JP2007535317A - 下等真核生物におけるガラクトシル化された糖タンパク質の産生 - Google Patents
下等真核生物におけるガラクトシル化された糖タンパク質の産生 Download PDFInfo
- Publication number
- JP2007535317A JP2007535317A JP2007507921A JP2007507921A JP2007535317A JP 2007535317 A JP2007535317 A JP 2007535317A JP 2007507921 A JP2007507921 A JP 2007507921A JP 2007507921 A JP2007507921 A JP 2007507921A JP 2007535317 A JP2007535317 A JP 2007535317A
- Authority
- JP
- Japan
- Prior art keywords
- glcnac
- galactose
- man
- pichia
- udp
- 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.)
- Withdrawn
Links
- 108090000288 Glycoproteins Proteins 0.000 title claims abstract description 116
- 102000003886 Glycoproteins Human genes 0.000 title claims abstract description 116
- 238000004519 manufacturing process Methods 0.000 title claims description 35
- 241000206602 Eukaryota Species 0.000 title description 19
- 238000000034 method Methods 0.000 claims abstract description 72
- HSCJRCZFDFQWRP-UHFFFAOYSA-N Uridindiphosphoglukose Natural products OC1C(O)C(O)C(CO)OC1OP(O)(=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(NC(=O)C=C2)=O)O1 HSCJRCZFDFQWRP-UHFFFAOYSA-N 0.000 claims abstract description 62
- HSCJRCZFDFQWRP-ABVWGUQPSA-N UDP-alpha-D-galactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1OP(O)(=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(NC(=O)C=C2)=O)O1 HSCJRCZFDFQWRP-ABVWGUQPSA-N 0.000 claims abstract description 57
- 238000012546 transfer Methods 0.000 claims abstract description 49
- 239000000758 substrate Substances 0.000 claims abstract description 33
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical group C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 claims abstract description 18
- 125000005629 sialic acid group Chemical group 0.000 claims abstract description 14
- WQZGKKKJIJFFOK-FPRJBGLDSA-N beta-D-galactose Chemical group OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-FPRJBGLDSA-N 0.000 claims abstract description 11
- 108090000623 proteins and genes Proteins 0.000 claims description 215
- OVRNDRQMDRJTHS-RTRLPJTCSA-N N-acetyl-D-glucosamine Chemical group CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-RTRLPJTCSA-N 0.000 claims description 179
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 claims description 169
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 claims description 168
- 210000004027 cell Anatomy 0.000 claims description 155
- 241000282414 Homo sapiens Species 0.000 claims description 122
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 115
- 230000000694 effects Effects 0.000 claims description 110
- 102000004169 proteins and genes Human genes 0.000 claims description 104
- 150000007523 nucleic acids Chemical class 0.000 claims description 100
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 92
- 229920001184 polypeptide Polymers 0.000 claims description 86
- 230000004927 fusion Effects 0.000 claims description 65
- 102000039446 nucleic acids Human genes 0.000 claims description 55
- 108020004707 nucleic acids Proteins 0.000 claims description 55
- 108090001066 Racemases and epimerases Proteins 0.000 claims description 47
- 102000004879 Racemases and epimerases Human genes 0.000 claims description 42
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 39
- 241000235648 Pichia Species 0.000 claims description 39
- 108010075920 UDP-galactose translocator Proteins 0.000 claims description 39
- 102100033782 UDP-galactose translocator Human genes 0.000 claims description 35
- 125000000539 amino acid group Chemical group 0.000 claims description 35
- 239000002773 nucleotide Substances 0.000 claims description 34
- 125000003729 nucleotide group Chemical group 0.000 claims description 34
- 239000012634 fragment Substances 0.000 claims description 33
- GRHWEVYJIHXESA-HBHDJDHDSA-N beta-D-Galp-(1->4)-beta-D-GlcpNAc-(1->2)-alpha-D-Manp-(1->3)-[beta-D-Galp-(1->4)-beta-D-GlcpNAc-(1->2)-alpha-D-Manp-(1->6)]-beta-D-Manp-(1->4)-beta-D-GlcpNAc-(1->4)-beta-D-GlcpNAc Chemical compound O[C@@H]1[C@@H](NC(=O)C)[C@H](O)O[C@H](CO)[C@H]1O[C@H]1[C@H](NC(C)=O)[C@@H](O)[C@H](O[C@H]2[C@H]([C@@H](O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@H]3[C@@H]([C@@H](O)[C@H](O[C@H]4[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O4)O)[C@@H](CO)O3)NC(C)=O)[C@H](O)[C@@H](CO[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@H]3[C@@H]([C@@H](O)[C@H](O[C@H]4[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O4)O)[C@@H](CO)O3)NC(C)=O)O2)O)[C@@H](CO)O1 GRHWEVYJIHXESA-HBHDJDHDSA-N 0.000 claims description 32
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 26
- 108060003306 Galactosyltransferase Proteins 0.000 claims description 22
- 102000030902 Galactosyltransferase Human genes 0.000 claims description 22
- 108010046068 N-Acetyllactosamine Synthase Proteins 0.000 claims description 22
- WYUKJASPBYYQRJ-VSJOFRJTSA-N beta-D-GlcpNAc-(1->2)-alpha-D-Manp-(1->3)-[beta-D-GlcpNAc-(1->2)-alpha-D-Manp-(1->6)]-beta-D-Manp-(1->4)-beta-GlcpNAc-(1->4)-beta-D-GlcpNAc Chemical compound O[C@@H]1[C@@H](NC(=O)C)[C@H](O)O[C@H](CO)[C@H]1O[C@H]1[C@H](NC(C)=O)[C@@H](O)[C@H](O[C@H]2[C@H]([C@@H](O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)NC(C)=O)[C@H](O)[C@@H](CO[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)NC(C)=O)O2)O)[C@@H](CO)O1 WYUKJASPBYYQRJ-VSJOFRJTSA-N 0.000 claims description 21
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 claims description 21
- 239000000203 mixture Substances 0.000 claims description 21
- 241000235058 Komagataella pastoris Species 0.000 claims description 20
- 108091033319 polynucleotide Proteins 0.000 claims description 20
- 102000040430 polynucleotide Human genes 0.000 claims description 20
- 239000002157 polynucleotide Substances 0.000 claims description 20
- 229920001542 oligosaccharide Polymers 0.000 claims description 18
- 102000005962 receptors Human genes 0.000 claims description 17
- 108020003175 receptors Proteins 0.000 claims description 17
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 claims description 16
- 230000027455 binding Effects 0.000 claims description 16
- 150000002482 oligosaccharides Chemical class 0.000 claims description 16
- PNNNRSAQSRJVSB-SLPGGIOYSA-N Fucose Natural products C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-SLPGGIOYSA-N 0.000 claims description 15
- 239000002777 nucleoside Substances 0.000 claims description 14
- 102100029724 Ectonucleoside triphosphate diphosphohydrolase 4 Human genes 0.000 claims description 13
- 108010008924 uridine diphosphatase Proteins 0.000 claims description 13
- 108020001507 fusion proteins Proteins 0.000 claims description 12
- 102000037865 fusion proteins Human genes 0.000 claims description 12
- 239000002243 precursor Substances 0.000 claims description 12
- 102100021735 Galectin-2 Human genes 0.000 claims description 11
- -1 cytokines Chemical compound 0.000 claims description 11
- 108700023157 Galactokinases Proteins 0.000 claims description 10
- 102000048120 Galactokinases Human genes 0.000 claims description 10
- 108010001496 Galectin 2 Proteins 0.000 claims description 10
- 230000002829 reductive effect Effects 0.000 claims description 10
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 claims description 10
- 241000223259 Trichoderma Species 0.000 claims description 9
- 108010058532 UTP-hexose-1-phosphate uridylyltransferase Proteins 0.000 claims description 9
- 102000006321 UTP-hexose-1-phosphate uridylyltransferase Human genes 0.000 claims description 9
- 101000672037 Homo sapiens UDP-glucose:glycoprotein glucosyltransferase 2 Proteins 0.000 claims description 8
- 108010054377 Mannosidases Proteins 0.000 claims description 8
- 102000001696 Mannosidases Human genes 0.000 claims description 8
- 241001138401 Kluyveromyces lactis Species 0.000 claims description 7
- 108010087568 Mannosyltransferases Proteins 0.000 claims description 7
- 102000006722 Mannosyltransferases Human genes 0.000 claims description 7
- 108010066816 Polypeptide N-acetylgalactosaminyltransferase Proteins 0.000 claims description 7
- 239000003446 ligand Substances 0.000 claims description 7
- 102100022622 Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Human genes 0.000 claims description 6
- 108010001517 Galectin 3 Proteins 0.000 claims description 6
- 102100039558 Galectin-3 Human genes 0.000 claims description 6
- 101000972916 Homo sapiens Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Proteins 0.000 claims description 6
- 241001489174 Ogataea minuta Species 0.000 claims description 6
- 102100040361 UDP-glucose:glycoprotein glucosyltransferase 2 Human genes 0.000 claims description 6
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 6
- 108010083819 mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase Proteins 0.000 claims description 6
- 240000006439 Aspergillus oryzae Species 0.000 claims description 5
- 235000002247 Aspergillus oryzae Nutrition 0.000 claims description 5
- 101000672024 Homo sapiens UDP-glucose:glycoprotein glucosyltransferase 1 Proteins 0.000 claims description 5
- 241000221960 Neurospora Species 0.000 claims description 5
- 241000320412 Ogataea angusta Species 0.000 claims description 5
- 229910052717 sulfur Inorganic materials 0.000 claims description 5
- 239000002753 trypsin inhibitor Substances 0.000 claims description 5
- 241000228245 Aspergillus niger Species 0.000 claims description 4
- 241000222122 Candida albicans Species 0.000 claims description 4
- 241000567178 Fusarium venenatum Species 0.000 claims description 4
