JP5754135B2 - 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 - Google Patents
関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 Download PDFInfo
- Publication number
- JP5754135B2 JP5754135B2 JP2010500980A JP2010500980A JP5754135B2 JP 5754135 B2 JP5754135 B2 JP 5754135B2 JP 2010500980 A JP2010500980 A JP 2010500980A JP 2010500980 A JP2010500980 A JP 2010500980A JP 5754135 B2 JP5754135 B2 JP 5754135B2
- Authority
- JP
- Japan
- Prior art keywords
- protein
- substrate
- cell
- interest
- polypeptide
- 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 - Fee Related
Links
- 108090000623 proteins and genes Proteins 0.000 title claims description 1006
- 102000004169 proteins and genes Human genes 0.000 title claims description 984
- 210000004027 cell Anatomy 0.000 title claims description 735
- 238000012216 screening Methods 0.000 title claims description 26
- 238000004519 manufacturing process Methods 0.000 title description 4
- 230000027455 binding Effects 0.000 claims description 494
- 239000000758 substrate Substances 0.000 claims description 288
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 260
- 238000000034 method Methods 0.000 claims description 224
- 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 claims description 197
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 140
- 229920001184 polypeptide Polymers 0.000 claims description 133
- 230000014509 gene expression Effects 0.000 claims description 118
- 229960002685 biotin Drugs 0.000 claims description 117
- 239000011616 biotin Substances 0.000 claims description 117
- 235000020958 biotin Nutrition 0.000 claims description 111
- 150000007523 nucleic acids Chemical class 0.000 claims description 95
- 108020004707 nucleic acids Proteins 0.000 claims description 93
- 102000039446 nucleic acids Human genes 0.000 claims description 93
- 239000000427 antigen Substances 0.000 claims description 56
- 108091007433 antigens Proteins 0.000 claims description 56
- 102000036639 antigens Human genes 0.000 claims description 56
- 210000002421 cell wall Anatomy 0.000 claims description 41
- 230000008569 process Effects 0.000 claims description 38
- 230000000694 effects Effects 0.000 claims description 36
- 230000028327 secretion Effects 0.000 claims description 35
- 230000001268 conjugating effect Effects 0.000 claims description 29
- 230000021615 conjugation Effects 0.000 claims description 27
- 108090000364 Ligases Proteins 0.000 claims description 22
- 102000003960 Ligases Human genes 0.000 claims description 22
- 101710167800 Capsid assembly scaffolding protein Proteins 0.000 claims description 20
- 101710130420 Probable capsid assembly scaffolding protein Proteins 0.000 claims description 20
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 20
- 230000003993 interaction Effects 0.000 claims description 20
- 230000003248 secreting effect Effects 0.000 claims description 20
- 101710204410 Scaffold protein Proteins 0.000 claims description 19
- 108010006519 Molecular Chaperones Proteins 0.000 claims description 15
- 238000012545 processing Methods 0.000 claims description 15
- 239000000592 Artificial Cell Substances 0.000 claims description 14
- 102000005431 Molecular Chaperones Human genes 0.000 claims description 14
- 239000012634 fragment Substances 0.000 claims description 14
- 210000005253 yeast cell Anatomy 0.000 claims description 14
- 230000003362 replicative effect Effects 0.000 claims description 13
- 238000011282 treatment Methods 0.000 claims description 13
- 230000003213 activating effect Effects 0.000 claims description 11
- 150000001875 compounds Chemical class 0.000 claims description 10
- 150000002632 lipids Chemical class 0.000 claims description 10
- 229920001282 polysaccharide Polymers 0.000 claims description 9
- 239000005017 polysaccharide Substances 0.000 claims description 9
- 229920001059 synthetic polymer Polymers 0.000 claims description 9
- 238000011156 evaluation Methods 0.000 claims description 8
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 6
- 230000003834 intracellular effect Effects 0.000 claims description 3
- 150000004676 glycans Chemical class 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 930
- 108090001008 Avidin Proteins 0.000 description 92
- 230000004048 modification Effects 0.000 description 82
- 238000012986 modification Methods 0.000 description 82
- 239000013598 vector Substances 0.000 description 76
- 102000004190 Enzymes Human genes 0.000 description 68
- 108090000790 Enzymes Proteins 0.000 description 68
- 229940088598 enzyme Drugs 0.000 description 68
- 230000006870 function Effects 0.000 description 48
- 108020001507 fusion proteins Proteins 0.000 description 43
- 102000037865 fusion proteins Human genes 0.000 description 43
- 102000018697 Membrane Proteins Human genes 0.000 description 31
- 108010052285 Membrane Proteins Proteins 0.000 description 31
- 235000001014 amino acid Nutrition 0.000 description 30
- 150000001413 amino acids Chemical class 0.000 description 30
- 238000001727 in vivo Methods 0.000 description 28
- 230000001939 inductive effect Effects 0.000 description 28
- 238000003556 assay Methods 0.000 description 26
- 239000003446 ligand Substances 0.000 description 26
- -1 polymerase Proteins 0.000 description 25
- 229930004094 glycosylphosphatidylinositol Natural products 0.000 description 23
- 238000004873 anchoring Methods 0.000 description 22
- 230000001965 increasing effect Effects 0.000 description 22
- 108010038196 saccharide-binding proteins Proteins 0.000 description 21
- 108050003866 Bifunctional ligase/repressor BirA Proteins 0.000 description 20
- 102100033743 Biotin-[acetyl-CoA-carboxylase] ligase Human genes 0.000 description 20
- 108010053098 biotin receptor Proteins 0.000 description 20
- 125000006850 spacer group Chemical group 0.000 description 20
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 18
- 230000006287 biotinylation Effects 0.000 description 17
- 238000007413 biotinylation Methods 0.000 description 17
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 16
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 16
- 230000001580 bacterial effect Effects 0.000 description 15
- 150000001720 carbohydrates Chemical class 0.000 description 15
- 238000005859 coupling reaction Methods 0.000 description 15
- 238000000338 in vitro Methods 0.000 description 15
- 125000003275 alpha amino acid group Chemical group 0.000 description 14
- 235000014633 carbohydrates Nutrition 0.000 description 14
- 230000008878 coupling Effects 0.000 description 14
- 238000010168 coupling process Methods 0.000 description 14
- 230000000670 limiting effect Effects 0.000 description 13
