DOP2006000277A (es) | 2005-12-12 | 2007-08-31 | Bayer Pharmaceuticals Corp | Anticuerpos anti mn y métodos para su utilización |
| US8273688B2 (en) * | 2005-12-20 | 2012-09-25 | Morphosys Ag | Collection of HCDR3 regions and uses therefor |
| BRPI0709917A2 (pt) | 2006-03-30 | 2011-07-05 | Novartis Ag | composições e métodos de uso para anticorpos de c-met |
| CA2651111A1 (en) | 2006-05-04 | 2007-11-15 | Abmaxis Inc. | Cross-species and multi-species display systems |
| EP2402437B1 (en) | 2006-07-05 | 2016-06-01 | Catalyst Biosciences, Inc. | Protease screening methods and proteases identified thereby |
| DK2102338T3 (da) | 2006-12-12 | 2010-11-01 | Morphosys Ag | Internalisering |
| JP2011504722A (ja) * | 2007-08-21 | 2011-02-17 | モルフォシス・アー・ゲー | ジスルフィド結合形成のための改良された方法 |
| DK2199390T3 (en) | 2007-08-30 | 2017-04-03 | Daiichi Sankyo Co Ltd | ANTI-EphA2 ANTIBODY |
| CN101855242B (zh) * | 2007-09-14 | 2014-07-30 | 阿迪马布有限责任公司 | 合理设计的合成抗体文库及其用途 |
| US8877688B2 (en) * | 2007-09-14 | 2014-11-04 | Adimab, Llc | Rationally designed, synthetic antibody libraries and uses therefor |
| TWI489993B (zh) | 2007-10-12 | 2015-07-01 | Novartis Ag | 骨硬化素（ｓｃｌｅｒｏｓｔｉｎ）抗體組合物及使用方法 |
| PL2215121T3 (pl) | 2007-11-26 | 2016-07-29 | Bayer Ip Gmbh | Przeciwciała przeciwko mezotelinie i ich zastosowania |
| ES2509959T5 (en) * | 2008-02-05 | 2024-12-19 | Bicyclerd Ltd | Methods and compositions |
| US9873957B2 (en) | 2008-03-13 | 2018-01-23 | Dyax Corp. | Libraries of genetic packages comprising novel HC CDR3 designs |
| US10485879B2 (en) | 2008-04-15 | 2019-11-26 | Government Of The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services, National Institutes Of Health | Plasma cell cytokine vehicle containing fusion proteins for targeted introduction of siRNA into cells and tissues |
| EP2276511A2 (en) | 2008-04-15 | 2011-01-26 | Government of the United States of America, as represented by the Secretary, Department of Health and Human Services | Compositions and methods for delivering inhibitory oligonucleotides |
| AU2009240481B2 (en) | 2008-04-24 | 2015-07-30 | Takeda Pharmaceutical Company Limited | Libraries of genetic packages comprising novel HC CDR1, CDR2, and CDR3 and novel LC CDR1, CDR2, and CDR3 designs |
| BRPI0916668B1 (pt) | 2008-08-05 | 2021-12-28 | Novartis Ag | Anticorpo monoclonal isolado, composição farmacêutica, ácido nucleico isolado e vetor |
| WO2010028347A2 (en) | 2008-09-05 | 2010-03-11 | President & Fellows Of Harvard College | Continuous directed evolution of proteins and nucleic acids |
| WO2010079189A1 (en) | 2009-01-09 | 2010-07-15 | Morphosys Ag | Display vectors and methods and uses thereof |
| TWI480050B (zh) | 2009-02-10 | 2015-04-11 | Daiichi Sankyo Co Ltd | 抗－ｍｓｔ１ｒ抗體及其用途 |
| MX2011011338A (es) | 2009-04-27 | 2012-04-19 | Novartis Ag | Composiciones y metodos de uso para anticuerpos terapeuticos especificos para la subunidad beta1 del receptor de il-12. |
| SG174273A1 (en) | 2009-04-27 | 2011-10-28 | Novartis Ag | Compositions and methods for increasing muscle growth |