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 4
- 101000605403 Homo sapiens Plasminogen Proteins 0.000 claims description 4
- 241000170280 Kluyveromyces sp. Species 0.000 claims description 4
- 241000489470 Ogataea trehalophila Species 0.000 claims description 4
- 241000826199 Ogataea wickerhamii Species 0.000 claims description 4
- 241000195887 Physcomitrella patens Species 0.000 claims description 4
- 241000370136 Wickerhamomyces pijperi Species 0.000 claims description 4
- 239000004202 carbamide Substances 0.000 claims description 4
- 230000012010 growth Effects 0.000 claims description 4
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 claims description 3
- 102400000068 Angiostatin Human genes 0.000 claims description 3
- 108010079709 Angiostatins Proteins 0.000 claims description 3
- 108090000672 Annexin A5 Proteins 0.000 claims description 3
- 102000004121 Annexin A5 Human genes 0.000 claims description 3
- 102000004411 Antithrombin III Human genes 0.000 claims description 3
- 108090000935 Antithrombin III Proteins 0.000 claims description 3
- 241000283690 Bos taurus Species 0.000 claims description 3
- 101001107784 Caenorhabditis elegans Deoxyribonuclease-2 Proteins 0.000 claims description 3
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 claims description 3
- 102000014914 Carrier Proteins Human genes 0.000 claims description 3
- 102100024539 Chymase Human genes 0.000 claims description 3
- 108090000227 Chymases Proteins 0.000 claims description 3
- 102100022641 Coagulation factor IX Human genes 0.000 claims description 3
- 102000001493 Cyclophilins Human genes 0.000 claims description 3
- 108010068682 Cyclophilins Proteins 0.000 claims description 3
- 102000004127 Cytokines Human genes 0.000 claims description 3
- 108090000695 Cytokines Proteins 0.000 claims description 3
- 101800003838 Epidermal growth factor Proteins 0.000 claims description 3
- 102400001368 Epidermal growth factor Human genes 0.000 claims description 3
- 108090000394 Erythropoietin Proteins 0.000 claims description 3
- 102000003951 Erythropoietin Human genes 0.000 claims description 3
- 108010076282 Factor IX Proteins 0.000 claims description 3
- 108010054218 Factor VIII Proteins 0.000 claims description 3
- 102000001690 Factor VIII Human genes 0.000 claims description 3
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 claims description 3
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 claims description 3
- 241000223218 Fusarium Species 0.000 claims description 3
- 102000004547 Glucosylceramidase Human genes 0.000 claims description 3
- 108010017544 Glucosylceramidase Proteins 0.000 claims description 3
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 claims description 3
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 claims description 3
- 101500025568 Homo sapiens Saposin-D Proteins 0.000 claims description 3
- 101000640793 Homo sapiens UDP-galactose translocator Proteins 0.000 claims description 3
- 102000009438 IgE Receptors Human genes 0.000 claims description 3
- 108010073816 IgE Receptors Proteins 0.000 claims description 3
- 102000010789 Interleukin-2 Receptors Human genes 0.000 claims description 3
- 108010038453 Interleukin-2 Receptors Proteins 0.000 claims description 3
- 102000015696 Interleukins Human genes 0.000 claims description 3
- 108010063738 Interleukins Proteins 0.000 claims description 3
- 102000008108 Osteoprotegerin Human genes 0.000 claims description 3
- 108010035042 Osteoprotegerin Proteins 0.000 claims description 3
- 241000235088 Saccharomyces sp. Species 0.000 claims description 3
- 108090000190 Thrombin Proteins 0.000 claims description 3
- 101710162629 Trypsin inhibitor Proteins 0.000 claims description 3
- 229940122618 Trypsin inhibitor Drugs 0.000 claims description 3
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 claims description 3
- 102100040247 Tumor necrosis factor Human genes 0.000 claims description 3
- 102100040363 UDP-glucose:glycoprotein glucosyltransferase 1 Human genes 0.000 claims description 3
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 claims description 3
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 claims description 3
- 239000012190 activator Substances 0.000 claims description 3
- 239000000427 antigen Substances 0.000 claims description 3
- 108091007433 antigens Proteins 0.000 claims description 3
- 102000036639 antigens Human genes 0.000 claims description 3
- 229960005348 antithrombin iii Drugs 0.000 claims description 3
- FZCSTZYAHCUGEM-UHFFFAOYSA-N aspergillomarasmine B Natural products OC(=O)CNC(C(O)=O)CNC(C(O)=O)CC(O)=O FZCSTZYAHCUGEM-UHFFFAOYSA-N 0.000 claims description 3
- 108091008324 binding proteins Proteins 0.000 claims description 3
- 229910052791 calcium Inorganic materials 0.000 claims description 3
- 239000011575 calcium Substances 0.000 claims description 3
- 229940095731 candida albicans Drugs 0.000 claims description 3
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 claims description 3
- 230000003511 endothelial effect Effects 0.000 claims description 3
- 229940116977 epidermal growth factor Drugs 0.000 claims description 3
- 229940105423 erythropoietin Drugs 0.000 claims description 3
- 229960004222 factor ix Drugs 0.000 claims description 3
- 229960000301 factor viii Drugs 0.000 claims description 3
- 229940028334 follicle stimulating hormone Drugs 0.000 claims description 3
- 239000008103 glucose Substances 0.000 claims description 3
- 229940100689 human protein c Drugs 0.000 claims description 3
- 102000028416 insulin-like growth factor binding Human genes 0.000 claims description 3
- 108091022911 insulin-like growth factor binding Proteins 0.000 claims description 3
- XXUPLYBCNPLTIW-UHFFFAOYSA-N octadec-7-ynoic acid Chemical compound CCCCCCCCCCC#CCCCCCC(O)=O XXUPLYBCNPLTIW-UHFFFAOYSA-N 0.000 claims description 3
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 claims description 3
- 239000000018 receptor agonist Substances 0.000 claims description 3
- 229940044601 receptor agonist Drugs 0.000 claims description 3
- 229960004072 thrombin Drugs 0.000 claims description 3
- 102000003298 tumor necrosis factor receptor Human genes 0.000 claims description 3
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 claims description 3
- 229960005356 urokinase Drugs 0.000 claims description 3
- 230000002792 vascular Effects 0.000 claims description 3
- 241001149959 Fusarium sp. Species 0.000 claims description 2
- 108010001515 Galectin 4 Proteins 0.000 claims description 2
- 102100024637 Galectin-10 Human genes 0.000 claims description 2
- 102100039556 Galectin-4 Human genes 0.000 claims description 2
- 101001011019 Gallus gallus Gallinacin-10 Proteins 0.000 claims description 2
- 101001011021 Gallus gallus Gallinacin-12 Proteins 0.000 claims description 2
- 241001599018 Melanogaster Species 0.000 claims description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 claims description 2
- 125000003835 nucleoside group Chemical group 0.000 claims description 2
- 108010039209 Blood Coagulation Factors Proteins 0.000 claims 2
- 102000015081 Blood Coagulation Factors Human genes 0.000 claims 2
- 108010051696 Growth Hormone Proteins 0.000 claims 2
- 102000018997 Growth Hormone Human genes 0.000 claims 2
- 239000003114 blood coagulation factor Substances 0.000 claims 2
- 239000000122 growth hormone Substances 0.000 claims 2
- 241000351920 Aspergillus nidulans Species 0.000 claims 1
- 102100021771 Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase Human genes 0.000 claims 1
- 241000269368 Xenopus laevis Species 0.000 claims 1
- 108010042381 alpha 1,3-mannosyltransferase Proteins 0.000 claims 1
- 108010009689 mannosyl-oligosaccharide 1,2-alpha-mannosidase Proteins 0.000 claims 1
- 230000017105 transposition Effects 0.000 claims 1
- 230000001225 therapeutic effect Effects 0.000 abstract description 9
- 239000013612 plasmid Substances 0.000 description 108
- 235000018102 proteins Nutrition 0.000 description 95
- 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 72
- 230000014509 gene expression Effects 0.000 description 66
- 239000013598 vector Substances 0.000 description 52
- 235000001014 amino acid Nutrition 0.000 description 42
- 102000004190 Enzymes Human genes 0.000 description 41
- 108090000790 Enzymes Proteins 0.000 description 41
- 229940088598 enzyme Drugs 0.000 description 41
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 40
- 229930182830 galactose Natural products 0.000 description 40
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 39
- 150000001413 amino acids Chemical class 0.000 description 37
- 229940024606 amino acid Drugs 0.000 description 36
- 108020004414 DNA Proteins 0.000 description 34
- 108010075202 UDP-glucose 4-epimerase Proteins 0.000 description 33
- 102100021436 UDP-glucose 4-epimerase Human genes 0.000 description 29
- 238000006206 glycosylation reaction Methods 0.000 description 29
- 230000000875 corresponding effect Effects 0.000 description 28
- 230000013595 glycosylation Effects 0.000 description 28
- 230000003248 secreting effect Effects 0.000 description 26
- 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 24
- 235000000346 sugar Nutrition 0.000 description 24
- 230000037361 pathway Effects 0.000 description 22
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 21
- 239000000047 product Substances 0.000 description 21
- 238000007792 addition Methods 0.000 description 20