- 108020003175 receptors Proteins 0.000 description 13
- 102000005962 receptors Human genes 0.000 description 13
- 108010090804 Streptavidin Proteins 0.000 description 12
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 12
- 230000003100 immobilizing effect Effects 0.000 description 12
- 238000002372 labelling Methods 0.000 description 12
- 230000004853 protein function Effects 0.000 description 12
- 108091005804 Peptidases Proteins 0.000 description 11
- 210000004899 c-terminal region Anatomy 0.000 description 11
- 102000014914 Carrier Proteins Human genes 0.000 description 10
- 239000004365 Protease Substances 0.000 description 10
- 108700026226 TATA Box Proteins 0.000 description 10
- 108091008324 binding proteins Proteins 0.000 description 10
- 239000000203 mixture Substances 0.000 description 10
- 230000008859 change Effects 0.000 description 9
- 230000004927 fusion Effects 0.000 description 9
- 230000001976 improved effect Effects 0.000 description 9
- 239000000178 monomer Substances 0.000 description 9
- 108010087904 neutravidin Proteins 0.000 description 9
- 101100120289 Drosophila melanogaster Flo1 gene Proteins 0.000 description 8
- 239000003795 chemical substances by application Substances 0.000 description 8
- 230000006698 induction Effects 0.000 description 8
- 150000004804 polysaccharides Chemical class 0.000 description 8
- 238000002818 protein evolution Methods 0.000 description 8
- 241000588724 Escherichia coli Species 0.000 description 7
- 108091034117 Oligonucleotide Proteins 0.000 description 7
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 7
- 241000235343 Saccharomycetales Species 0.000 description 7
- 238000007792 addition Methods 0.000 description 7
- 230000008901 benefit Effects 0.000 description 7
- 210000000170 cell membrane Anatomy 0.000 description 7
- 239000000539 dimer Substances 0.000 description 7
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 7
- 230000007613 environmental effect Effects 0.000 description 7
- 210000004962 mammalian cell Anatomy 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 230000001105 regulatory effect Effects 0.000 description 7
- 235000000346 sugar Nutrition 0.000 description 7
- 230000001225 therapeutic effect Effects 0.000 description 7
- 108020004414 DNA Proteins 0.000 description 6
- 102000004856 Lectins Human genes 0.000 description 6
- 108090001090 Lectins Proteins 0.000 description 6
- 230000003197 catalytic effect Effects 0.000 description 6
- 239000002523 lectin Substances 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- 239000002773 nucleotide Substances 0.000 description 6
- 125000003729 nucleotide group Chemical group 0.000 description 6
- 230000002829 reductive effect Effects 0.000 description 6
- 229920002498 Beta-glucan Polymers 0.000 description 5
- 102000007474 Multiprotein Complexes Human genes 0.000 description 5
- 108010085220 Multiprotein Complexes Proteins 0.000 description 5
- 150000001412 amines Chemical class 0.000 description 5
- 125000000539 amino acid group Chemical group 0.000 description 5
- 108091006004 biotinylated proteins Proteins 0.000 description 5
- 238000004113 cell culture Methods 0.000 description 5
- 230000032823 cell division Effects 0.000 description 5
- 229920002678 cellulose Polymers 0.000 description 5
- 239000001913 cellulose Substances 0.000 description 5
- 230000000415 inactivating effect Effects 0.000 description 5
- 230000002503 metabolic effect Effects 0.000 description 5
- 230000035772 mutation Effects 0.000 description 5
- 230000011664 signaling Effects 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 101710204899 Alpha-agglutinin Proteins 0.000 description 4
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 4
- 108091028043 Nucleic acid sequence Proteins 0.000 description 4
- 102000035195 Peptidases Human genes 0.000 description 4
- 108700019535 Phosphoprotein Phosphatases Proteins 0.000 description 4
- 102000045595 Phosphoprotein Phosphatases Human genes 0.000 description 4
- 102000001253 Protein Kinase Human genes 0.000 description 4
- 101710183280 Topoisomerase Proteins 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 102000025171 antigen binding proteins Human genes 0.000 description 4
- 108091000831 antigen binding proteins Proteins 0.000 description 4
- 101150117627 bpl1 gene Proteins 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 238000010494 dissociation reaction Methods 0.000 description 4
- 230000005593 dissociations Effects 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 239000013604 expression vector Substances 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 229920001223 polyethylene glycol Polymers 0.000 description 4
- 108060006633 protein kinase Proteins 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 3
- 229920002101 Chitin Polymers 0.000 description 3
- 108010062580 Concanavalin A Proteins 0.000 description 3
- 108090000695 Cytokines Proteins 0.000 description 3
- 102000004127 Cytokines Human genes 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 3
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 3
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 3
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 3
- 108090001030 Lipoproteins Proteins 0.000 description 3
- 102000004895 Lipoproteins Human genes 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- KYRVNWMVYQXFEU-UHFFFAOYSA-N Nocodazole Chemical compound C1=C2NC(NC(=O)OC)=NC2=CC=C1C(=O)C1=CC=CS1 KYRVNWMVYQXFEU-UHFFFAOYSA-N 0.000 description 3
- 108010047620 Phytohemagglutinins Proteins 0.000 description 3
- 239000002202 Polyethylene glycol Substances 0.000 description 3
- 102000019197 Superoxide Dismutase Human genes 0.000 description 3
- 108010012715 Superoxide dismutase Proteins 0.000 description 3
- 102000050760 Vitamin D-binding protein Human genes 0.000 description 3
- 101710179590 Vitamin D-binding protein Proteins 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
- 239000000910 agglutinin Substances 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 108091008400 carbohydrate binding proteins Proteins 0.000 description 3
- 102000023852 carbohydrate binding proteins Human genes 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 230000003196 chaotropic effect Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 210000004748 cultured cell Anatomy 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 230000009088 enzymatic function Effects 0.000 description 3
- 230000009144 enzymatic modification Effects 0.000 description 3
- 238000001952 enzyme assay Methods 0.000 description 3
- 108091006047 fluorescent proteins Proteins 0.000 description 3
- 102000034287 fluorescent proteins Human genes 0.000 description 3
