CA2764370C - Fucosylation-deficient cells - Google Patents
Fucosylation-deficient cells Download PDFInfo
- Publication number
- CA2764370C CA2764370C CA2764370A CA2764370A CA2764370C CA 2764370 C CA2764370 C CA 2764370C CA 2764370 A CA2764370 A CA 2764370A CA 2764370 A CA2764370 A CA 2764370A CA 2764370 C CA2764370 C CA 2764370C
- Authority
- CA
- Canada
- Prior art keywords
- cell
- glycoprotein
- protein
- modification
- amino acid
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 230000033581 fucosylation Effects 0.000 title claims abstract description 141
- 230000002950 deficient Effects 0.000 title description 4
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 160
- 102000003886 Glycoproteins Human genes 0.000 claims abstract description 159
- 108090000288 Glycoproteins Proteins 0.000 claims abstract description 159
- 101001030665 Dictyostelium discoideum GDP-L-fucose synthase Proteins 0.000 claims abstract description 78
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 54
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 37
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 37
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims abstract description 30
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 claims abstract description 30
- 238000000034 method Methods 0.000 claims abstract description 29
- 239000004475 Arginine Substances 0.000 claims abstract description 12
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims abstract description 12
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims abstract description 12
- 239000004472 Lysine Substances 0.000 claims abstract description 12
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims abstract description 12
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 claims abstract description 12
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 claims abstract description 12
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 claims abstract description 12
- 210000004027 cell Anatomy 0.000 claims description 508
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical compound C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 claims description 125
- 230000004048 modification Effects 0.000 claims description 115
- 238000012986 modification Methods 0.000 claims description 115
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 claims description 114
- 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 101
- 102000004169 proteins and genes Human genes 0.000 claims description 85
- 150000001413 amino acids Chemical class 0.000 claims description 33
- 108060003951 Immunoglobulin Proteins 0.000 claims description 27
- 102000018358 immunoglobulin Human genes 0.000 claims description 27
- 238000006467 substitution reaction Methods 0.000 claims description 25
- 241000699802 Cricetulus griseus Species 0.000 claims description 18
- 241000699666 Mus <mouse, genus> Species 0.000 claims description 16
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 15
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 15
- 210000004962 mammalian cell Anatomy 0.000 claims description 12
- 241000700159 Rattus Species 0.000 claims description 9
- 238000012258 culturing Methods 0.000 claims description 8
- 241000282693 Cercopithecidae Species 0.000 claims description 6
- 210000001672 ovary Anatomy 0.000 claims description 6
- 241000699800 Cricetinae Species 0.000 claims description 5
- 229910052799 carbon Inorganic materials 0.000 claims description 3
- 239000002773 nucleotide Substances 0.000 claims 6
- 125000003729 nucleotide group Chemical group 0.000 claims 6
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims 2
- 101001052793 Homo sapiens GDP-L-fucose synthase Proteins 0.000 claims 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 claims 2
- 102000050085 human TSTA3 Human genes 0.000 claims 2
- 239000000203 mixture Substances 0.000 abstract description 13
- 241000282414 Homo sapiens Species 0.000 description 47
- 150000004676 glycans Chemical class 0.000 description 43
- 230000037361 pathway Effects 0.000 description 42
- 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 33
- 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 32
- 108010034897 lentil lectin Proteins 0.000 description 24