- 150000004676 glycans Chemical class 0.000 description 20
- 238000004458 analytical method Methods 0.000 description 19
- 230000010354 integration Effects 0.000 description 19
- 108010076504 Protein Sorting Signals Proteins 0.000 description 17
- 239000002299 complementary DNA Substances 0.000 description 16
- 239000002609 medium Substances 0.000 description 16
- 230000004048 modification Effects 0.000 description 15
- 238000012986 modification Methods 0.000 description 15
- 238000006467 substitution reaction Methods 0.000 description 15
- 238000012217 deletion Methods 0.000 description 14
- 230000037430 deletion Effects 0.000 description 14
- 101150082479 GAL gene Proteins 0.000 description 13
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 12
- 102000004856 Lectins Human genes 0.000 description 12
- 108090001090 Lectins Proteins 0.000 description 12
- 102000004357 Transferases Human genes 0.000 description 12
- 108090000992 Transferases Proteins 0.000 description 12
- 230000015572 biosynthetic process Effects 0.000 description 12
- 210000002288 golgi apparatus Anatomy 0.000 description 12
- 239000002523 lectin Substances 0.000 description 12
- 230000009466 transformation Effects 0.000 description 12
- 238000010367 cloning Methods 0.000 description 11
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- 238000010276 construction Methods 0.000 description 10
- 108010078791 Carrier Proteins Proteins 0.000 description 9
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 9
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 9
- 241000233866 Fungi Species 0.000 description 9
- 230000003197 catalytic effect Effects 0.000 description 9
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 9
- 238000000338 in vitro Methods 0.000 description 9
- 230000003834 intracellular effect Effects 0.000 description 9
- 125000000311 mannosyl group Chemical group C1([C@@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 9
- 239000003550 marker Substances 0.000 description 9
- 241000894007 species Species 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- LFTYTUAZOPRMMI-UHFFFAOYSA-N UNPD164450 Natural products O1C(CO)C(O)C(O)C(NC(=O)C)C1OP(O)(=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(NC(=O)C=C2)=O)O1 LFTYTUAZOPRMMI-UHFFFAOYSA-N 0.000 description 8
- 239000001177 diphosphate Substances 0.000 description 8
- 235000011180 diphosphates Nutrition 0.000 description 8
- 230000006870 function Effects 0.000 description 8
- 238000009396 hybridization Methods 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- 101150061302 och1 gene Proteins 0.000 description 8
- 241000255601 Drosophila melanogaster Species 0.000 description 7
- 241000196324 Embryophyta Species 0.000 description 7
- 239000000872 buffer Substances 0.000 description 7
- 238000006243 chemical reaction Methods 0.000 description 7
- 230000000295 complement effect Effects 0.000 description 7
- 150000001875 compounds Chemical class 0.000 description 7
- 239000013604 expression vector Substances 0.000 description 7
- 125000002519 galactosyl group Chemical group C1([C@H](O)[C@@H](O)[C@@H](O)[C@H](O1)CO)* 0.000 description 7
- 230000035772 mutation Effects 0.000 description 7
- 239000000523 sample Substances 0.000 description 7
- 150000008163 sugars Chemical class 0.000 description 7
- 238000003786 synthesis reaction Methods 0.000 description 7
- 230000032258 transport Effects 0.000 description 7
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 6
- TXCIAUNLDRJGJZ-BILDWYJOSA-N CMP-N-acetyl-beta-neuraminic acid Chemical compound O1[C@@H]([C@H](O)[C@H](O)CO)[C@H](NC(=O)C)[C@@H](O)C[C@]1(C(O)=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(N=C(N)C=C2)=O)O1 TXCIAUNLDRJGJZ-BILDWYJOSA-N 0.000 description 6
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 6
- 241000282412 Homo Species 0.000 description 6
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 description 6
- 238000012408 PCR amplification Methods 0.000 description 6
- 101150040428 SEC4 gene Proteins 0.000 description 6
- 102000003838 Sialyltransferases Human genes 0.000 description 6
- 108090000141 Sialyltransferases Proteins 0.000 description 6
- HSCJRCZFDFQWRP-JZMIEXBBSA-N UDP-alpha-D-glucose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OP(O)(=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(NC(=O)C=C2)=O)O1 HSCJRCZFDFQWRP-JZMIEXBBSA-N 0.000 description 6
- 238000003776 cleavage reaction Methods 0.000 description 6
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 6
- 210000004962 mammalian cell Anatomy 0.000 description 6
- 230000007017 scission Effects 0.000 description 6
- 238000011144 upstream manufacturing Methods 0.000 description 6
- UQBIAGWOJDEOMN-UHFFFAOYSA-N 2-O-(2-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranosyl)-D-mannopyranose Natural products OC1C(O)C(CO)OC(O)C1OC1C(OC2C(C(O)C(O)C(CO)O2)O)C(O)C(O)C(CO)O1 UQBIAGWOJDEOMN-UHFFFAOYSA-N 0.000 description 5
- 108091026890 Coding region Proteins 0.000 description 5
- 108700023372 Glycosyltransferases Proteins 0.000 description 5
- 101150093457 MNN2 gene Proteins 0.000 description 5
- SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 description 5
- 108700026244 Open Reading Frames Proteins 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 238000002869 basic local alignment search tool Methods 0.000 description 5
- 210000000172 cytosol Anatomy 0.000 description 5
- 230000002950 deficient Effects 0.000 description 5
- 230000002538 fungal effect Effects 0.000 description 5
- 108010029257 guanosine-diphosphatase Proteins 0.000 description 5
- 108010045961 human beta1,4-galactosyltransferase Proteins 0.000 description 5
- 102000005383 human beta1,4-galactosyltransferase Human genes 0.000 description 5
- 210000003734 kidney Anatomy 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 239000011159 matrix material Substances 0.000 description 5
- 230000003278 mimic effect Effects 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 238000001228 spectrum Methods 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- 102000005427 Asialoglycoprotein Receptor Human genes 0.000 description 4
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- TXCIAUNLDRJGJZ-UHFFFAOYSA-N CMP-N-acetyl neuraminic acid Natural products O1C(C(O)C(O)CO)C(NC(=O)C)C(O)CC1(C(O)=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(N=C(N)C=C2)=O)O1 TXCIAUNLDRJGJZ-UHFFFAOYSA-N 0.000 description 4
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 4
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 4
- 241000238631 Hexapoda Species 0.000 description 4
- 108010021466 Mutant Proteins Proteins 0.000 description 4
- 102000008300 Mutant Proteins Human genes 0.000 description 4
- 229910019142 PO4 Inorganic materials 0.000 description 4
- 101710132662 Protein K3 Proteins 0.000 description 4
- LFTYTUAZOPRMMI-NESSUJCYSA-N UDP-N-acetyl-alpha-D-galactosamine Chemical compound O1[C@H](CO)[C@H](O)[C@H](O)[C@@H](NC(=O)C)[C@H]1O[P@](O)(=O)O[P@](O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(NC(=O)C=C2)=O)O1 LFTYTUAZOPRMMI-NESSUJCYSA-N 0.000 description 4
- LFTYTUAZOPRMMI-CFRASDGPSA-N UDP-N-acetyl-alpha-D-glucosamine Chemical compound O1[C@H](CO)[C@@H](O)[C@H](O)[C@@H](NC(=O)C)[C@H]1OP(O)(=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(NC(=O)C=C2)=O)O1 LFTYTUAZOPRMMI-CFRASDGPSA-N 0.000 description 4
- 230000009471 action Effects 0.000 description 4
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 4
- 108010006523 asialoglycoprotein receptor Proteins 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 229910052799 carbon Inorganic materials 0.000 description 4
- 210000000349 chromosome Anatomy 0.000 description 4
- 238000007796 conventional method Methods 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 108010090279 galactose permease Proteins 0.000 description 4
- 238000010353 genetic engineering Methods 0.000 description 4
- 238000001727 in vivo Methods 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 239000000543 intermediate Substances 0.000 description 4
- 150000004712 monophosphates Chemical class 0.000 description 4
- 238000002703 mutagenesis Methods 0.000 description 4
- 231100000350 mutagenesis Toxicity 0.000 description 4
- 230000007935 neutral effect Effects 0.000 description 4
- 238000011330 nucleic acid test Methods 0.000 description 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 230000001105 regulatory effect Effects 0.000 description 4
- 239000011347 resin Substances 0.000 description 4
- 229920005989 resin Polymers 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 238000013518 transcription Methods 0.000 description 4
- 230000035897 transcription Effects 0.000 description 4
- 239000007222 ypd medium Substances 0.000 description 4
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 101710194180 Alcohol oxidase 1 Proteins 0.000 description 3
- 108010002913 Asialoglycoproteins Proteins 0.000 description 3
- 101100184475 Candida albicans (strain SC5314 / ATCC MYA-2876) MNN24 gene Proteins 0.000 description 3
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 3
- 108010019236 Fucosyltransferases Proteins 0.000 description 3
- 102000006471 Fucosyltransferases Human genes 0.000 description 3
- 101000819146 Homo sapiens UDP-glucose 4-epimerase Proteins 0.000 description 3
- 101100488151 Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) YEA4 gene Proteins 0.000 description 3
- 241000124008 Mammalia Species 0.000 description 3