| AR076284A1 (es) | 2009-04-29 | 2011-06-01 | Bayer Schering Pharma Ag | Inmunoconjugados de antimesotelina y usos de los mismos |
| JP2012525134A (ja) * | 2009-04-30 | 2012-10-22 | サイトス バイオテクノロジー アーゲー | インフルエンザ赤血球凝集素の組成物とその使用 |
| SG175407A1 (en) | 2009-05-29 | 2011-11-28 | Morphosys Ag | A collection and methods for its use |
| WO2011021146A1 (en) | 2009-08-20 | 2011-02-24 | Pfizer Inc. | Osteopontin antibodies |
| US20110082054A1 (en) * | 2009-09-14 | 2011-04-07 | Dyax Corp. | Libraries of genetic packages comprising novel hc cdr3 designs |
| WO2011035205A2 (en) | 2009-09-18 | 2011-03-24 | Calmune Corporation | Antibodies against candida, collections thereof and methods of use |
| EP2501824A4 (en) | 2009-11-17 | 2013-06-19 | Janssen Biotech Inc | IMPROVED PROTEIN DEPOSITION ON BACTERIA MEMBRANES |
| ES2581571T3 (es) | 2009-11-17 | 2016-09-06 | Janssen Biotech, Inc. | Presentación de proteínas diméricas de disulfuro vinculado en fagos filamentosos |
| EP2528944B1 (en) | 2010-01-29 | 2015-08-12 | MorphoSys AG | Rodent combinatorial antibody libraries |
| PE20130206A1 (es) | 2010-05-06 | 2013-02-28 | Novartis Ag | Anticuerpos multivalentes antagonistas de lrp6 (proteina relacionada con lipoproteinas de baja densidad 6) y composiciones |
| WO2011138392A1 (en) | 2010-05-06 | 2011-11-10 | Novartis Ag | Compositions and methods of use for therapeutic low density lipoprotein -related protein 6 (lrp6) antibodies |
| EP3336225B1 (en) | 2010-07-16 | 2020-02-19 | Adimab, LLC | Antibody libraries |
| ME02637B (me) | 2010-08-20 | 2017-06-20 | Novartis Ag | Antitela za receptor 3 faktora rasta epiderma (her3) |
| CA2810359C (en) | 2010-09-09 | 2021-06-22 | Pfizer Inc. | 4-1bb binding molecules |
| KR20130066682A (ko) | 2010-10-05 | 2013-06-20 | 다이이찌 산쿄 가부시키가이샤 | 항체 표적 파골세포－관련 단백질 ｓｉｇｌｅｃ－１５ |
| NZ609707A (en) | 2010-11-19 | 2014-12-24 | Morphosys Ag | A collection and methods for its use |
| WO2012088381A2 (en) | 2010-12-22 | 2012-06-28 | President And Fellows Of Harvard College | Continuous directed evolution |
| WO2013010955A1 (en) | 2011-07-15 | 2013-01-24 | Morphosys Ag | Antibodies that are cross-reactive for macrophage migration inhibitory factor (mif) and d-dopachrome tautomerase (d-dt) |
| JP2014530836A (ja) | 2011-10-19 | 2014-11-20 | モルフォシス・アー・ゲー | 炎症障害治療用のｉｌ１７ｃのアンタゴニスト |
| ES2758433T3 (es) | 2011-12-05 | 2020-05-05 | Novartis Ag | Anticuerpos contra el receptor 3 del factor de crecimiento epidérmico (HER3) |
| KR20140103135A (ko) | 2011-12-05 | 2014-08-25 | 노파르티스 아게 | Her3의 도메인 ii에 대해 지시된 표피 성장 인자 수용체 3 (her3)에 대한 항체 |
| EP2810069A4 (en) * | 2012-02-03 | 2015-08-12 | Univ Alberta | METHOD FOR THE QUANTIFICATION OF PEPTIDE DERIVATIVE LIBRARIES BY PHAG DISPLAY |
| SG11201408330XA (en) | 2012-05-24 | 2015-01-29 | Mountgate Group Ltd | Compositions and methods related to prevention and treatment of rabies infection |
| ES2734130T3 (es) | 2012-08-17 | 2019-12-04 | Morphosys Ag | Anticuerpos específicos de complejos y fragmentos de anticuerpo y su uso |
| JOP20200308A1 (ar) | 2012-09-07 | 2017-06-16 | Novartis Ag | جزيئات إرتباط il-18 |