- 238000002825 functional assay Methods 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 239000005090 green fluorescent protein Substances 0.000 description 3
- 239000003262 industrial enzyme Substances 0.000 description 3
- 238000003780 insertion Methods 0.000 description 3
- 230000037431 insertion Effects 0.000 description 3
- 230000002452 interceptive effect Effects 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 229950006344 nocodazole Drugs 0.000 description 3
- 230000001885 phytohemagglutinin Effects 0.000 description 3
- 230000001323 posttranslational effect Effects 0.000 description 3
- 230000012846 protein folding Effects 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 238000005215 recombination Methods 0.000 description 3
- 238000012552 review Methods 0.000 description 3
- 230000009870 specific binding Effects 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- 230000032258 transport Effects 0.000 description 3
- VHYRHFNOWKMCHQ-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 4-formylbenzoate Chemical compound C1=CC(C=O)=CC=C1C(=O)ON1C(=O)CCC1=O VHYRHFNOWKMCHQ-UHFFFAOYSA-N 0.000 description 2
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Natural products CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- 108010039627 Aprotinin Proteins 0.000 description 2
- 108010018763 Biotin carboxylase Proteins 0.000 description 2
- 102000008203 CTLA-4 Antigen Human genes 0.000 description 2
- 108010021064 CTLA-4 Antigen Proteins 0.000 description 2
- 241000282836 Camelus dromedarius Species 0.000 description 2
- 101100083069 Candida albicans (strain SC5314 / ATCC MYA-2876) PGA62 gene Proteins 0.000 description 2
- 101100106993 Candida albicans (strain SC5314 / ATCC MYA-2876) YWP1 gene Proteins 0.000 description 2
- 101100056797 Canis lupus familiaris SAG gene Proteins 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- 108010078791 Carrier Proteins Proteins 0.000 description 2
- 230000033616 DNA repair Effects 0.000 description 2
- 108700022150 Designed Ankyrin Repeat Proteins Proteins 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 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 2
- 108010020195 FLAG peptide Proteins 0.000 description 2
- 101150054379 FLO1 gene Proteins 0.000 description 2
- 101150094690 GAL1 gene Proteins 0.000 description 2
- 102100028501 Galanin peptides Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 101150105462 HIS6 gene Proteins 0.000 description 2
- 102100024023 Histone PARylation factor 1 Human genes 0.000 description 2
- 101100121078 Homo sapiens GAL gene Proteins 0.000 description 2
- 101001077660 Homo sapiens Serine protease inhibitor Kazal-type 1 Proteins 0.000 description 2
- 108091006905 Human Serum Albumin Proteins 0.000 description 2
- 102000008100 Human Serum Albumin Human genes 0.000 description 2
- 101001082397 Human adenovirus B serotype 3 Hexon-associated protein Proteins 0.000 description 2
- 108010058683 Immobilized Proteins Proteins 0.000 description 2
- 108010006444 Leucine-Rich Repeat Proteins Proteins 0.000 description 2
- 102000009112 Mannose-Binding Lectin Human genes 0.000 description 2
- 108010087870 Mannose-Binding Lectin Proteins 0.000 description 2
- MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 description 2
- 101100395023 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) his-7 gene Proteins 0.000 description 2
- 108010013639 Peptidoglycan Proteins 0.000 description 2
- 102100024952 Protein CBFA2T1 Human genes 0.000 description 2
- 101001120093 Pseudoalteromonas phage PM2 Protein P8 Proteins 0.000 description 2
- 101100532512 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) SAG1 gene Proteins 0.000 description 2
- 108091008874 T cell receptors Proteins 0.000 description 2
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 150000001299 aldehydes Chemical class 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 108010048079 amyloid beta-protein precursor inhibitor Proteins 0.000 description 2
- 239000011230 binding agent Substances 0.000 description 2
- 102000043871 biotin binding protein Human genes 0.000 description 2
- 108700021042 biotin binding protein Proteins 0.000 description 2
- 150000001615 biotins Chemical class 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 239000005515 coenzyme Substances 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000009792 diffusion process Methods 0.000 description 2
- 230000008034 disappearance Effects 0.000 description 2
- 150000002148 esters Chemical group 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 210000002288 golgi apparatus Anatomy 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 239000000710 homodimer Substances 0.000 description 2
- 102000057815 human SPINK1 Human genes 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000003999 initiator Substances 0.000 description 2
- 230000000977 initiatory effect Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 210000004901 leucine-rich repeat Anatomy 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000007898 magnetic cell sorting Methods 0.000 description 2
- 210000004897 n-terminal region Anatomy 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 230000002018 overexpression Effects 0.000 description 2
- KHIWWQKSHDUIBK-UHFFFAOYSA-N periodic acid Chemical compound OI(=O)(=O)=O KHIWWQKSHDUIBK-UHFFFAOYSA-N 0.000 description 2
- 238000002823 phage display Methods 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 108091033319 polynucleotide Proteins 0.000 description 2
- 102000040430 polynucleotide Human genes 0.000 description 2
- 239000002157 polynucleotide Substances 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 230000019491 signal transduction Effects 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 235000019731 tricalcium phosphate Nutrition 0.000 description 2
- 108091005957 yellow fluorescent proteins Proteins 0.000 description 2
- 229910052725 zinc Inorganic materials 0.000 description 2
- 239000011701 zinc Substances 0.000 description 2
- CRDAMVZIKSXKFV-FBXUGWQNSA-N (2-cis,6-cis)-farnesol Chemical compound CC(C)=CCC\C(C)=C/CC\C(C)=C/CO CRDAMVZIKSXKFV-FBXUGWQNSA-N 0.000 description 1
- 239000000260 (2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ol Substances 0.000 description 1
- 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 compound 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 1
- YCZTUBHUGXHSKE-VVCAKUBGSA-N 1-[5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoyloxy]-2,5-dioxopyrrolidine-3-sulfonic acid Chemical compound O=C1C(S(=O)(=O)O)CC(=O)N1OC(=O)CCCC[C@H]1[C@H]2NC(=O)N[C@H]2CS1 YCZTUBHUGXHSKE-VVCAKUBGSA-N 0.000 description 1