- MBLBDJOUHNCFQT-UHFFFAOYSA-N N-acetyl-D-galactosamine Natural products CC(=O)NC(C=O)C(O)C(O)C(O)CO MBLBDJOUHNCFQT-UHFFFAOYSA-N 0.000 description 3
- 101710146026 Peptidoglycan D,D-transpeptidase FtsI Proteins 0.000 description 3
- 101710181936 Phosphate-binding protein PstS 3 Proteins 0.000 description 3
- 241000982698 Prorodonopsis coli Species 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- HXXFSFRBOHSIMQ-FPRJBGLDSA-N alpha-D-galactose 1-phosphate Chemical compound OC[C@H]1O[C@H](OP(O)(O)=O)[C@H](O)[C@@H](O)[C@H]1O HXXFSFRBOHSIMQ-FPRJBGLDSA-N 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 230000033228 biological regulation Effects 0.000 description 3
- 239000006227 byproduct Substances 0.000 description 3
- 210000000170 cell membrane Anatomy 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 239000013599 cloning vector Substances 0.000 description 3
- 230000001143 conditioned effect Effects 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 230000001747 exhibiting effect Effects 0.000 description 3
- 102000045442 glycosyltransferase activity proteins Human genes 0.000 description 3
- 108700014210 glycosyltransferase activity proteins Proteins 0.000 description 3
- 150000002402 hexoses Chemical class 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 238000002372 labelling Methods 0.000 description 3
- 230000000670 limiting effect Effects 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 238000005621 mannosylation reaction Methods 0.000 description 3
- 230000035800 maturation Effects 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 229950006780 n-acetylglucosamine Drugs 0.000 description 3
- 229910052757 nitrogen Inorganic materials 0.000 description 3
- 150000003833 nucleoside derivatives Chemical class 0.000 description 3
- 239000010452 phosphate Substances 0.000 description 3
- 229910052698 phosphorus Inorganic materials 0.000 description 3
- 230000026731 phosphorylation Effects 0.000 description 3
- 238000006366 phosphorylation reaction Methods 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 230000004481 post-translational protein modification Effects 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- 210000005253 yeast cell Anatomy 0.000 description 3
- 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 2
- CERZMXAJYMMUDR-QBTAGHCHSA-N 5-amino-3,5-dideoxy-D-glycero-D-galacto-non-2-ulopyranosonic acid Chemical compound N[C@@H]1[C@@H](O)CC(O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO CERZMXAJYMMUDR-QBTAGHCHSA-N 0.000 description 2
- IZZIWIAOVZOBLF-UHFFFAOYSA-N 5-methoxysalicylic acid Chemical compound COC1=CC=C(O)C(C(O)=O)=C1 IZZIWIAOVZOBLF-UHFFFAOYSA-N 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 241000228212 Aspergillus Species 0.000 description 2
- 239000002028 Biomass Substances 0.000 description 2
- 235000015256 Chionanthus virginicus Nutrition 0.000 description 2
- 101800004419 Cleaved form Proteins 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 241000195493 Cryptophyta Species 0.000 description 2
- NBSCHQHZLSJFNQ-QTVWNMPRSA-N D-Mannose-6-phosphate Chemical compound OC1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H](O)[C@@H]1O NBSCHQHZLSJFNQ-QTVWNMPRSA-N 0.000 description 2
- 101000672031 Drosophila melanogaster UDP-glucose:glycoprotein glucosyltransferase Proteins 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- 102000051366 Glycosyltransferases Human genes 0.000 description 2
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 2
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 2
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 2
- 101150017040 I gene Proteins 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108010006769 Monosaccharide Transport Proteins Proteins 0.000 description 2
- 102000005455 Monosaccharide Transport Proteins Human genes 0.000 description 2
- 102100036518 Nucleoside diphosphate phosphatase ENTPD5 Human genes 0.000 description 2
- 241001452677 Ogataea methanolica Species 0.000 description 2
- 108010055817 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Proteins 0.000 description 2
- 102000000447 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Human genes 0.000 description 2
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
- 240000001857 Phyllostachys elegans Species 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 241000206572 Rhodophyta Species 0.000 description 2
- 108010086873 UDP-N-acetylglucosamine transporter Proteins 0.000 description 2
- 101150050575 URA3 gene Proteins 0.000 description 2
- 101150044776 URA5 gene Proteins 0.000 description 2
- DZBUGLKDJFMEHC-UHFFFAOYSA-N acridine Chemical compound C1=CC=CC2=CC3=CC=CC=C3N=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-N 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 210000004436 artificial bacterial chromosome Anatomy 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 108010005774 beta-Galactosidase Proteins 0.000 description 2
- 239000012148 binding buffer Substances 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 150000001720 carbohydrates Chemical group 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 230000001086 cytosolic effect Effects 0.000 description 2
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical group [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 2
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 239000003623 enhancer Substances 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 239000012467 final product Substances 0.000 description 2
- 239000007789 gas Substances 0.000 description 2
- 238000012239 gene modification Methods 0.000 description 2
- 230000005017 genetic modification Effects 0.000 description 2
- 235000013617 genetically modified food Nutrition 0.000 description 2
- 239000005090 green fluorescent protein Substances 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 238000013537 high throughput screening Methods 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 229960002591 hydroxyproline Drugs 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 239000002054 inoculum Substances 0.000 description 2
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- GUBGYTABKSRVRQ-QKKXKWKRSA-N lactose group Chemical group OC1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@@H](O)[C@H](O2)CO)[C@H](O1)CO GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 2
- KWGKDLIKAYFUFQ-UHFFFAOYSA-M lithium chloride Chemical compound [Li+].[Cl-] KWGKDLIKAYFUFQ-UHFFFAOYSA-M 0.000 description 2
- 230000004807 localization Effects 0.000 description 2
- 238000004949 mass spectrometry Methods 0.000 description 2
- 238000000816 matrix-assisted laser desorption--ionisation Methods 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 230000004060 metabolic process Effects 0.000 description 2
- CERZMXAJYMMUDR-UHFFFAOYSA-N neuraminic acid Natural products NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO CERZMXAJYMMUDR-UHFFFAOYSA-N 0.000 description 2
- 238000007899 nucleic acid hybridization Methods 0.000 description 2
- 108010028546 nucleoside-diphosphatase Proteins 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 239000000816 peptidomimetic Substances 0.000 description 2
- 235000021317 phosphate Nutrition 0.000 description 2
- 230000003389 potentiating effect Effects 0.000 description 2
- 238000000159 protein binding assay Methods 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- ZCCUUQDIBDJBTK-UHFFFAOYSA-N psoralen Chemical compound C1=C2OC(=O)C=CC2=CC2=C1OC=C2 ZCCUUQDIBDJBTK-UHFFFAOYSA-N 0.000 description 2
- 238000003259 recombinant expression Methods 0.000 description 2
- 230000009962 secretion pathway Effects 0.000 description 2
- 238000011218 seed culture Methods 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- 230000007704 transition Effects 0.000 description 2
- 239000001226 triphosphate Substances 0.000 description 2
- 235000011178 triphosphate Nutrition 0.000 description 2
- 239000013603 viral vector Substances 0.000 description 2
- SBKVPJHMSUXZTA-MEJXFZFPSA-N (2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-5-amino-2-[[2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoyl]amino]-5-oxopentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]amino]-4-methylsulfanylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoic acid Chemical 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
- QJXVSNXFASTKDB-PSJDMVPZSA-N 1-[(2R,3S,4R,5R)-5-amino-3,4,6-trihydroxy-2-(hydroxymethyl)oxan-2-yl]ethanone Chemical compound C(C)(=O)[C@]1([C@H]([C@@H]([C@H](C(O)O1)N)O)O)CO QJXVSNXFASTKDB-PSJDMVPZSA-N 0.000 description 1
- ZSUQDICQCXVVKD-UBHLDEDJSA-N 1-[(2S,3S,4R,5R)-5-amino-3,4,6-trihydroxyoxan-2-yl]-1-hydroxypropan-2-one Chemical compound C(C)(=O)C([C@@H]1[C@H]([C@@H]([C@H](C(O)O1)N)O)O)O ZSUQDICQCXVVKD-UBHLDEDJSA-N 0.000 description 1
- WXTMDXOMEHJXQO-UHFFFAOYSA-N 2,5-dihydroxybenzoic acid Chemical compound OC(=O)C1=CC(O)=CC=C1O WXTMDXOMEHJXQO-UHFFFAOYSA-N 0.000 description 1
- PKAUICCNAWQPAU-UHFFFAOYSA-N 2-(4-chloro-2-methylphenoxy)acetic acid;n-methylmethanamine Chemical compound CNC.CC1=CC(Cl)=CC=C1OCC(O)=O PKAUICCNAWQPAU-UHFFFAOYSA-N 0.000 description 1
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
- AAUQLHHARJUJEH-UHFFFAOYSA-N 2-hydroxy-5-methoxybenzoic acid Natural products COC1=CC=CC(O)=C1C(O)=O AAUQLHHARJUJEH-UHFFFAOYSA-N 0.000 description 1
- BRMWTNUJHUMWMS-UHFFFAOYSA-N 3-Methylhistidine Natural products CN1C=NC(CC(N)C(O)=O)=C1 BRMWTNUJHUMWMS-UHFFFAOYSA-N 0.000 description 1