| BR112015010722A2 (pt) | 2012-11-09 | 2017-08-22 | Pfizer | Anticorpos específicos de fator de crescimento derivado de plaquetas de isoforma b e composições e usos dos mesmos |
| US9428577B2 (en) | 2012-11-09 | 2016-08-30 | Pfizer Inc. | Platelet-derived growth factor B specific antibodies and compositions and uses thereof |
| EP2935324B1 (en) | 2012-12-20 | 2019-10-23 | MorphoSys AG | Anti-staphylococcal antibodies |
| CN105246916A (zh) | 2013-03-14 | 2016-01-13 | 诺华股份有限公司 | 针对notch 3的抗体 |
| KR20150131173A (ko) | 2013-03-15 | 2015-11-24 | 노파르티스 아게 | 항체 약물 접합체 |
| KR20150140752A (ko) | 2013-04-12 | 2015-12-16 | 모르포시스 아게 | M-csf를 표적으로 하는 항체 |
| WO2014170317A1 (en) | 2013-04-17 | 2014-10-23 | Morphosys Ag | Antibodies targeting specifically human cxcr2 |
| US10494434B2 (en) | 2013-12-20 | 2019-12-03 | Fred Hutchinson Cancer Research Center | Tagged chimeric effector molecules and receptors thereof |
| US10179911B2 (en) | 2014-01-20 | 2019-01-15 | President And Fellows Of Harvard College | Negative selection and stringency modulation in continuous evolution systems |
| RU2722696C2 (ru) | 2014-03-14 | 2020-06-03 | Иммунокор Лимитед | Библиотеки tcr |
| WO2016020791A1 (en) | 2014-08-05 | 2016-02-11 | Novartis Ag | Ckit antibody drug conjugates |
| WO2016077052A2 (en) | 2014-10-22 | 2016-05-19 | President And Fellows Of Harvard College | Evolution of proteases |
| WO2016075670A1 (en) | 2014-11-14 | 2016-05-19 | Novartis Ag | Antibody drug conjugates |
| ES2904573T3 (es) | 2015-03-27 | 2022-04-05 | Univ Southern California | Terapia con células T dirigida a LHR para el tratamiento de tumores sólidos |
| WO2016168631A1 (en) | 2015-04-17 | 2016-10-20 | President And Fellows Of Harvard College | Vector-based mutagenesis system |
| JP6985934B2 (ja) * | 2015-04-29 | 2021-12-22 | フレッド ハッチンソン キャンサー リサーチ センター | 操作された造血幹細胞／前駆細胞及び非ｔエフェクター細胞、ならびにその使用 |
| US11827904B2 (en) | 2015-04-29 | 2023-11-28 | Fred Hutchinson Cancer Center | Modified stem cells and uses thereof |
| EP3095465A1 (en) | 2015-05-19 | 2016-11-23 | U3 Pharma GmbH | Combination of fgfr4-inhibitor and bile acid sequestrant |
| AU2016270474A1 (en) | 2015-06-04 | 2018-01-04 | University Of Southern California | Lym-1 and Lym-2 targeted CAR cell immunotherapy |
| AU2016273028B2 (en) | 2015-06-05 | 2019-02-14 | Novartis Ag | Antibodies targeting bone morphogenetic protein 9 (BMP9) and methods therefor |
| JOP20200312A1 (ar) | 2015-06-26 | 2017-06-16 | Novartis Ag | الأجسام المضادة للعامل xi وطرق الاستخدام |
| US10392674B2 (en) | 2015-07-22 | 2019-08-27 | President And Fellows Of Harvard College | Evolution of site-specific recombinases |
| US11524983B2 (en) | 2015-07-23 | 2022-12-13 | President And Fellows Of Harvard College | Evolution of Bt toxins |
| WO2017019895A1 (en) | 2015-07-30 | 2017-02-02 | President And Fellows Of Harvard College | Evolution of talens |
| EP3347377B1 (en) | 2015-09-09 | 2021-02-17 | Novartis AG | Thymic stromal lymphopoietin (tslp)-binding antibodies and methods of using the antibodies |
| WO2017042701A1 (en) | 2015-09-09 | 2017-03-16 | Novartis Ag | Thymic stromal lymphopoietin (tslp)-binding antibodies and methods of using the antibodies |