- VSNHCAURESNICA-NJFSPNSNSA-N 1-oxidanylurea Chemical compound N[14C](=O)NO VSNHCAURESNICA-NJFSPNSNSA-N 0.000 description 1
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 1
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 1
- 102100038222 60 kDa heat shock protein, mitochondrial Human genes 0.000 description 1
- 101710186708 Agglutinin Proteins 0.000 description 1
- 102000006306 Antigen Receptors Human genes 0.000 description 1
- 108010083359 Antigen Receptors Proteins 0.000 description 1
- 101100107610 Arabidopsis thaliana ABCF4 gene Proteins 0.000 description 1
- 108010014223 Armadillo Domain Proteins Proteins 0.000 description 1
- 102000016904 Armadillo Domain Proteins Human genes 0.000 description 1
- 108020000946 Bacterial DNA Proteins 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- SPNJNGBLQSTLMI-UHFFFAOYSA-N CC(C)=NN.NNC1=CC=NC=C1C(=O)ON1C(=O)CCC1=O Chemical compound CC(C)=NN.NNC1=CC=NC=C1C(=O)ON1C(=O)CCC1=O SPNJNGBLQSTLMI-UHFFFAOYSA-N 0.000 description 1
- 101150089473 CWP1 gene Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 102100029968 Calreticulin Human genes 0.000 description 1
- 108090000549 Calreticulin Proteins 0.000 description 1
- 101100464175 Candida albicans (strain SC5314 / ATCC MYA-2876) PIR32 gene Proteins 0.000 description 1
- 101100166585 Candida albicans (strain SC5314 / ATCC MYA-2876) SSR1 gene Proteins 0.000 description 1
- 108090000489 Carboxy-Lyases Proteins 0.000 description 1
- 101710163595 Chaperone protein DnaK Proteins 0.000 description 1
- 108010058432 Chaperonin 60 Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 108010069514 Cyclic Peptides Proteins 0.000 description 1
- 102000001189 Cyclic Peptides Human genes 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 102000004594 DNA Polymerase I Human genes 0.000 description 1
- 108010017826 DNA Polymerase I Proteins 0.000 description 1
- 238000007702 DNA assembly Methods 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 101100013145 Drosophila melanogaster Flo2 gene Proteins 0.000 description 1
- 241000218991 Ecballium Species 0.000 description 1
- 101710194146 Ecotin Proteins 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 102100031857 Endoplasmic reticulum resident protein 29 Human genes 0.000 description 1
- 101710113964 Endoplasmic reticulum resident protein 29 Proteins 0.000 description 1
- 102100039328 Endoplasmin Human genes 0.000 description 1
- 102000002090 Fibronectin type III Human genes 0.000 description 1
- 108050009401 Fibronectin type III Proteins 0.000 description 1
- 241000724791 Filamentous phage Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- 229920001503 Glucan Polymers 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 1
- 101710178376 Heat shock 70 kDa protein Proteins 0.000 description 1
- 101710152018 Heat shock cognate 70 kDa protein Proteins 0.000 description 1
- 101710113864 Heat shock protein 90 Proteins 0.000 description 1
- 102100034051 Heat shock protein HSP 90-alpha Human genes 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 102000009331 Homeodomain Proteins Human genes 0.000 description 1
- 108010048671 Homeodomain Proteins Proteins 0.000 description 1
- 101000889990 Homo sapiens Apolipoprotein(a) Proteins 0.000 description 1
- 101001047783 Homo sapiens Histone PARylation factor 1 Proteins 0.000 description 1
- 101001006892 Homo sapiens Krueppel-like factor 10 Proteins 0.000 description 1
- 101001121408 Homo sapiens L-amino-acid oxidase Proteins 0.000 description 1
- 101000881131 Homo sapiens RNA/RNP complex-1-interacting phosphatase Proteins 0.000 description 1
- 101000836383 Homo sapiens Serpin H1 Proteins 0.000 description 1
- 101000687855 Homo sapiens Suppressor of cytokine signaling 3 Proteins 0.000 description 1
- 101000956004 Homo sapiens Vitamin D-binding protein Proteins 0.000 description 1
- 101710146024 Horcolin Proteins 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 102100020755 Hypoxia up-regulated protein 1 Human genes 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 1
- 241000588747 Klebsiella pneumoniae Species 0.000 description 1
- 102100027798 Krueppel-like factor 10 Human genes 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical group SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- 102100026388 L-amino-acid oxidase Human genes 0.000 description 1
- WZNJWVWKTVETCG-YFKPBYRVSA-N L-mimosine Chemical compound OC(=O)[C@@H](N)CN1C=CC(=O)C(O)=C1 WZNJWVWKTVETCG-YFKPBYRVSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 235000019687 Lamb Nutrition 0.000 description 1
- 101710189395 Lectin Proteins 0.000 description 1
- WHXSMMKQMYFTQS-UHFFFAOYSA-N Lithium Chemical compound [Li] WHXSMMKQMYFTQS-UHFFFAOYSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 229920000057 Mannan Polymers 0.000 description 1
- 101710179758 Mannose-specific lectin Proteins 0.000 description 1
- 101710150763 Mannose-specific lectin 1 Proteins 0.000 description 1
- 101710150745 Mannose-specific lectin 2 Proteins 0.000 description 1
- 108010038049 Mating Factor Proteins 0.000 description 1
- 101710089743 Mating factor alpha Proteins 0.000 description 1
- 108010027796 Membrane Fusion Proteins Proteins 0.000 description 1
- 102000018897 Membrane Fusion Proteins Human genes 0.000 description 1
- 108010059724 Micrococcal Nuclease Proteins 0.000 description 1
- 102000002151 Microfilament Proteins Human genes 0.000 description 1
- 108010040897 Microfilament Proteins Proteins 0.000 description 1
- PCZOHLXUXFIOCF-UHFFFAOYSA-N Monacolin X Natural products C12C(OC(=O)C(C)CC)CC(C)C=C2C=CC(C)C1CCC1CC(O)CC(=O)O1 PCZOHLXUXFIOCF-UHFFFAOYSA-N 0.000 description 1
- 101100018717 Mus musculus Il1rl1 gene Proteins 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 1
- 101710204212 Neocarzinostatin Proteins 0.000 description 1
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 1
- 108700028353 OmpC Proteins 0.000 description 1
- 101100043636 Oryza sativa subsp. japonica SSIIIA gene Proteins 0.000 description 1
- 101710116435 Outer membrane protein Proteins 0.000 description 1
- 102000000470 PDZ domains Human genes 0.000 description 1
- 108050008994 PDZ domains Proteins 0.000 description 1
- 101150045321 PIR3 gene Proteins 0.000 description 1
- 108010066305 Parkinson Disease Associated Proteins Proteins 0.000 description 1
- 102000018315 Parkinson Disease Associated Proteins Human genes 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 241000235648 Pichia Species 0.000 description 1
- 102100037097 Protein disulfide-isomerase A3 Human genes 0.000 description 1
- 101710106224 Protein disulfide-isomerase A3 Proteins 0.000 description 1
- 108010067787 Proteoglycans Proteins 0.000 description 1