- 230000000694 effects Effects 0.000 description 23
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 21
- 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 19
- 230000015572 biosynthetic process Effects 0.000 description 19
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 19
- 239000002609 medium Substances 0.000 description 18
- 102000014914 Carrier Proteins Human genes 0.000 description 16
- 108010062427 GDP-mannose 4,6-dehydratase Proteins 0.000 description 16
- 102000002312 GDPmannose 4,6-dehydratase Human genes 0.000 description 16
- 108091008324 binding proteins Proteins 0.000 description 16
- 230000035772 mutation Effects 0.000 description 16
- 239000013598 vector Substances 0.000 description 16
- 238000004128 high performance liquid chromatography Methods 0.000 description 15
- RWZYAGGXGHYGMB-UHFFFAOYSA-N anthranilic acid Chemical compound NC1=CC=CC=C1C(O)=O RWZYAGGXGHYGMB-UHFFFAOYSA-N 0.000 description 14
- 101000819490 Homo sapiens Alpha-(1,6)-fucosyltransferase Proteins 0.000 description 13
- SHZGCJCMOBCMKK-PQMKYFCFSA-N L-Fucose Natural products C[C@H]1O[C@H](O)[C@@H](O)[C@@H](O)[C@@H]1O SHZGCJCMOBCMKK-PQMKYFCFSA-N 0.000 description 13
- PNNNRSAQSRJVSB-UHFFFAOYSA-N L-rhamnose Natural products CC(O)C(O)C(O)C(O)C=O PNNNRSAQSRJVSB-UHFFFAOYSA-N 0.000 description 13
- 238000002360 preparation method Methods 0.000 description 13
- 230000009467 reduction Effects 0.000 description 13
- 238000010186 staining Methods 0.000 description 13
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 12
- 108010048367 enhanced green fluorescent protein Proteins 0.000 description 12
- 238000012239 gene modification Methods 0.000 description 12
- 108700028369 Alleles Proteins 0.000 description 11
- 102100021266 Alpha-(1,6)-fucosyltransferase Human genes 0.000 description 11
- 102220354163 c.270T>G Human genes 0.000 description 11
- 238000004949 mass spectrometry Methods 0.000 description 11
- 238000003786 synthesis reaction Methods 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- 101710203794 GDP-fucose transporter Proteins 0.000 description 10
- 230000012478 N-glycan fucosylation Effects 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- 238000000684 flow cytometry Methods 0.000 description 9
- 102200077457 rs36088178 Human genes 0.000 description 9
- 230000008685 targeting Effects 0.000 description 9
- 108020004684 Internal Ribosome Entry Sites Proteins 0.000 description 8
- 102000025171 antigen binding proteins Human genes 0.000 description 8
- 108091000831 antigen binding proteins Proteins 0.000 description 8
- 125000000311 mannosyl group Chemical group C1([C@@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 8
- 102200058952 rs121909543 Human genes 0.000 description 8
- 102220041685 rs587780689 Human genes 0.000 description 8
- 108700026220 vif Genes Proteins 0.000 description 8
- 239000002299 complementary DNA Substances 0.000 description 7
- 239000012634 fragment Substances 0.000 description 7
- 238000004519 manufacturing process Methods 0.000 description 7
- 229920001542 oligosaccharide Polymers 0.000 description 7
- 150000002482 oligosaccharides Chemical class 0.000 description 7
- 238000000926 separation method Methods 0.000 description 7
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 6
- 239000001963 growth medium Substances 0.000 description 6
- 229940041290 mannose Drugs 0.000 description 6
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 6
- 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 5
- MVMSCBBUIHUTGJ-GDJBGNAASA-N GDP-alpha-D-mannose Chemical compound C([C@H]1O[C@H]([C@@H]([C@@H]1O)O)N1C=2N=C(NC(=O)C=2N=C1)N)OP(O)(=O)OP(O)(=O)O[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]1O MVMSCBBUIHUTGJ-GDJBGNAASA-N 0.000 description 5
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 5
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 5
- 239000000427 antigen Substances 0.000 description 5
- 108091007433 antigens Proteins 0.000 description 5
- 102000036639 antigens Human genes 0.000 description 5
- OEYIOHPDSNJKLS-UHFFFAOYSA-N choline Chemical compound C[N+](C)(C)CCO OEYIOHPDSNJKLS-UHFFFAOYSA-N 0.000 description 5
- 229960001231 choline Drugs 0.000 description 5
- 239000010432 diamond Substances 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- 239000000725 suspension Substances 0.000 description 5