| GB201516269D0 (en) | 2015-09-15 | 2015-10-28 | Adaptimmune Ltd And Immunocore Ltd | TCR Libraries |
| GB201516277D0 (en) | 2015-09-15 | 2015-10-28 | Adaptimmune Ltd And Immunocore Ltd | TCR libraries |
| GB201516272D0 (en) | 2015-09-15 | 2015-10-28 | Adaptimmune Ltd And Immunocore Ltd | TCR Libraries |
| GB201516275D0 (en) | 2015-09-15 | 2015-10-28 | Adaptimmune Ltd And Immunocore Ltd | TCR Libraries |
| GB201516265D0 (en) | 2015-09-15 | 2015-10-28 | Adaptimmune Ltd And Immunocore Ltd | TCR Libraries |
| GB201516274D0 (en) | 2015-09-15 | 2015-10-28 | Adaptimmune Ltd And Immunocore Ltd | TCR Libraries |
| GB201516270D0 (en) | 2015-09-15 | 2015-10-28 | Adaptimmune Ltd And Immunocore Ltd | TCR Libraries |
| EP3569244A1 (en) | 2015-09-23 | 2019-11-20 | CytoImmune Therapeutics, LLC | Flt3 directed car cells for immunotherapy |
| US12043852B2 (en) | 2015-10-23 | 2024-07-23 | President And Fellows Of Harvard College | Evolved Cas9 proteins for gene editing |
| US11180546B2 (en) | 2016-02-17 | 2021-11-23 | Novartis Ag | TGFbeta 2 antibodies |
| MA43088B1 (fr) | 2016-02-19 | 2020-10-28 | Morphosys Ag | Anticorps anti-il-17c |
| TW201802121A (zh) | 2016-05-25 | 2018-01-16 | 諾華公司 | 抗因子XI/XIa抗體之逆轉結合劑及其用途 |
| EP3538552B1 (en) | 2016-11-14 | 2023-09-13 | MorphoSys AG | Fab molecules with a rodent hinge region and a non-rodent ch1 region |
| WO2018229715A1 (en) | 2017-06-16 | 2018-12-20 | Novartis Ag | Compositions comprising anti-cd32b antibodies and methods of use thereof |
| US11447809B2 (en) | 2017-07-06 | 2022-09-20 | President And Fellows Of Harvard College | Evolution of tRNA synthetases |
| EP3444275A1 (en) | 2017-08-16 | 2019-02-20 | Exiris S.r.l. | Monoclonal antibody anti-fgfr4 |
| WO2019040935A1 (en) | 2017-08-25 | 2019-02-28 | President And Fellows Of Harvard College | EVOLUTION OF PEPTIDASES BONT |
| WO2019056002A1 (en) | 2017-09-18 | 2019-03-21 | President And Fellows Of Harvard College | CONTINUOUS EVOLUTION FOR STABILIZED PROTEINS |
| WO2019094595A2 (en) | 2017-11-09 | 2019-05-16 | Pinteon Therapeutics Inc. | Methods and compositions for the generation and use of humanized conformation-specific phosphorylated tau antibodies |
| CN111902427A (zh) | 2017-11-22 | 2020-11-06 | 诺华股份有限公司 | 抗因子XI/XIa抗体的逆转结合剂及其用途 |
| EP3774926A1 (en) | 2018-04-05 | 2021-02-17 | Bio-Rad ABD Serotec GmbH | Display systems for proteins of interest |
| JP7080352B2 (ja) | 2018-05-16 | 2022-06-03 | モルフォシス・アーゲー | 糖タンパク質ｖｉを標的とする抗体 |
| US11913044B2 (en) | 2018-06-14 | 2024-02-27 | President And Fellows Of Harvard College | Evolution of cytidine deaminases |
| WO2019244107A1 (en) | 2018-06-21 | 2019-12-26 | Daiichi Sankyo Company, Limited | Compositions including cd3 antigen binding fragments and uses thereof |
| CA3106722A1 (en) | 2018-07-23 | 2020-01-30 | The Governors Of The University Of Alberta | Genetically-encoded bicyclic peptide libraries |
| UY38407A (es) | 2018-10-15 | 2020-05-29 | Novartis Ag | Anticuerpos estabilizadores de trem2 |
| EP3938400B1 (en) | 2019-03-11 | 2025-07-30 | Memorial Sloan Kettering Cancer Center | Cd22 antibodies and methods of using the same |