- 102000016611 Proteoglycans Human genes 0.000 description 1
- 102100037566 RNA/RNP complex-1-interacting phosphatase Human genes 0.000 description 1
- 101150006985 STE2 gene Proteins 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 101100001141 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) AGA1 gene Proteins 0.000 description 1
- 101100165358 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) BIO5 gene Proteins 0.000 description 1
- 101100166586 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) CCW14 gene Proteins 0.000 description 1
- 101100008072 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) CWP2 gene Proteins 0.000 description 1
- 101100012902 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) FIG2 gene Proteins 0.000 description 1
- 101100066911 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) FLO5 gene Proteins 0.000 description 1
- 101100068078 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GCN4 gene Proteins 0.000 description 1
- 101100204213 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) STE3 gene Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 102100027287 Serpin H1 Human genes 0.000 description 1
- 101100111651 Serratia marcescens smeA gene Proteins 0.000 description 1
- 108700018543 Sinapis alba MTI2 Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 101800001707 Spacer peptide Proteins 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 241000186983 Streptomyces avidinii Species 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 102100024283 Suppressor of cytokine signaling 3 Human genes 0.000 description 1
- 102100024554 Tetranectin Human genes 0.000 description 1
- 102100036407 Thioredoxin Human genes 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 101710112927 Trypsin inhibitor 2 Proteins 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 229930003316 Vitamin D Natural products 0.000 description 1
- QYSXJUFSXHHAJI-XFEUOLMDSA-N Vitamin D3 Natural products C1(/[C@@H]2CC[C@@H]([C@]2(CCC1)C)[C@H](C)CCCC(C)C)=C/C=C1\C[C@@H](O)CCC1=C QYSXJUFSXHHAJI-XFEUOLMDSA-N 0.000 description 1
- 241000269370 Xenopus <genus> Species 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000002730 additional effect Effects 0.000 description 1
- 238000012382 advanced drug delivery Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 150000001335 aliphatic alkanes Chemical class 0.000 description 1
- 125000000088 alpha-mannosyl group Chemical group C1([C@@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- NOFOAYPPHIUXJR-APNQCZIXSA-N aphidicolin Chemical compound C1[C@@]23[C@@]4(C)CC[C@@H](O)[C@@](C)(CO)[C@@H]4CC[C@H]3C[C@H]1[C@](CO)(O)CC2 NOFOAYPPHIUXJR-APNQCZIXSA-N 0.000 description 1
- SEKZNWAQALMJNH-YZUCACDQSA-N aphidicolin Natural products C[C@]1(CO)CC[C@]23C[C@H]1C[C@@H]2CC[C@H]4[C@](C)(CO)[C@H](O)CC[C@]34C SEKZNWAQALMJNH-YZUCACDQSA-N 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 238000002819 bacterial display Methods 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 108010002833 beta-lactamase TEM-1 Proteins 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 239000003130 blood coagulation factor inhibitor Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 125000000837 carbohydrate group Chemical group 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000022131 cell cycle Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- 108010081370 chymotrypsin inhibitor 2 Proteins 0.000 description 1
- 238000002983 circular dichroism Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000010924 continuous production Methods 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 108010014507 erythroagglutinating phytohemagglutinin Proteins 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 229940043259 farnesol Drugs 0.000 description 1
- 229930002886 farnesol Natural products 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 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 1
- 238000012921 fluorescence analysis Methods 0.000 description 1
- 108010021843 fluorescent protein 583 Proteins 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 230000004110 gluconeogenesis Effects 0.000 description 1
- 108010008714 glucose-regulated protein 170 Proteins 0.000 description 1
- 108010017007 glucose-regulated proteins Proteins 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 229960000789 guanidine hydrochloride Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 239000000833 heterodimer Substances 0.000 description 1
- 238000012203 high throughput assay Methods 0.000 description 1
- 102000051433 human GC Human genes 0.000 description 1
- 102000045903 human LPA Human genes 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000002637 immunotoxin Effects 0.000 description 1
- 239000002596 immunotoxin Substances 0.000 description 1
- 231100000608 immunotoxin Toxicity 0.000 description 1
- 229940051026 immunotoxin Drugs 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 108010078480 insect defensin A Proteins 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- WZNJWVWKTVETCG-UHFFFAOYSA-N kojic acid Natural products OC(=O)C(N)CN1C=CC(=O)C(O)=C1 WZNJWVWKTVETCG-UHFFFAOYSA-N 0.000 description 1
- 230000000503 lectinlike effect Effects 0.000 description 1
- VHOGYURTWQBHIL-UHFFFAOYSA-N leflunomide Chemical compound O1N=CC(C(=O)NC=2C=CC(=CC=2)C(F)(F)F)=C1C VHOGYURTWQBHIL-UHFFFAOYSA-N 0.000 description 1
- 229960000681 leflunomide Drugs 0.000 description 1
- 108020001756 ligand binding domains Proteins 0.000 description 1
- 230000004132 lipogenesis Effects 0.000 description 1
- 229910052744 lithium Inorganic materials 0.000 description 1
- 229960001078 lithium Drugs 0.000 description 1
- PCZOHLXUXFIOCF-BXMDZJJMSA-N lovastatin Chemical compound C([C@H]1[C@@H](C)C=CC2=C[C@H](C)C[C@@H]([C@H]12)OC(=O)[C@@H](C)CC)C[C@@H]1C[C@@H](O)CC(=O)O1 PCZOHLXUXFIOCF-BXMDZJJMSA-N 0.000 description 1
- 229960004844 lovastatin Drugs 0.000 description 1
- QLJODMDSTUBWDW-UHFFFAOYSA-N lovastatin hydroxy acid Natural products C1=CC(C)C(CCC(O)CC(O)CC(O)=O)C2C(OC(=O)C(C)CC)CC(C)C=C21 QLJODMDSTUBWDW-UHFFFAOYSA-N 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000002824 mRNA display Methods 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 108010005335 mannoproteins Proteins 0.000 description 1
- 125000000311 mannosyl group Chemical group C1([C@@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 230000008172 membrane trafficking Effects 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 229950002289 mimosine Drugs 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 230000009149 molecular binding Effects 0.000 description 1