- MVMSCBBUIHUTGJ-UHFFFAOYSA-N 10108-97-1 Natural products C1=2NC(N)=NC(=O)C=2N=CN1C(C(C1O)O)OC1COP(O)(=O)OP(O)(=O)OC1OC(CO)C(O)C(O)C1O MVMSCBBUIHUTGJ-UHFFFAOYSA-N 0.000 description 4
- 108010087819 Fc receptors Proteins 0.000 description 4
- 102000009109 Fc receptors Human genes 0.000 description 4
- 108010019236 Fucosyltransferases Proteins 0.000 description 4
- 102000000447 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Human genes 0.000 description 4
- 108010055817 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Proteins 0.000 description 4
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 4
- 239000003636 conditioned culture medium Substances 0.000 description 4
- 108010021843 fluorescent protein 583 Proteins 0.000 description 4
- 230000013595 glycosylation Effects 0.000 description 4
- 238000006206 glycosylation reaction Methods 0.000 description 4
- 238000001819 mass spectrum Methods 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 230000002207 retinal effect Effects 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 108091005942 ECFP Proteins 0.000 description 3
- 102000006471 Fucosyltransferases Human genes 0.000 description 3
- PNHLMHWWFOPQLK-BKUUWRAGSA-N GDP-4-dehydro-6-deoxy-alpha-D-mannose Chemical compound O[C@H]1[C@@H](O)C(=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 PNHLMHWWFOPQLK-BKUUWRAGSA-N 0.000 description 3
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 3
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 3
- 241000124008 Mammalia Species 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 241000282320 Panthera leo Species 0.000 description 3
- 241000700157 Rattus norvegicus Species 0.000 description 3
- PZBFGYYEXUXCOF-UHFFFAOYSA-N TCEP Chemical compound OC(=O)CCP(CCC(O)=O)CCC(O)=O PZBFGYYEXUXCOF-UHFFFAOYSA-N 0.000 description 3
- HXXFSFRBOHSIMQ-RWOPYEJCSA-N alpha-D-mannose 1-phosphate Chemical compound OC[C@H]1O[C@H](OP(O)(O)=O)[C@@H](O)[C@@H](O)[C@@H]1O HXXFSFRBOHSIMQ-RWOPYEJCSA-N 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 230000008827 biological function Effects 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- 230000010354 integration Effects 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 229950010131 puromycin Drugs 0.000 description 3
- 239000012679 serum free medium Substances 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 101710117290 Aldo-keto reductase family 1 member C4 Proteins 0.000 description 2
- 101001073212 Arabidopsis thaliana Peroxidase 33 Proteins 0.000 description 2
- 108091033380 Coding strand Proteins 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 101150050927 Fcgrt gene Proteins 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 102000009465 Growth Factor Receptors Human genes 0.000 description 2
- 108010009202 Growth Factor Receptors Proteins 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 101001123325 Homo sapiens Peroxisome proliferator-activated receptor gamma coactivator 1-beta Proteins 0.000 description 2
- 108090001090 Lectins Proteins 0.000 description 2
- 102000004856 Lectins Human genes 0.000 description 2
- 241000282560 Macaca mulatta Species 0.000 description 2
- 241000699660 Mus musculus Species 0.000 description 2
- 108091005461 Nucleic proteins Chemical group 0.000 description 2
- 102100028961 Peroxisome proliferator-activated receptor gamma coactivator 1-beta Human genes 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 108700005077 Viral Genes Proteins 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 230000001588 bifunctional effect Effects 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 150000001720 carbohydrates Chemical group 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 230000007547 defect Effects 0.000 description 2
- 230000022811 deglycosylation Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 230000005284 excitation Effects 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 2
- 125000002446 fucosyl group Chemical group C1([C@@H](O)[C@H](O)[C@H](O)[C@@H](O1)C)* 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 210000002288 golgi apparatus Anatomy 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 239000002523 lectin Substances 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 239000002207 metabolite Substances 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 238000003153 stable transfection Methods 0.000 description 2