| CN113574072B (zh) | 2019-03-14 | 2023-12-12 | 莫佛塞斯公司 | 靶向C5aR的抗体 |
| TW202124446A (zh) | 2019-09-18 | 2021-07-01 | 瑞士商諾華公司 | 與ｅｎｔｐｄ２抗體之組合療法 |
| CR20230009A (es) | 2020-07-16 | 2023-01-25 | Novartis Ag | Anticuerpos anti-betacelulina, fragmentos de los mismos, y moléculas de unión multiespecíficas |
| CA3189473A1 (en) | 2020-09-24 | 2022-03-31 | Andreas Bultmann | Novel human antibodies binding to human cd3 epsilon |
| CN117425500A (zh) | 2021-01-13 | 2024-01-19 | 纪念斯隆凯特琳癌症中心 | 抗dll3抗体-药物缀合物 |
| EP4277664A1 (en) | 2021-01-13 | 2023-11-22 | Memorial Sloan Kettering Cancer Center | Antibody-pyrrolobenzodiazepine derivative conjugate |
| JPWO2023032955A1 (enExample) | 2021-08-31 | 2023-03-09 | ||
| CN118922448A (zh) | 2022-03-22 | 2024-11-08 | 莫佛塞斯公司 | Cd3特异性的去免疫抗体 |
| GB202204159D0 (en) | 2022-03-24 | 2022-05-11 | Heptares Therapeutics Ltd | Antibodies |
| WO2024236163A1 (en) | 2023-05-17 | 2024-11-21 | Morphosys Ag | T cell receptor beta constant region 2 (trbc2) antibodies |
| WO2025003511A1 (en) | 2023-06-30 | 2025-01-02 | Morphosys Ag | Dual-targeting of flt3 and cd123 co-expressing tumor cells by functional complementation of cycat® halfbody molecules |
| WO2025082777A1 (en) | 2023-10-17 | 2025-04-24 | Morphosys Ag | Dual-targeting of muc16 and mesothelin co-expressing tumor cells by functional complementation of cycat® halfbody molecules |
Family Cites Families (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE8203855D0 (sv) | 1982-06-21 | 1982-06-21 | Astra Laekemedel Ab | Novel derivatives of guanine i |
| ATE114723T1 (de) | 1987-03-02 | 1994-12-15 | Enzon Lab Inc | Organismus als träger für ''single chain antibody domain (scad)''. |
| EP0436597B1 (en) | 1988-09-02 | 1997-04-02 | Protein Engineering Corporation | Generation and selection of recombinant varied binding proteins |
| US5747334A (en) * | 1990-02-15 | 1998-05-05 | The University Of North Carolina At Chapel Hill | Random peptide library |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| US5723286A (en) | 1990-06-20 | 1998-03-03 | Affymax Technologies N.V. | Peptide library and screening systems |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5871974A (en) * | 1990-09-28 | 1999-02-16 | Ixsys Inc. | Surface expression libraries of heteromeric receptors |
| US5770434A (en) * | 1990-09-28 | 1998-06-23 | Ixsys Incorporated | Soluble peptides having constrained, secondary conformation in solution and method of making same |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| GB9114003D0 (en) * | 1991-06-28 | 1991-08-14 | Mastico Robert A | Chimaeric protein |
| GB9213601D0 (en) * | 1992-06-26 | 1992-08-12 | Mastico Robert A | Protein based delivery system |
| CA2115811A1 (en) * | 1993-02-17 | 1994-08-18 | Claus Krebber | A method for in vivo selection of ligand-binding proteins |
| GB9313509D0 (en) * | 1993-06-30 | 1993-08-11 | Medical Res Council | Chemisynthetic libraries |
| US6309642B1 (en) * | 1997-04-28 | 2001-10-30 | The Research And Development Institute, Inc. | Peptides which mimic candida carbohydrate epitopes and their use in a vaccine |