- VXGRJERITKFWPL-UHFFFAOYSA-N 4',5'-Dihydropsoralen Natural products C1=C2OC(=O)C=CC2=CC2=C1OCC2 VXGRJERITKFWPL-UHFFFAOYSA-N 0.000 description 1
- 229940117976 5-hydroxylysine Drugs 0.000 description 1
- 101150006240 AOX2 gene Proteins 0.000 description 1
- 108010006533 ATP-Binding Cassette Transporters Proteins 0.000 description 1
- 102000005416 ATP-Binding Cassette Transporters Human genes 0.000 description 1
- 108091005508 Acid proteases Proteins 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 241000589158 Agrobacterium Species 0.000 description 1
- 101150039297 Alg3 gene Proteins 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 101710180924 Alpha-1,2-galactosyltransferase Proteins 0.000 description 1
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 108010007730 Apyrase Proteins 0.000 description 1
- 102000007347 Apyrase Human genes 0.000 description 1
- 101000776503 Arabidopsis thaliana UDP-rhamnose/UDP-galactose transporter 1 Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 102100022548 Beta-hexosaminidase subunit alpha Human genes 0.000 description 1
- 101001065525 Bos taurus Lysozyme C Proteins 0.000 description 1
- 101100166113 Candida albicans (strain SC5314 / ATCC MYA-2876) SAP9 gene Proteins 0.000 description 1
- 244000237791 Chionanthus virginicus Species 0.000 description 1
- 241000195628 Chlorophyta Species 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 241000199914 Dinophyceae Species 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 102100039371 ER lumen protein-retaining receptor 1 Human genes 0.000 description 1
- 108050001049 Extracellular proteins Proteins 0.000 description 1
- 208000024720 Fabry Disease Diseases 0.000 description 1
- 241000005398 Figaro Species 0.000 description 1
- 101150094690 GAL1 gene Proteins 0.000 description 1
- 101150037782 GAL2 gene Proteins 0.000 description 1
- LQEBEXMHBLQMDB-UHFFFAOYSA-N GDP-L-fucose Natural products OC1C(O)C(O)C(C)OC1OP(O)(=O)OP(O)(=O)OCC1C(O)C(O)C(N2C3=C(C(N=C(N)N3)=O)N=C2)O1 LQEBEXMHBLQMDB-UHFFFAOYSA-N 0.000 description 1
- LQEBEXMHBLQMDB-JGQUBWHWSA-N GDP-beta-L-fucose Chemical compound O[C@H]1[C@H](O)[C@H](O)[C@H](C)O[C@@H]1OP(O)(=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C3=C(C(NC(N)=N3)=O)N=C2)O1 LQEBEXMHBLQMDB-JGQUBWHWSA-N 0.000 description 1
- 101710193897 Galactose transporter Proteins 0.000 description 1
- 101710103223 Galactose-proton symporter Proteins 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- 241000234271 Galanthus Species 0.000 description 1
- 102100039555 Galectin-7 Human genes 0.000 description 1
- 101150102398 Galt gene Proteins 0.000 description 1
- 208000015872 Gaucher disease Diseases 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 102100039847 Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 Human genes 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 108010070675 Glutathione transferase Proteins 0.000 description 1
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 1
- 102000038461 Growth Hormone-Releasing Hormone Human genes 0.000 description 1
- 239000000095 Growth Hormone-Releasing Hormone Substances 0.000 description 1
- 101150009006 HIS3 gene Proteins 0.000 description 1
- 101150069554 HIS4 gene Proteins 0.000 description 1
- 101100246753 Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) pyrF gene Proteins 0.000 description 1
- 102100029100 Hematopoietic prostaglandin D synthase Human genes 0.000 description 1
- 101000812437 Homo sapiens ER lumen protein-retaining receptor 1 Proteins 0.000 description 1
- 101001012435 Homo sapiens Ectonucleoside triphosphate diphosphohydrolase 4 Proteins 0.000 description 1
- 101000608772 Homo sapiens Galectin-7 Proteins 0.000 description 1
- 101000887519 Homo sapiens Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 Proteins 0.000 description 1
- 101001040734 Homo sapiens Golgi phosphoprotein 3 Proteins 0.000 description 1
- 101000739046 Homo sapiens RNA-binding protein PNO1 Proteins 0.000 description 1
- 101150062179 II gene Proteins 0.000 description 1
- 101150098499 III gene Proteins 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-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
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 108010070158 Lactose synthase Proteins 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 208000015439 Lysosomal storage disease Diseases 0.000 description 1
- 101150053531 MNN1 gene Proteins 0.000 description 1
- 101150009164 MNN14 gene Proteins 0.000 description 1
- 101150102717 MNN4 gene Proteins 0.000 description 1
- 229910021380 Manganese Chloride Inorganic materials 0.000 description 1
- GLFNIEUTAYBVOC-UHFFFAOYSA-L Manganese chloride Chemical compound Cl[Mn]Cl GLFNIEUTAYBVOC-UHFFFAOYSA-L 0.000 description 1
- 108010090665 Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Proteins 0.000 description 1
- 108010038049 Mating Factor Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 108010085220 Multiprotein Complexes Proteins 0.000 description 1
- 102000007474 Multiprotein Complexes Human genes 0.000 description 1
- DTERQYGMUDWYAZ-ZETCQYMHSA-N N(6)-acetyl-L-lysine Chemical compound CC(=O)NCCCC[C@H]([NH3+])C([O-])=O DTERQYGMUDWYAZ-ZETCQYMHSA-N 0.000 description 1
- JDHILDINMRGULE-LURJTMIESA-N N(pros)-methyl-L-histidine Chemical compound CN1C=NC=C1C[C@H](N)C(O)=O JDHILDINMRGULE-LURJTMIESA-N 0.000 description 1
- OVRNDRQMDRJTHS-CBQIKETKSA-N N-Acetyl-D-Galactosamine Chemical compound CC(=O)N[C@H]1[C@@H](O)O[C@H](CO)[C@H](O)[C@@H]1O OVRNDRQMDRJTHS-CBQIKETKSA-N 0.000 description 1
- OSKIPPQETUTOMW-YHLOVPAPSA-N N-[(2R,3R,4R,5S,6R)-5-[(2S,3R,4R,5S,6R)-3-Acetamido-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5S,6R)-3-[(2S,3S,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-[[(2S,3S,4S,5R,6R)-6-[[(2S,3S,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxymethyl]-3,5-dihydroxy-4-[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxymethyl]-3,5-dihydroxyoxan-2-yl]oxy-4-hydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-2,4-dihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide Chemical compound O[C@@H]1[C@@H](NC(=O)C)[C@H](O)O[C@H](CO)[C@H]1O[C@H]1[C@H](NC(C)=O)[C@@H](O)[C@H](O[C@@H]2[C@H]([C@@H](O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O)[C@H](O)[C@@H](CO[C@@H]3[C@H]([C@@H](O[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O)[C@H](O)[C@@H](CO[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O)O3)O)O2)O)[C@@H](CO)O1 OSKIPPQETUTOMW-YHLOVPAPSA-N 0.000 description 1
- 125000003047 N-acetyl group Chemical group 0.000 description 1
- JJIHLJJYMXLCOY-BYPYZUCNSA-N N-acetyl-L-serine Chemical compound CC(=O)N[C@@H](CO)C(O)=O JJIHLJJYMXLCOY-BYPYZUCNSA-N 0.000 description 1
- 102100023315 N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase Human genes 0.000 description 1
- 108010056664 N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase Proteins 0.000 description 1
- SQVRNKJHWKZAKO-LUWBGTNYSA-N N-acetylneuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)CC(O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-LUWBGTNYSA-N 0.000 description 1
- PYUSHNKNPOHWEZ-YFKPBYRVSA-N N-formyl-L-methionine Chemical compound CSCC[C@@H](C(O)=O)NC=O PYUSHNKNPOHWEZ-YFKPBYRVSA-N 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 241000244206 Nematoda Species 0.000 description 1
- 108010006232 Neuraminidase Proteins 0.000 description 1
- 102000005348 Neuraminidase Human genes 0.000 description 1
- 241000080590 Niso Species 0.000 description 1
- 108030001281 Nucleotide diphosphatases Proteins 0.000 description 1
- 102100039306 Nucleotide pyrophosphatase Human genes 0.000 description 1
- 102000005823 Nucleotide-sugar transporter Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 101150051118 PTM1 gene Proteins 0.000 description 1
- 101100080112 Parietaria judaica PMAI gene Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102100038551 Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase Human genes 0.000 description 1
- 241000199919 Phaeophyceae Species 0.000 description 1
- 241000530350 Phaffomyces opuntiae Species 0.000 description 1
- 241000529953 Phaffomyces thermotolerans Species 0.000 description 1
- IAJOBQBIJHVGMQ-UHFFFAOYSA-N Phosphinothricin Natural products CP(O)(=O)CCC(N)C(O)=O IAJOBQBIJHVGMQ-UHFFFAOYSA-N 0.000 description 1
- 241000235062 Pichia membranifaciens Species 0.000 description 1
- 241000235061 Pichia sp. Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 101710180012 Protease 7 Proteins 0.000 description 1
- 102100037294 RNA-binding protein PNO1 Human genes 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 1
- WNYXRWJUZBOMBX-UHFFFAOYSA-N SC(=O)c1ccc[pH]1 Chemical compound SC(=O)c1ccc[pH]1 WNYXRWJUZBOMBX-UHFFFAOYSA-N 0.000 description 1
- 101150014136 SUC2 gene Proteins 0.000 description 1
- 101100181264 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) KTR6 gene Proteins 0.000 description 1
- 101100184479 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) MNN4 gene Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 101710142969 Somatoliberin Proteins 0.000 description 1
- 241001466451 Stramenopiles Species 0.000 description 1
- 208000022292 Tay-Sachs disease Diseases 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 241000499912 Trichoderma reesei Species 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 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
- 101710110533 UDP-galactose transporter 1 Proteins 0.000 description 1