- QZGIWPZCWHMVQL-UIYAJPBUSA-N neocarzinostatin chromophore Chemical compound O1[C@H](C)[C@H](O)[C@H](O)[C@@H](NC)[C@H]1O[C@@H]1C/2=C/C#C[C@H]3O[C@@]3([C@@H]3OC(=O)OC3)C#CC\2=C[C@H]1OC(=O)C1=C(O)C=CC2=C(C)C=C(OC)C=C12 QZGIWPZCWHMVQL-UIYAJPBUSA-N 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000031787 nutrient reservoir activity Effects 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 238000006384 oligomerization reaction Methods 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 239000013110 organic ligand Substances 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 108700041181 parathymosin alpha Proteins 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000003672 processing method Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 230000003946 protein process Effects 0.000 description 1
- 230000020978 protein processing Effects 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000014493 regulation of gene expression Effects 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000002702 ribosome display Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000000646 scanning calorimetry Methods 0.000 description 1
- 230000002000 scavenging effect Effects 0.000 description 1
- 239000002795 scorpion venom Substances 0.000 description 1
- 238000007423 screening assay Methods 0.000 description 1
- 210000002955 secretory cell Anatomy 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 229950001790 tendamistat Drugs 0.000 description 1
- 108010037401 tendamistate Proteins 0.000 description 1
- GFKSKVCFBACPGK-UHFFFAOYSA-N terephthalic acid;hydrochloride Chemical compound Cl.OC(=O)C1=CC=C(C(O)=O)C=C1 GFKSKVCFBACPGK-UHFFFAOYSA-N 0.000 description 1
- 108010013645 tetranectin Proteins 0.000 description 1
- 150000003573 thiols Chemical class 0.000 description 1
- 108060008226 thioredoxin Proteins 0.000 description 1
- 229940094937 thioredoxin Drugs 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- CRDAMVZIKSXKFV-UHFFFAOYSA-N trans-Farnesol Natural products CC(C)=CCCC(C)=CCCC(C)=CCO CRDAMVZIKSXKFV-UHFFFAOYSA-N 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 108091005703 transmembrane proteins Proteins 0.000 description 1
- 102000035160 transmembrane proteins Human genes 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 238000010798 ubiquitination Methods 0.000 description 1
- 230000034512 ubiquitination Effects 0.000 description 1
- 230000007332 vesicle formation Effects 0.000 description 1
- 235000019166 vitamin D Nutrition 0.000 description 1
- 239000011710 vitamin D Substances 0.000 description 1
- 150000003710 vitamin D derivatives Chemical class 0.000 description 1
- 229940046008 vitamin d Drugs 0.000 description 1
- 229920001221 xylan Polymers 0.000 description 1
- 150000004823 xylans Chemical class 0.000 description 1
- 229950009268 zinostatin Drugs 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/566—Immunoassay; Biospecific binding assay; Materials therefor using specific carrier or receptor proteins as ligand binding reagents where possible specific carrier or receptor proteins are classified with their target compounds
-
- 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
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B10/00—Directed molecular evolution of macromolecules, e.g. RNA, DNA or proteins
-
- 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
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B40/00—Libraries per se, e.g. arrays, mixtures
- C40B40/04—Libraries containing only organic compounds
- C40B40/06—Libraries containing nucleotides or polynucleotides, or derivatives thereof
- C40B40/08—Libraries containing RNA or DNA which encodes proteins, e.g. gene libraries
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/035—Fusion polypeptide containing a localisation/targetting motif containing a signal for targeting to the external surface of a cell, e.g. to the outer membrane of Gram negative bacteria, GPI- anchored eukaryote proteins
-
- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B30/00—Methods of screening libraries
- C40B30/04—Methods of screening libraries by measuring the ability to specifically bind a target molecule, e.g. antibody-antigen binding, receptor-ligand binding
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/705—Assays involving receptors, cell surface antigens or cell surface determinants
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Immunology (AREA)
- Physics & Mathematics (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Biophysics (AREA)
- Virology (AREA)
- Plant Pathology (AREA)
- Crystallography & Structural Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Food Science & Technology (AREA)
- Analytical Chemistry (AREA)
- Cell Biology (AREA)
- Pathology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (9)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US92037807P | 2007-03-26 | 2007-03-26 | |
| US92037507P | 2007-03-26 | 2007-03-26 | |
| US60/920,375 | 2007-03-26 | ||
| US60/920,378 | 2007-03-26 | ||
| US95971907P | 2007-07-16 | 2007-07-16 | |
| US60/959,719 | 2007-07-16 | ||
| US484107P | 2007-12-01 | 2007-12-01 | |
| US61/004,841 | 2007-12-01 | ||
| PCT/US2008/003978 WO2008118476A2 (en) | 2007-03-26 | 2008-03-26 | Cell surface display, screening and production of proteins of interest |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2013170132A Division JP2013233157A (ja) | 2007-03-26 | 2013-08-20 | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2010522561A JP2010522561A (ja) | 2010-07-08 |
| JP2010522561A5 JP2010522561A5 (enExample) | 2012-05-10 |
| JP5754135B2 true JP5754135B2 (ja) | 2015-07-29 |
Family
ID=39709282
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2010500980A Expired - Fee Related JP5754135B2 (ja) | 2007-03-26 | 2008-03-26 | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
| JP2013170132A Withdrawn JP2013233157A (ja) | 2007-03-26 | 2013-08-20 | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2013170132A Withdrawn JP2013233157A (ja) | 2007-03-26 | 2013-08-20 | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
Country Status (4)
| Country | Link |
|---|---|
| US (4) | US8709980B2 (enExample) |
| EP (2) | EP2137308B1 (enExample) |
| JP (2) | JP5754135B2 (enExample) |
| WO (1) | WO2008118476A2 (enExample) |
Families Citing this family (36)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP5754135B2 (ja) | 2007-03-26 | 2015-07-29 | アジェナス インコーポレイテッド | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
| ES2475973T3 (es) * | 2008-06-27 | 2014-07-11 | Sapphire Energy, Inc. | Inducción de la floculaci�n en organismos fotosint�ticos |
| US8067339B2 (en) | 2008-07-09 | 2011-11-29 | Merck Sharp & Dohme Corp. | Surface display of whole antibodies in eukaryotes |