| US6341256B1 (en) * | 1995-03-31 | 2002-01-22 | Curagen Corporation | Consensus configurational bias Monte Carlo method and system for pharmacophore structure determination |
| ES2176484T3 (es) | 1995-08-18 | 2002-12-01 | Morphosys Ag | Bancos de proteinas/(poli)peptidos. |
| GB9608540D0 (en) * | 1996-04-25 | 1996-07-03 | Medical Res Council | Isolation of enzymes |
| JP2002501721A (ja) * | 1997-08-01 | 2002-01-22 | モルフォシス・アクチェンゲゼルシャフト | 多量体（ポリ）ペプチドコンプレックスのメンバーをコードする核酸配列を同定するための新規方法およびファージ |
| CA2328422A1 (en) | 1998-05-13 | 1999-11-18 | Diversys Limited | Selection system |
-
2000
- 2000-07-20 EP EP00945941A patent/EP1144607B1/en not_active Expired - Lifetime
- 2000-07-20 AU AU59864/00A patent/AU781396B2/en not_active Expired
- 2000-07-20 ES ES00945941T patent/ES2327382T3/es not_active Expired - Lifetime
- 2000-07-20 PT PT00945941T patent/PT1144607E/pt unknown
- 2000-07-20 IL IL14202500A patent/IL142025A0/xx unknown
- 2000-07-20 DE DE60041119T patent/DE60041119D1/de not_active Expired - Lifetime
- 2000-07-20 JP JP2001511164A patent/JP4312403B2/ja not_active Expired - Lifetime
- 2000-07-20 WO PCT/EP2000/006968 patent/WO2001005950A2/en not_active Ceased
- 2000-07-20 EP EP08153541A patent/EP1990409A3/en not_active Withdrawn
- 2000-07-20 AT AT00945941T patent/ATE417925T1/de active
- 2000-07-20 CA CA2347973A patent/CA2347973C/en not_active Expired - Lifetime
- 2000-07-20 DK DK00945941T patent/DK1144607T5/da active
-
2001
- 2001-03-14 IL IL142025A patent/IL142025A/en active IP Right Grant
- 2001-03-15 US US09/809,517 patent/US6753136B2/en not_active Expired - Lifetime
- 2001-03-19 NO NO20011386A patent/NO331199B1/no not_active IP Right Cessation
-
2003
- 2003-09-10 US US10/658,752 patent/US7785859B2/en not_active Expired - Fee Related
-
2007
- 2007-02-28 US US11/680,259 patent/US20070292947A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| NO20011386L (no) | 2001-05-18 |
| DE60041119D1 (de) | 2009-01-29 |
| IL142025A0 (en) | 2002-03-10 |
| IL142025A (en) | 2009-12-24 |
| EP1144607B1 (en) | 2008-12-17 |
| US6753136B2 (en) | 2004-06-22 |
| NO20011386D0 (no) | 2001-03-19 |
| EP1990409A3 (en) | 2011-05-18 |
| ES2327382T3 (es) | 2009-10-29 |
| AU5986400A (en) | 2001-02-05 |
| PT1144607E (pt) | 2009-04-22 |
| JP2003505025A (ja) | 2003-02-12 |
| EP1144607A2 (en) | 2001-10-17 |
| DK1144607T5 (da) | 2009-10-05 |
| DK1144607T3 (da) | 2009-08-24 |
| US20020034733A1 (en) | 2002-03-21 |
| NO331199B1 (no) | 2011-10-31 |
| ATE417925T1 (de) | 2009-01-15 |
| US7785859B2 (en) | 2010-08-31 |
| CA2347973C (en) | 2010-06-22 |
| EP1990409A2 (en) | 2008-11-12 |
| WO2001005950A3 (en) | 2001-08-02 |
| US20050058984A1 (en) | 2005-03-17 |
| WO2001005950A2 (en) | 2001-01-25 |
| AU781396B2 (en) | 2005-05-19 |
| US20070292947A1 (en) | 2007-12-20 |
| CA2347973A1 (en) | 2001-01-25 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4312403B2 (ja) | （ポリ）ペプチド／タンパク質を、ジスルフィド結合を介してバクテリオファージ粒子に表示させる新規方法 | |
| Carmen et al. | Concepts in antibody phage display | |
| AU2002345421B2 (en) | Chimaeric phages | |
| EP0527839A1 (en) | Recombinant library screening methods | |