- 108010082433 UDP-glucose-hexose-1-phosphate uridylyltransferase Proteins 0.000 description 1
- 101150024327 UGT1 gene Proteins 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 241000269370 Xenopus <genus> Species 0.000 description 1
- 101150008621 YPS1 gene Proteins 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- QPMSXSBEVQLBIL-CZRHPSIPSA-N ac1mix0p Chemical compound C1=CC=C2N(C[C@H](C)CN(C)C)C3=CC(OC)=CC=C3SC2=C1.O([C@H]1[C@]2(OC)C=CC34C[C@@H]2[C@](C)(O)CCC)C2=C5[C@]41CCN(C)[C@@H]3CC5=CC=C2O QPMSXSBEVQLBIL-CZRHPSIPSA-N 0.000 description 1
- 230000001133 acceleration Effects 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 125000000218 acetic acid group Chemical group C(C)(=O)* 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 108091022872 aldose 1-epimerase Proteins 0.000 description 1
- 102000020006 aldose 1-epimerase Human genes 0.000 description 1
- 239000002168 alkylating agent Substances 0.000 description 1
- 229940100198 alkylating agent Drugs 0.000 description 1
- 108010039255 alpha 1,6-mannosyltransferase Proteins 0.000 description 1
- 108010070113 alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase I Proteins 0.000 description 1
- HXXFSFRBOHSIMQ-VFUOTHLCSA-N alpha-D-glucose 1-phosphate Chemical compound OC[C@H]1O[C@H](OP(O)(O)=O)[C@H](O)[C@@H](O)[C@@H]1O HXXFSFRBOHSIMQ-VFUOTHLCSA-N 0.000 description 1
- 108010061314 alpha-L-Fucosidase Proteins 0.000 description 1
- 102000012086 alpha-L-Fucosidase Human genes 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 239000000908 ammonium hydroxide Substances 0.000 description 1
- 230000002337 anti-port Effects 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 108010022308 beta-1,4-galactosyltransferase I Proteins 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 150000004657 carbamic acid derivatives Chemical class 0.000 description 1
- UHBYWPGGCSDKFX-UHFFFAOYSA-N carboxyglutamic acid Chemical compound OC(=O)C(N)CC(C(O)=O)C(O)=O UHBYWPGGCSDKFX-UHFFFAOYSA-N 0.000 description 1
- 230000021523 carboxylation Effects 0.000 description 1
- 238000006473 carboxylation reaction Methods 0.000 description 1
- 210000000748 cardiovascular system Anatomy 0.000 description 1
- 108020001778 catalytic domains Proteins 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 239000012707 chemical precursor Substances 0.000 description 1
- 239000005081 chemiluminescent agent Substances 0.000 description 1
- 238000013375 chromatographic separation Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- YSMODUONRAFBET-UHFFFAOYSA-N delta-DL-hydroxylysine Natural products NCC(O)CCC(N)C(O)=O YSMODUONRAFBET-UHFFFAOYSA-N 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- NAGJZTKCGNOGPW-UHFFFAOYSA-K dioxido-sulfanylidene-sulfido-$l^{5}-phosphane Chemical compound [O-]P([O-])([S-])=S NAGJZTKCGNOGPW-UHFFFAOYSA-K 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 238000006345 epimerization reaction Methods 0.000 description 1
- YSMODUONRAFBET-UHNVWZDZSA-N erythro-5-hydroxy-L-lysine Chemical compound NC[C@H](O)CC[C@H](N)C(O)=O YSMODUONRAFBET-UHNVWZDZSA-N 0.000 description 1
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- 108091006047 fluorescent proteins Proteins 0.000 description 1
- 102000034287 fluorescent proteins Human genes 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 101150002054 galE gene Proteins 0.000 description 1
- 150000002256 galaktoses Chemical class 0.000 description 1
- 101150037231 gda1 gene Proteins 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 229950010772 glucose-1-phosphate Drugs 0.000 description 1
- IAJOBQBIJHVGMQ-BYPYZUCNSA-N glufosinate-P Chemical compound CP(O)(=O)CC[C@H](N)C(O)=O IAJOBQBIJHVGMQ-BYPYZUCNSA-N 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 108010026195 glycanase Proteins 0.000 description 1
- 229930182470 glycoside Natural products 0.000 description 1
- 150000002338 glycosides Chemical class 0.000 description 1
- 125000003147 glycosyl group Chemical group 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 235000003642 hunger Nutrition 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 125000001841 imino group Chemical group [H]N=* 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 210000003712 lysosome Anatomy 0.000 description 1
- 230000001868 lysosomic effect Effects 0.000 description 1
- 239000011565 manganese chloride Substances 0.000 description 1
- 235000002867 manganese chloride Nutrition 0.000 description 1
- 229940099607 manganese chloride Drugs 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
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- CAAULPUQFIIOTL-UHFFFAOYSA-N methyl dihydrogen phosphate Chemical compound COP(O)(O)=O CAAULPUQFIIOTL-UHFFFAOYSA-N 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000000302 molecular modelling Methods 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229940060155 neuac Drugs 0.000 description 1
- 108020003699 nucleotide-sugar transporter Proteins 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000002611 ovarian Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 101150113864 pat gene Proteins 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 108040002068 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity proteins Proteins 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 150000008298 phosphoramidates Chemical class 0.000 description 1
- BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical compound OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 230000001124 posttranscriptional effect Effects 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 230000025098 protein galactosylation Effects 0.000 description 1
- 238000000164 protein isolation Methods 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 238000003345 scintillation counting Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 238000012807 shake-flask culturing Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- MWEMXEWFLIDTSJ-UHFFFAOYSA-M sodium;3-morpholin-4-ylpropane-1-sulfonate Chemical compound [Na+].[O-]S(=O)(=O)CCCN1CCOCC1 MWEMXEWFLIDTSJ-UHFFFAOYSA-M 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 210000001082 somatic cell Anatomy 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000037351 starvation Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 238000001269 time-of-flight mass spectrometry Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 210000003412 trans-golgi network Anatomy 0.000 description 1
- 230000005026 transcription initiation Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000006276 transfer reaction Methods 0.000 description 1
- 238000005820 transferase reaction Methods 0.000 description 1
- 238000000844 transformation Methods 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000010798 ubiquitination Methods 0.000 description 1
- 230000034512 ubiquitination Effects 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 238000007794 visualization technique Methods 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 101150108619 ynd1 gene Proteins 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
- C12N9/1051—Hexosyltransferases (2.4.1)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/37—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi
- C07K14/39—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi from yeasts
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
- A61P5/10—Drugs for disorders of the endocrine system of the posterior pituitary hormones, e.g. oxytocin, ADH
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
- A61P5/24—Drugs for disorders of the endocrine system of the sex hormones
- A61P5/30—Oestrogens
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/04—Antihaemorrhagics; Procoagulants; Haemostatic agents; Antifibrinolytic agents
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/90—Isomerases (5.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/005—Glycopeptides, glycoproteins
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Diabetes (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Hematology (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Endocrinology (AREA)
- Mycology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US56242404P | 2004-04-15 | 2004-04-15 | |
| PCT/IB2005/051249 WO2005100584A2 (en) | 2004-04-15 | 2005-04-15 | Production of galactosylated glycoproteins in lower eukaryotes |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2011157566A Division JP5584660B2 (ja) | 2004-04-15 | 2011-07-19 | 下等真核生物におけるガラクトシル化された糖タンパク質の産生 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JP2007535317A true JP2007535317A (ja) | 2007-12-06 |
Family
ID=35150558
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2007507921A Withdrawn JP2007535317A (ja) | 2004-04-15 | 2005-04-15 | 下等真核生物におけるガラクトシル化された糖タンパク質の産生 |
| JP2011157566A Expired - Fee Related JP5584660B2 (ja) | 2004-04-15 | 2011-07-19 | 下等真核生物におけるガラクトシル化された糖タンパク質の産生 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2011157566A Expired - Fee Related JP5584660B2 (ja) | 2004-04-15 | 2011-07-19 | 下等真核生物におけるガラクトシル化された糖タンパク質の産生 |
Country Status (6)
| Country | Link |
|---|---|
| EP (1) | EP1737969B2 (https=) |
| JP (2) | JP2007535317A (https=) |
| CN (2) | CN1950496B (https=) |
| AU (1) | AU2005233387B2 (https=) |
| CA (1) | CA2562772A1 (https=) |
| WO (1) | WO2005100584A2 (https=) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2012518419A (ja) * | 2009-02-25 | 2012-08-16 | メルク・シャープ・エンド・ドーム・コーポレイション | 糖操作酵母ピチア・パストリスにおけるガラクトース同化経路の代謝操作 |