| WO2010069913A1 (en) | 2008-12-16 | 2010-06-24 | Novartis Ag | Yeast display systems |
| WO2010129541A1 (en) * | 2009-05-04 | 2010-11-11 | Affomix Corporation | Emulsion selection of antibodies |
| WO2010129485A2 (en) * | 2009-05-04 | 2010-11-11 | San Diego State University Foundation | Compositions and methods for identifying enzyme and transport protein inhibitors |
| BR122015012748A2 (pt) * | 2009-07-17 | 2020-01-07 | Bioatla, Llc | Métodos de evolução, identificação e produção de uma proteína |
| WO2011075761A1 (en) | 2009-12-23 | 2011-06-30 | Affinity Biosciences Pty Ltd | Protein display |
| US9169312B2 (en) | 2010-09-21 | 2015-10-27 | San Diego State University Research Foundation | Compositions and methods for identifying enzyme and transport protein inhibitors |
| IL210093A0 (en) * | 2010-12-19 | 2011-06-30 | David Helman | Membrane bound reporter molecules and their use in cell sorting |
| DE102010056289A1 (de) | 2010-12-24 | 2012-06-28 | Geneart Ag | Verfahren zur Herstellung von Leseraster-korrekten Fragment-Bibliotheken |
| CA2840650C (en) | 2011-06-29 | 2019-08-20 | Affinity Biosciences Pty Ltd | Method of protein display |
| WO2013020087A2 (en) * | 2011-08-03 | 2013-02-07 | Texas Biomedical Research Insitute | Nucleic acid compositions, methods and kits for rapid pairing of affinity agents |
| US20140342932A1 (en) * | 2011-09-23 | 2014-11-20 | Merck Sharp & Dohme Corp. | Functional cell surface display of ligands for the insulin and/or insulin growth factor 1 receptor and applications thereof |
| CA2865033C (en) | 2012-02-23 | 2021-11-02 | Stage Cell Therapeutics Gmbh | Chromatographic isolation of cells and other complex biological materials |
| US20150322479A1 (en) * | 2012-06-20 | 2015-11-12 | Cytospan Technologies Corporation | Apparatus and method for quantification of replicative lifespan and observation of senescene |
| US10544449B2 (en) | 2013-06-14 | 2020-01-28 | Pacific Biosciences Of California, Inc. | Bis-biotinylation tags |
| EP3008094B1 (en) * | 2013-06-14 | 2018-12-26 | Pacific Biosciences Of California, Inc. | Bis-biotinylation tags |
| CN105873946A (zh) | 2013-10-17 | 2016-08-17 | 阿尔萨尼斯生物科学有限责任公司 | 交叉反应性金黄色葡萄球菌抗体序列 |
| JP6814634B2 (ja) | 2014-02-05 | 2021-01-20 | モレキュラー テンプレーツ, インク.Molecular Templates, Inc. | リボ毒性の一時的な減少に基づき、細胞毒性組換えポリペプチドをスクリーニングし、選択し、同定する方法 |
| CN116656605A (zh) * | 2014-04-16 | 2023-08-29 | 朱诺治疗有限公司 | 用于扩增细胞群的方法、试剂盒及装置 |
| GB201410262D0 (en) * | 2014-06-10 | 2014-07-23 | Cambridge Entpr Ltd | Novel method |
| TWI695011B (zh) | 2014-06-18 | 2020-06-01 | 美商梅爾莎納醫療公司 | 抗her2表位之單株抗體及其使用之方法 |
| WO2016066260A1 (en) | 2014-10-28 | 2016-05-06 | Merck Patent Gmbh | Methods for non-covalent fc-domain-containing protein display on the surface of cells and methods of screening thereof |
| US20180179267A1 (en) | 2015-04-17 | 2018-06-28 | Arsanis Biosciences Gmbh | Anti-staphylococcus aureus antibody combination preparation |
| MA45489A (fr) | 2015-10-22 | 2018-08-29 | Juno Therapeutics Gmbh | Procédés de culture de cellules, kits et appareil associés |
| MA45488A (fr) | 2015-10-22 | 2018-08-29 | Juno Therapeutics Gmbh | Procédés, kits et appareil de culture de cellules |
| AU2016341527B2 (en) | 2015-10-22 | 2023-04-27 | Juno Therapeutics Gmbh | Methods, kits, agents and apparatuses for transduction |
| AU2016347051A1 (en) * | 2015-10-26 | 2018-05-24 | Buckman Laboratories International, Inc. | Lignocellulose polymer probes and methods |
| US10947317B2 (en) | 2016-03-15 | 2021-03-16 | Mersana Therapeutics, Inc. | NaPi2b-targeted antibody-drug conjugates and methods of use thereof |
| WO2018041740A1 (en) | 2016-09-01 | 2018-03-08 | Bayer Pharma Aktiengesellschaft | Non-covalent display system using fimgt/dsf |
| GB201704115D0 (en) * | 2017-03-15 | 2017-04-26 | Oxford Genetics Ltd | Method of selecting for antibodies |
| EP4647493A2 (en) | 2017-04-27 | 2025-11-12 | Juno Therapeutics, Inc. | Oligomeric particle reagents and methods of use thereof |
| WO2018213242A1 (en) * | 2017-05-15 | 2018-11-22 | University Of Maryland, Baltimore | Live salmonella typhi vectors engineered to express heterologous outer membrane protein antigens and methods of use thereof |
| CN117015710A (zh) * | 2021-03-10 | 2023-11-07 | 索尼集团公司 | 生物粒子分析方法及用于生物粒子分析的试剂盒 |
| WO2023051972A1 (en) | 2021-09-29 | 2023-04-06 | Miltenyi Biotec B.V. & Co. KG | Method for the generation and selection of a producer cell |
Family Cites Families (40)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US5252466A (en) | 1989-05-19 | 1993-10-12 | Biotechnology Research And Development Corporation | Fusion proteins having a site for in vivo post-translation modification and methods of making and purifying them |
| US5747334A (en) | 1990-02-15 | 1998-05-05 | The University Of North Carolina At Chapel Hill | Random peptide library |
| AU8740491A (en) | 1990-09-28 | 1992-04-28 | Protein Engineering Corporation | Proteinaceous anti-dental plaque agents |
| US20030036092A1 (en) | 1991-11-15 | 2003-02-20 | Board Of Regents, The University Of Texas System | Directed evolution of enzymes and antibodies |
| US5348867A (en) | 1991-11-15 | 1994-09-20 | George Georgiou | Expression of proteins on bacterial surface |
| US5866344A (en) | 1991-11-15 | 1999-02-02 | Board Of Regents, The University Of Texas System | Antibody selection methods using cell surface expressed libraries |
| ES2196009T3 (es) | 1992-07-08 | 2003-12-16 | Unilever Nv | Procedimiento para inmovilizar enzimas en la pared celular de una celula microbiana mediante la produccion de una proteina de fusion. |
| US7166423B1 (en) | 1992-10-21 | 2007-01-23 | Miltenyi Biotec Gmbh | Direct selection of cells by secretion product |
| CA2146974C (en) | 1992-10-21 | 2010-02-02 | Andreas Radbruch | Direct selection of cells by secretion product |
| PT682710E (pt) | 1993-02-10 | 2004-03-31 | Unilever Nv | Processo de isolamento utilizando proteinas imobilizadas com capacidades de ligacao especificas |
| EP0711303B2 (en) | 1993-07-30 | 2009-06-10 | Affymax, Inc. | Biotinylation of proteins |
| US6300065B1 (en) | 1996-05-31 | 2001-10-09 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6699658B1 (en) | 1996-05-31 | 2004-03-02 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6696251B1 (en) | 1996-05-31 | 2004-02-24 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| ATE230850T1 (de) | 1996-10-08 | 2003-01-15 | Bisys B V U | Verfahren und mittel zur auswahl von peptiden und proteinen mit spezifischer affinität zu einem zielmolekül |
| WO1998047343A2 (en) | 1997-04-04 | 1998-10-29 | Biosite Diagnostics, Inc. | Antibodies or binding protein libraries displayed on phage, cells, or other replicatable genetic packages |