| JP2002501721A (ja) | 多量体（ポリ）ペプチドコンプレックスのメンバーをコードする核酸配列を同定するための新規方法およびファージ | |
| KR100961392B1 (ko) | 항체 파지 표면제시 라이브러리 제조방법, 상기 방법에의해 제조된 항체 파지 표면제시 라이브러리, 상기 항체파지 표면제시 라이브러리 유전자를 포함한 파지미드 벡터 | |
| US8969253B2 (en) | Method for screening phage display libraries against each other | |
| JP6181626B2 (ja) | ジスルフィド結合形成のための改良された方法 | |
| CA2505849A1 (en) | Novel tricistronic vectors and uses therefor | |
| Vaccaro et al. | Efficient display of scFv antibodies on bacteriophage lambda | |
| KR100458083B1 (ko) | 파아지 디스플레이 라이브러리로부터 특정 이종 단백질의효율적인 분리를 위한 개선된 헬퍼 파아지 시스템 | |
| US8728982B2 (en) | Engineered hybrid phage vectors for the design and the generation of a human non-antibody peptide or protein phage library via fusion to pIX of M13 phage | |
| Wang et al. | Adapter-directed display: a modular design for shuttling display on phage surfaces | |
| US7070926B2 (en) | Chimaeric phages | |
| HK1145858A (en) | Improved methods for the formation of disulphide bonds | |
| Carmen et al. | in antibody phage display |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20060802 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20080805 |
|
| RD04 | Notification of resignation of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7424 Effective date: 20080815 |
|
| A871 | Explanation of circumstances concerning accelerated examination |
Free format text: JAPANESE INTERMEDIATE CODE: A871 Effective date: 20080805 |
|
| A975 | Report on accelerated examination |
Free format text: JAPANESE INTERMEDIATE CODE: A971005 Effective date: 20080908 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20080924 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20081222 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20090106 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20090123 |
|
| RD03 | Notification of appointment of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7423 Effective date: 20090126 |
|
| RD04 | Notification of resignation of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7424 Effective date: 20090126 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20090428 |
|
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20090513 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20120522 Year of fee payment: 3 |
|
| R150 | Certificate of patent or registration of utility model |
Free format text: JAPANESE INTERMEDIATE CODE: R150 Ref document number: 4312403 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20120522 Year of fee payment: 3 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20130522 Year of fee payment: 4 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| S531 | Written request for registration of change of domicile |
Free format text: JAPANESE INTERMEDIATE CODE: R313531 |
|
| S533 | Written request for registration of change of name |
Free format text: JAPANESE INTERMEDIATE CODE: R313533 |
|
| R350 | Written notification of registration of transfer |
Free format text: JAPANESE INTERMEDIATE CODE: R350 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| EXPY | Cancellation because of completion of term |