| JP2012527223A (ja) * | 2009-05-28 | 2012-11-08 | イーティーエイチ・チューリッヒ | Ｎ−グリカンコアβ−ガラクトシルトランスフェラーゼおよびその使用 |
| JP2013511272A (ja) * | 2009-11-19 | 2013-04-04 | オキシレイン ユーケー リミテッド | 哺乳類様複合ｎ−グリカンを生成する酵母株 |
| JP2021168671A (ja) * | 2011-06-07 | 2021-10-28 | キッコーマン株式会社 | フラビン結合型グルコースデヒドロゲナーゼ、フラビン結合型グルコースデヒドロゲナーゼの製造方法、およびそれを用いたグルコース測定方法 |
Families Citing this family (104)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7449308B2 (en) | 2000-06-28 | 2008-11-11 | Glycofi, Inc. | Combinatorial DNA library for producing modified N-glycans in lower eukaryotes |
| ES2252261T3 (es) | 2000-06-28 | 2006-05-16 | Glycofi, Inc. | Metodos para producir glicoproteinas modificadas. |
| US7981420B2 (en) | 2000-12-22 | 2011-07-19 | Max-Planck-Gesellschaft Zur Foederung Der Wissenschaften E.V. | Therapeutic use of antibodies directed against repulsive guidance molecule (RGM) |
| DE10303974A1 (de) | 2003-01-31 | 2004-08-05 | Abbott Gmbh & Co. Kg | Amyloid-β(1-42)-Oligomere, Verfahren zu deren Herstellung und deren Verwendung |
| US7332299B2 (en) | 2003-02-20 | 2008-02-19 | Glycofi, Inc. | Endomannosidases in the modification of glycoproteins in eukaryotes |
| US7507573B2 (en) * | 2003-11-14 | 2009-03-24 | Vib, Vzw | Modification of protein glycosylation in methylotrophic yeast |
| CN103145842A (zh) | 2005-06-30 | 2013-06-12 | Abbvie公司 | Il-12/p40结合蛋白 |
| NZ612578A (en) | 2005-08-19 | 2014-11-28 | Abbvie Inc | Dual variable domain immunoglobin and uses thereof |
| EP2500355A3 (en) | 2005-08-19 | 2012-10-24 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| US7612181B2 (en) | 2005-08-19 | 2009-11-03 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| EP1928905B1 (de) | 2005-09-30 | 2015-04-15 | AbbVie Deutschland GmbH & Co KG | Bindungsdomänen von proteinen der repulsive guidance molecule (rgm) proteinfamilie und funktionale fragmente davon sowie deren verwendung |
| HRP20140240T4 (hr) | 2005-11-30 | 2017-02-24 | Abbvie Inc. | Monoklonalna antitijela protiv amiloidnih beta proteina i njihova upotreba |
| US8691224B2 (en) | 2005-11-30 | 2014-04-08 | Abbvie Inc. | Anti-Aβ globulomer 5F7 antibodies |
| JP5110563B2 (ja) * | 2006-03-03 | 2012-12-26 | 独立行政法人産業技術総合研究所 | ムチン型糖鎖結合タンパク質の製造方法 |
| JP2010502224A (ja) | 2006-09-08 | 2010-01-28 | アボット・ラボラトリーズ | インターロイキン１３結合タンパク質 |
| US8455626B2 (en) | 2006-11-30 | 2013-06-04 | Abbott Laboratories | Aβ conformer selective anti-aβ globulomer monoclonal antibodies |
| US8895004B2 (en) | 2007-02-27 | 2014-11-25 | AbbVie Deutschland GmbH & Co. KG | Method for the treatment of amyloidoses |
| CA2887752C (en) | 2007-04-03 | 2020-03-24 | Vib Vzw | Glycosylation of molecules |
| IL182956A0 (en) * | 2007-05-03 | 2008-01-20 | Yeda Res & Dev | Glycan modified soluble receptors and binding proteins and their use |
| US8962803B2 (en) | 2008-02-29 | 2015-02-24 | AbbVie Deutschland GmbH & Co. KG | Antibodies against the RGM A protein and uses thereof |
| SG190572A1 (en) | 2008-04-29 | 2013-06-28 | Abbott Lab | Dual variable domain immunoglobulins and uses thereof |
| EP2116556B1 (en) | 2008-05-09 | 2016-03-23 | AbbVie Deutschland GmbH & Co KG | Antibodies to receptor of advanced glycation end products (RAGE) and uses thereof |
| TW201006485A (en) | 2008-06-03 | 2010-02-16 | Abbott Lab | Dual variable domain immunoglobulins and uses thereof |
| CA2726087A1 (en) | 2008-06-03 | 2009-12-10 | Tariq Ghayur | Dual variable domain immunoglobulins and uses thereof |
| CN102149825B (zh) | 2008-07-08 | 2015-07-22 | Abbvie公司 | 前列腺素e2双重可变结构域免疫球蛋白及其用途 |
| TW201014602A (en) | 2008-07-08 | 2010-04-16 | Abbott Lab | Prostaglandin E2 binding proteins and uses thereof |
| US8030026B2 (en) | 2009-02-24 | 2011-10-04 | Abbott Laboratories | Antibodies to troponin I and methods of use thereof |
| US8283162B2 (en) | 2009-03-10 | 2012-10-09 | Abbott Laboratories | Antibodies relating to PIVKAII and uses thereof |
| WO2011028811A2 (en) | 2009-09-01 | 2011-03-10 | Abbott Laboratories | Dual variable domain immunoglobulins and uses thereof |
| KR102000383B1 (ko) | 2009-09-29 | 2019-07-15 | 유니버시테이트 젠트 | 만노스-1-포스포-6-만노스 결합의 포스포-6-만노스로의 가수분해 |
| BR112012008833A2 (pt) | 2009-10-15 | 2015-09-08 | Abbott Lab | imunoglobulinas de dominio variavel duplo e usos das mesmas |
| UY32979A (es) | 2009-10-28 | 2011-02-28 | Abbott Lab | Inmunoglobulinas con dominio variable dual y usos de las mismas |
| WO2011053707A1 (en) | 2009-10-31 | 2011-05-05 | Abbott Laboratories | Antibodies to receptor for advanced glycation end products (rage) and uses thereof |
| MX2012006560A (es) | 2009-12-08 | 2012-10-05 | Abbott Gmbh & Co Kg | Anticuerpos monoclonales contra la proteina rgm a para utilizarse en el tratamiento de degeneracion de capa de fibra de nervio retinal. |
| US8987419B2 (en) | 2010-04-15 | 2015-03-24 | AbbVie Deutschland GmbH & Co. KG | Amyloid-beta binding proteins |
| AR081246A1 (es) | 2010-05-14 | 2012-07-18 | Abbott Lab | Proteinas de union a il-1 |
| CN102030823A (zh) * | 2010-06-21 | 2011-04-27 | 中国人民解放军军事医学科学院放射与辐射医学研究所 | 一种肝脏靶向性的基因工程干扰素及其制备方法 |
| WO2012006500A2 (en) | 2010-07-08 | 2012-01-12 | Abbott Laboratories | Monoclonal antibodies against hepatitis c virus core protein |
| UY33492A (es) | 2010-07-09 | 2012-01-31 | Abbott Lab | Inmunoglobulinas con dominio variable dual y usos de las mismas |
| US9120862B2 (en) | 2010-07-26 | 2015-09-01 | Abbott Laboratories | Antibodies relating to PIVKA-II and uses thereof |
| EP3252072A3 (en) | 2010-08-03 | 2018-03-14 | AbbVie Inc. | Dual variable domain immunoglobulins and uses thereof |
| EP3533803B1 (en) | 2010-08-14 | 2021-10-27 | AbbVie Inc. | Anti-amyloid-beta antibodies |
| JP2013539364A (ja) | 2010-08-26 | 2013-10-24 | アッヴィ・インコーポレイテッド | 二重可変ドメイン免疫グロブリンおよびその使用 |
| CA2812872C (en) | 2010-09-29 | 2021-08-03 | Oxyrane Uk Limited | De-mannosylation of phosphorylated n-glycans |
| US9347050B2 (en) | 2010-09-29 | 2016-05-24 | Oxyrane Uk Limited | Mannosidases capable of uncapping mannose-1-phospho-6-mannose linkages and demannosylating phosphorylated N-glycans and methods of facilitating mammalian cellular uptake of glycoproteins |
| PE20141060A1 (es) | 2010-12-21 | 2014-09-26 | Abbvie Inc | Inmunoglobulinas de dominio variable dual biespecificas de il-1 alfa y beta y su uso |
| US9062106B2 (en) | 2011-04-27 | 2015-06-23 | Abbvie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| SG10201505454SA (en) | 2011-07-13 | 2015-09-29 | Abbvie Inc | Methods and compositions for treating asthma using anti-il-13 antibodies |
| CN103827134A (zh) | 2011-07-20 | 2014-05-28 | 泽普泰恩股份有限公司 | 多肽分离方法 |
| TW201333035A (zh) | 2011-12-30 | 2013-08-16 | Abbvie Inc | 針對ｉｌ－１３及／或ｉｌ－１７之雙特異性結合蛋白 |
| EP3369746A1 (en) | 2012-01-27 | 2018-09-05 | AbbVie Deutschland GmbH & Co KG | Composition and method for diagnosis and treatment of diseases associated with neurite degeneration |
| EP3628326B1 (en) | 2012-03-15 | 2024-02-28 | Oxyrane UK Limited | Methods and materials for treatment of pompe's disease |
| WO2013158273A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Methods to modulate c-terminal lysine variant distribution |
| WO2013158279A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Protein purification methods to reduce acidic species |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| TW201808342A (zh) | 2012-05-02 | 2018-03-16 | 喜納製藥公司 | 包含四ｇａｌｎａｃ之新穎結合物及傳送寡核苷酸之方法 |
| AR090905A1 (es) | 2012-05-02 | 2014-12-17 | Merck Sharp & Dohme | Conjugados que contienen tetragalnac y peptidos y procedimientos para la administracion de oligonucleotidos, composicion farmaceutica |
| UY34905A (es) | 2012-07-12 | 2014-01-31 | Abbvie Inc | Proteínas de unión a il-1 |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| TW202037609A (zh) | 2012-11-01 | 2020-10-16 | 美商艾伯維有限公司 | 抗-vegf/dll4雙重可變區域免疫球蛋白及其用途 |
| US9550986B2 (en) | 2012-12-21 | 2017-01-24 | Abbvie Inc. | High-throughput antibody humanization |
| US9458244B2 (en) | 2012-12-28 | 2016-10-04 | Abbvie Inc. | Single chain multivalent binding protein compositions and methods |
| WO2014106015A2 (en) | 2012-12-28 | 2014-07-03 | Abbvie, Inc. | Multivalent binding protein compositions |
| EP2948177A1 (en) | 2013-01-22 | 2015-12-02 | AbbVie Inc. | Methods for optimizing domain stability of binding proteins |
| HK1207960A1 (en) | 2013-03-12 | 2016-02-19 | Abbvie Inc. | Human antibodies that bind human tnf-alpha and methods of preparing the same |
| MX362075B (es) | 2013-03-14 | 2019-01-07 | Abbott Lab | Ensayo de combinación de antígeno-anticuerpo del virus de la hepatitis c (vhc) y métodos y composiciones para usarlo. |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| JP2016512241A (ja) | 2013-03-14 | 2016-04-25 | アボット・ラボラトリーズＡｂｂｏｔｔ Ｌａｂｏｒａｔｏｒｉｅｓ | 改良された抗体検出のためのｈｃｖｎｓ３組換え抗原およびこの突然変異体 |
| US9499614B2 (en) | 2013-03-14 | 2016-11-22 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosaccharides |
| WO2014143343A1 (en) | 2013-03-14 | 2014-09-18 | Abbott Laboratories | Hcv core lipid binding domain monoclonal antibodies |
| WO2014144280A2 (en) | 2013-03-15 | 2014-09-18 | Abbvie Inc. | DUAL SPECIFIC BINDING PROTEINS DIRECTED AGAINST IL-1β AND / OR IL-17 |
| US9598667B2 (en) | 2013-10-04 | 2017-03-21 | Abbvie Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US20150139988A1 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| AR099812A1 (es) | 2014-03-21 | 2016-08-17 | Abbvie Inc | Anticuerpos y conjugados de anticuerpo y fármaco anti-egfr |
| US10093733B2 (en) | 2014-12-11 | 2018-10-09 | Abbvie Inc. | LRP-8 binding dual variable domain immunoglobulin proteins |