| US6555310B1 (en) | 1997-04-04 | 2003-04-29 | Biosite Diagnostics, Inc. | Polyclonal libraries |
| US6057098A (en) | 1997-04-04 | 2000-05-02 | Biosite Diagnostics, Inc. | Polyvalent display libraries |
| US6759243B2 (en) | 1998-01-20 | 2004-07-06 | Board Of Trustees Of The University Of Illinois | High affinity TCR proteins and methods |
| US6255075B1 (en) | 1998-10-20 | 2001-07-03 | Smithkline Beecham Corporation | Bira |
| US7223533B2 (en) | 1999-09-10 | 2007-05-29 | Cadus Technologies, Inc. | Cell surface proteins and use thereof as indicators of activation of cellular signal transduction pathways |
| US6686168B1 (en) | 1999-11-04 | 2004-02-03 | Zymogenetics, Inc. | Cell surface display of proteins by recombinant host cells |
| WO2002012509A1 (en) | 2000-07-26 | 2002-02-14 | Korea Research Institute Of Bioscience And Biotechnology | Novel cell wall anchor proteins derived from yeast, genes thereof and cell surface expression systems using the same |
| US20020142355A1 (en) | 2000-11-14 | 2002-10-03 | Baylor College Of Medicine | Methods for the in vivo biotin labeling of polypeptides |
| JP4368196B2 (ja) | 2000-11-17 | 2009-11-18 | ユニバーシティー オブ ロチェスター | 真核細胞において免疫グロブリン分子を製造および同定するインビトロにおける方法 |
| WO2002057423A2 (en) | 2001-01-16 | 2002-07-25 | Regeneron Pharmaceuticals, Inc. | Isolating cells expressing secreted proteins |
| US7192764B2 (en) | 2001-04-19 | 2007-03-20 | Kansai Chemical Engineering, Co. | Cell surface layer-binding protein and utilization thereof |
| GB0118337D0 (en) | 2001-07-27 | 2001-09-19 | Lonza Biologics Plc | Method for selecting antibody expressing cells |
| CA2462113C (en) | 2001-10-01 | 2013-01-29 | Dyax Corp. | Multi-chain eukaryotic display vectors and uses thereof |
| GB0202018D0 (en) | 2002-01-29 | 2002-03-13 | Sense Proteomic Ltd | Tag and method |
| EP1367125A1 (en) | 2002-05-30 | 2003-12-03 | Centre National De La Recherche Scientifique (Cnrs) | Vectors for expression of biotinylated proteins in mammalian cells, and their use for identification of protein-nucleic acid interactions in vivo |
| US20040132133A1 (en) | 2002-07-08 | 2004-07-08 | Invitrogen Corporation | Methods and compositions for the production, identification and purification of fusion proteins |
| US20040033603A1 (en) | 2002-08-19 | 2004-02-19 | Lin Zhang | Biotinylation of proteins |
| FI20031663A0 (fi) | 2003-11-14 | 2003-11-14 | Jyvaeskylaen Yliopisto | Avidiinin mutantteja |
| US7795411B2 (en) | 2006-10-05 | 2010-09-14 | Fred Hutchinson Cancer Research Center | Vectors for expressing in vivo biotinylated recombinant proteins |
| WO2008063310A2 (en) | 2006-10-13 | 2008-05-29 | Archer-Daniels-Midland Company | Use of cell surface displays in yeast cell catalyst supports |
| US8067179B2 (en) | 2006-11-30 | 2011-11-29 | Research Development Foundation | Immunoglobulin libraries |
| JP5754135B2 (ja) | 2007-03-26 | 2015-07-29 | アジェナス インコーポレイテッド | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
| US8043830B2 (en) | 2008-02-01 | 2011-10-25 | The Regents Of The University Of California | Biotin-ligase system for secretion of biotinylated protein |
-
2008
- 2008-03-26 JP JP2010500980A patent/JP5754135B2/ja not_active Expired - Fee Related
- 2008-03-26 WO PCT/US2008/003978 patent/WO2008118476A2/en not_active Ceased
- 2008-03-26 EP EP08727167.2A patent/EP2137308B1/en not_active Not-in-force
- 2008-03-26 EP EP12154795.4A patent/EP2617827A1/en not_active Withdrawn
- 2008-03-26 US US12/056,264 patent/US8709980B2/en not_active Expired - Fee Related
-
2009
- 2009-08-24 US US12/546,583 patent/US8722586B2/en not_active Expired - Fee Related
-
2013
- 2013-08-20 JP JP2013170132A patent/JP2013233157A/ja not_active Withdrawn
-
2014
- 2014-03-26 US US14/226,114 patent/US9645146B2/en not_active Expired - Fee Related
-
2017
- 2017-03-28 US US15/471,604 patent/US20170261506A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| US20140357508A1 (en) | 2014-12-04 |
| US20090005264A1 (en) | 2009-01-01 |
| US8709980B2 (en) | 2014-04-29 |
| US8722586B2 (en) | 2014-05-13 |
| EP2137308A2 (en) | 2009-12-30 |
| JP2013233157A (ja) | 2013-11-21 |
| US20170261506A1 (en) | 2017-09-14 |
| US9645146B2 (en) | 2017-05-09 |
| EP2137308B1 (en) | 2016-08-03 |
| US20100267057A1 (en) | 2010-10-21 |
| EP2617827A1 (en) | 2013-07-24 |
| WO2008118476A2 (en) | 2008-10-02 |
| JP2010522561A (ja) | 2010-07-08 |
| WO2008118476A3 (en) | 2008-11-13 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP5754135B2 (ja) | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 | |
| US11078479B2 (en) | Polypeptide display libraries and methods of making and using thereof | |
| CN102245771B (zh) | 酵母展示系统 | |
| JP7419248B2 (ja) | ペリプラズム空間中におけるタンパク質の酵母ディスプレイ | |
| CN105659088A (zh) | 用于监测肽的细胞运输的方法 | |
| EP2516702B1 (en) | Protein display | |
| US10908163B2 (en) | Analysis method of molecular interactions on protein nanoparticles using flow cytometry | |
| HK40043087A (en) | Yeast display of proteins in the periplasmic space |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20110325 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20110325 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20111226 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20111226 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20120309 |
|
| A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A711 Effective date: 20120420 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20120420 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20130220 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20130513 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20130520 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20130619 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20130626 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20130712 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20130722 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20130820 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20140507 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20140807 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20140814 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20140905 |
|
| 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: 20150310 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20150406 |
|
| A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A711 Effective date: 20150511 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20150511 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20150511 |
|
| R150 | Certificate of patent or registration of utility model |
Ref document number: 5754135 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| LAPS | Cancellation because of no payment of annual fees |