| WO2016160976A2 (en) | 2015-03-30 | 2016-10-06 | Abbvie Inc. | Monovalent tnf binding proteins |
| CN107810198B (zh) | 2015-05-29 | 2021-09-03 | 艾伯维公司 | 抗cd40抗体及其用途 |
| TW201710286A (zh) | 2015-06-15 | 2017-03-16 | 艾伯維有限公司 | 抗ｖｅｇｆ、ｐｄｇｆ及／或其受體之結合蛋白 |
| AU2017279550A1 (en) | 2016-06-08 | 2019-01-03 | Abbvie Inc. | Anti-B7-H3 antibodies and antibody drug conjugates |
| RU2018147224A (ru) | 2016-06-08 | 2020-07-14 | Эббви Инк. | Конъюгаты антитела к egfr и лекарственного средства |
| MX2018015285A (es) | 2016-06-08 | 2019-09-18 | Abbvie Inc | Anticuerpos anti-b7-h3 y conjugados de anticuerpo y farmaco. |
| WO2017214322A1 (en) | 2016-06-08 | 2017-12-14 | Abbvie Inc. | Anti-b7-h3 antibodies and antibody drug conjugates |
| WO2017214462A2 (en) | 2016-06-08 | 2017-12-14 | Abbvie Inc. | Anti-cd98 antibodies and antibody drug conjugates |
| US20200147235A1 (en) | 2016-06-08 | 2020-05-14 | Abbvie Inc. | Anti-cd98 antibodies and antibody drug conjugates |
| JP2019524651A (ja) | 2016-06-08 | 2019-09-05 | アッヴィ・インコーポレイテッド | 抗ｃｄ９８抗体及び抗体薬物コンジュゲート |
| BR112018075639A2 (pt) | 2016-06-08 | 2019-04-09 | Abbvie Inc. | conjugados de anticorpo fármaco anti-egfr |
| AU2017277534A1 (en) | 2016-06-08 | 2019-01-03 | Abbvie Inc. | Anti-EGFR antibody drug conjugates |
| EP3544628A4 (en) | 2016-11-23 | 2020-11-18 | Immunoah Therapeutics, Inc. | 4-1BB BINDING PROTEINS AND THEIR USES |
| EP3554544A4 (en) | 2016-12-16 | 2020-07-29 | Bluefin Biomedicine, Inc. | ANTI-PROTEIN 1 ANTIBODY CONTAINING AN ANTI-CUB DOMAIN (CDCP1), ANTIBODY-DRUG CONJUGATES AND THEIR METHODS OF USE |
| EP3612567B1 (en) | 2017-04-19 | 2024-09-11 | Bluefin Biomedicine, Inc. | Anti-vtcn1 antibodies and antibody drug conjugates |
| CA3066918A1 (en) | 2017-06-12 | 2018-12-20 | Bluefin Biomedicine, Inc. | Anti-il1rap antibodies and antibody drug conjugates |
| WO2020033827A1 (en) * | 2018-08-10 | 2020-02-13 | Genentech, Inc. | Cell culture strategies for modulating protein glycosylation |
| JP7591501B2 (ja) * | 2018-12-04 | 2024-11-28 | グリコム・アクティーゼルスカブ | フコシル化オリゴ糖の合成 |
| KR20220137698A (ko) | 2020-02-05 | 2022-10-12 | 라리마 테라퓨틱스, 인코포레이티드 | Tat 펩티드 결합 단백질 및 이의 용도 |
| AR124681A1 (es) | 2021-01-20 | 2023-04-26 | Abbvie Inc | Conjugados anticuerpo-fármaco anti-egfr |
| WO2022221163A1 (en) * | 2021-04-16 | 2022-10-20 | Merck Sharp & Dohme Llc | Solid-phase glycan remodeling of glycoproteins |
| CN113265434B (zh) * | 2021-05-19 | 2023-05-02 | 吉林大学 | 一种合成udp-半乳糖及合成半乳糖基化合物的方法 |
| DK4186529T3 (da) | 2021-11-25 | 2025-08-25 | Veraxa Biotech Gmbh | Forbedrede antistof-payload-konjugater (apc) fremstillet ved stedspecifik konjugering ved hjælp af genetisk kodeudvidelse |
| WO2023094525A1 (en) | 2021-11-25 | 2023-06-01 | Veraxa Biotech Gmbh | Improved antibody-payload conjugates (apcs) prepared by site-specific conjugation utilizing genetic code expansion |
| CN114507658B (zh) * | 2022-04-02 | 2022-07-05 | 深圳瑞德林生物技术有限公司 | 酶共表达系统及其在合成唾液酸的应用 |
| WO2025027529A1 (en) | 2023-07-31 | 2025-02-06 | Advesya | Anti-il-1rap antibody drug conjugates and methods of use thereof |
| TW202530255A (zh) | 2023-12-15 | 2025-08-01 | 法商亞維西亞有限公司 | 抗ｉｌ－１ｒａｐ結合結構域及其抗體－藥物偶聯物 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5834251A (en) * | 1994-12-30 | 1998-11-10 | Alko Group Ltd. | Methods of modifying carbohydrate moieties |
| WO2000034490A1 (en) * | 1998-12-09 | 2000-06-15 | Tatsuji Seki | A method for manufacturing glycoproteins having human-type glycosylation |
| WO2002057468A2 (en) * | 2001-01-19 | 2002-07-25 | The Dow Chemical Company | Method for secretory production of glycoprotein having human-type sugar chain using plant cell |
| WO2003035835A2 (en) * | 2001-10-25 | 2003-05-01 | Genentech, Inc. | Glycoprotein compositions |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6528286B1 (en) * | 1998-05-29 | 2003-03-04 | Genentech, Inc. | Mammalian cell culture process for producing glycoproteins |
| US20020012979A1 (en) * | 1998-06-08 | 2002-01-31 | Alan Berry | Vitamin c production in microorganisms and plants |
| DE60032370T2 (de) * | 1999-08-19 | 2007-10-11 | Kirin Beer K.K. | Hefevarianten und verfahren zur herstellung von glykoprotein enthaltenden zuckerketten vom säugetiertyp |
| DE60044858D1 (de) † | 1999-10-26 | 2010-09-30 | Stichting Dienst Landbouwkundi | Säugetierartige Glykosylierung in Pflanzen |
| CN1331290A (zh) * | 2000-06-26 | 2002-01-16 | 上海博德基因开发有限公司 | 一种新的多肽——人β－1,4半乳糖苷转运酶18.59和编码这种多肽的多核苷酸 |
| ES2252261T3 (es) * | 2000-06-28 | 2006-05-16 | Glycofi, Inc. | Metodos para producir glicoproteinas modificadas. |
| US7449308B2 (en) † | 2000-06-28 | 2008-11-11 | Glycofi, Inc. | Combinatorial DNA library for producing modified N-glycans in lower eukaryotes |
| US6800739B2 (en) * | 2001-04-05 | 2004-10-05 | Davisco Foods International, Inc. | Isolation of glycoproteins from bovine milk |
| CA2471551C (en) * | 2001-12-27 | 2014-09-30 | Glycofi, Inc. | Methods to engineer mammalian-type carbohydrate structures |
-
2005
- 2005-04-15 AU AU2005233387A patent/AU2005233387B2/en not_active Ceased
- 2005-04-15 JP JP2007507921A patent/JP2007535317A/ja not_active Withdrawn
- 2005-04-15 WO PCT/IB2005/051249 patent/WO2005100584A2/en not_active Ceased
- 2005-04-15 EP EP05732293.5A patent/EP1737969B2/en not_active Expired - Lifetime
- 2005-04-15 CN CN200580011116.4A patent/CN1950496B/zh not_active Expired - Fee Related
- 2005-04-15 CA CA002562772A patent/CA2562772A1/en not_active Abandoned
- 2005-04-15 CN CN201510004041.2A patent/CN104611245A/zh active Pending
-
2011
- 2011-07-19 JP JP2011157566A patent/JP5584660B2/ja not_active Expired - Fee Related
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5834251A (en) * | 1994-12-30 | 1998-11-10 | Alko Group Ltd. | Methods of modifying carbohydrate moieties |
| WO2000034490A1 (en) * | 1998-12-09 | 2000-06-15 | Tatsuji Seki | A method for manufacturing glycoproteins having human-type glycosylation |
| WO2002057468A2 (en) * | 2001-01-19 | 2002-07-25 | The Dow Chemical Company | Method for secretory production of glycoprotein having human-type sugar chain using plant cell |
| WO2003035835A2 (en) * | 2001-10-25 | 2003-05-01 | Genentech, Inc. | Glycoprotein compositions |
Non-Patent Citations (8)
| Title |
|---|
| DATABASE GENBANK, ACCESSION NO.AF022382, 12-MAR-1998 UPLOADED，, JPN6011002243, ISSN: 0001826852 * |
| DATABASE GENBANK, ACCESSION NO.M12999, 27-APR-1993 UPLOADED，, JPN6011002242, ISSN: 0001826851 * |
| DATABASE GENBANK, ACCESSION NO.M81879, 27-APR-1993 UPLOADED，, JPN6011002241, ISSN: 0001826850 * |
| DATABASE GENBANK, ACCESSION NO.MM70427, 23-MAY-1996 UPLOADED, JPN6011002236, ISSN: 0001826846 * |
| GLYCOBIOLOGY, VOL.14, P.399-407 (MARCH 19, 2004), JPN6011002239, ISSN: 0001826848 * |
| GLYCOBIOLOGY, VOL.14, P.757-766 (2004 SEPT), JPN6011002237, ISSN: 0001826853 * |
| SCIENCE, VOL.301, P.1244-1246 (2003), JPN6011002238, ISSN: 0001826847 * |
| 蛋白質核酸酵素,第43巻(1998),2604-2610頁, JPN6011002240, ISSN: 0001826849 * |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2012518419A (ja) * | 2009-02-25 | 2012-08-16 | メルク・シャープ・エンド・ドーム・コーポレイション | 糖操作酵母ピチア・パストリスにおけるガラクトース同化経路の代謝操作 |
| JP2012527223A (ja) * | 2009-05-28 | 2012-11-08 | イーティーエイチ・チューリッヒ | Ｎ−グリカンコアβ−ガラクトシルトランスフェラーゼおよびその使用 |
| JP2013511272A (ja) * | 2009-11-19 | 2013-04-04 | オキシレイン ユーケー リミテッド | 哺乳類様複合ｎ−グリカンを生成する酵母株 |
| JP2021168671A (ja) * | 2011-06-07 | 2021-10-28 | キッコーマン株式会社 | フラビン結合型グルコースデヒドロゲナーゼ、フラビン結合型グルコースデヒドロゲナーゼの製造方法、およびそれを用いたグルコース測定方法 |
| JP2023175795A (ja) * | 2011-06-07 | 2023-12-12 | キッコーマン株式会社 | フラビン結合型グルコースデヒドロゲナーゼ、フラビン結合型グルコースデヒドロゲナーゼの製造方法、およびそれを用いたグルコース測定方法 |
Also Published As
| Publication number | Publication date |
|---|---|
| CN104611245A (zh) | 2015-05-13 |
| EP1737969A2 (en) | 2007-01-03 |
| CN1950496B (zh) | 2015-02-04 |
| WO2005100584A3 (en) | 2006-12-21 |
| JP5584660B2 (ja) | 2014-09-03 |
| EP1737969A4 (en) | 2011-09-28 |
| JP2011254822A (ja) | 2011-12-22 |
| CN1950496A (zh) | 2007-04-18 |
| EP1737969B2 (en) | 2018-09-12 |
| EP1737969B1 (en) | 2015-06-17 |
| WO2005100584A2 (en) | 2005-10-27 |
| AU2005233387B2 (en) | 2011-05-26 |
| AU2005233387A1 (en) | 2005-10-27 |
| CA2562772A1 (en) | 2005-10-27 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP5584660B2 (ja) | 下等真核生物におけるガラクトシル化された糖タンパク質の産生 | |
| US7795002B2 (en) | Production of galactosylated glycoproteins in lower eukaryotes | |
| AU2004213868B2 (en) | Production of modified glycoproteins having multiple antennary structures | |
| JP5514541B2 (ja) | 下等真核生物におけるシアル酸付加ｎ−グリカンの産生 | |
| ES2399736T3 (es) | Expresión de manosidasa de clase 2 y manosidasa de clase III en células eucariotas inferiores | |
| US8067551B2 (en) | Combinatorial DNA library for producing modified N-glycans in lower eukaryotes | |
| US8697394B2 (en) | Production of modified glycoproteins having multiple antennary structures | |
| AU2011205185B2 (en) | Production of galactosylated glycoproteins in lower eukaryotes |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20080407 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20110118 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20110412 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20110419 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20110719 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20110816 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20111215 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20111216 |
|
| A761 | Written withdrawal of application |
Free format text: JAPANESE INTERMEDIATE CODE: A761 Effective date: 20120321 |