- 238000004114 suspension culture Methods 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 210000004881 tumor cell Anatomy 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 235000008979 vitamin B4 Nutrition 0.000 description 2
- 239000003643 water by type Substances 0.000 description 2
- 108091008875 B cell receptors Proteins 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 101100013695 Caenorhabditis elegans fut-8 gene Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 108010045674 Fucose-1-phosphate guanylyltransferase Proteins 0.000 description 1
- 102100037047 Fucose-1-phosphate guanylyltransferase Human genes 0.000 description 1
- PNHLMHWWFOPQLK-ZQXLIXSRSA-N GDP-4-dehydro-beta-L-fucose Chemical compound O[C@H]1[C@H](O)C(=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(N=C(N)N3)=O)N=C2)O1 PNHLMHWWFOPQLK-ZQXLIXSRSA-N 0.000 description 1
- 101000690301 Homo sapiens Aldo-keto reductase family 1 member C4 Proteins 0.000 description 1
- 101001116548 Homo sapiens Protein CBFA2T1 Proteins 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- 102100040648 L-fucose kinase Human genes 0.000 description 1
- 101710091950 L-fucose kinase Proteins 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 241000699673 Mesocricetus auratus Species 0.000 description 1
- 108090000143 Mouse Proteins Proteins 0.000 description 1
- UGJBHEZMOKVTIM-UHFFFAOYSA-N N-formylglycine Chemical compound OC(=O)CNC=O UGJBHEZMOKVTIM-UHFFFAOYSA-N 0.000 description 1
- ACFIXJIJDZMPPO-NNYOXOHSSA-N NADPH Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](OP(O)(O)=O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 ACFIXJIJDZMPPO-NNYOXOHSSA-N 0.000 description 1
- 241001452677 Ogataea methanolica Species 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 102000018120 Recombinases Human genes 0.000 description 1
- 108010091086 Recombinases Proteins 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 241000255993 Trichoplusia ni Species 0.000 description 1
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 1
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000012445 acidic reagent Substances 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- PNNNRSAQSRJVSB-KVTDHHQDSA-N aldehydo-D-rhamnose Chemical compound C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-KVTDHHQDSA-N 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- PTVXQARCLQPGIR-SXUWKVJYSA-N beta-L-fucose 1-phosphate Chemical compound C[C@@H]1O[C@H](OP(O)(O)=O)[C@@H](O)[C@H](O)[C@@H]1O PTVXQARCLQPGIR-SXUWKVJYSA-N 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 102000003675 cytokine receptors Human genes 0.000 description 1
- 108010057085 cytokine receptors Proteins 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 239000012483 derivatization solution Substances 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 229960003722 doxycycline Drugs 0.000 description 1
- XQTWDDCIUJNLTR-CVHRZJFOSA-N doxycycline monohydrate Chemical compound O.O=C1C2=C(O)C=CC=C2[C@H](C)[C@@H]2C1=C(O)[C@]1(O)C(=O)C(C(N)=O)=C(O)[C@@H](N(C)C)[C@@H]1[C@H]2O XQTWDDCIUJNLTR-CVHRZJFOSA-N 0.000 description 1
- -1 e.g. Proteins 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 229930182830 galactose Natural products 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 230000005017 genetic modification Effects 0.000 description 1
- 235000013617 genetically modified food Nutrition 0.000 description 1
- 101150106565 gmd gene Proteins 0.000 description 1
- 108010064833 guanylyltransferase Proteins 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 102000054751 human RUNX1T1 Human genes 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 102000002467 interleukin receptors Human genes 0.000 description 1
- 108010093036 interleukin receptors Proteins 0.000 description 1
- 125000000468 ketone group Chemical group 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000009630 liquid culture Methods 0.000 description 1
- 230000015100 lysosomal transport Effects 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 238000000816 matrix-assisted laser desorption--ionisation Methods 0.000 description 1
- 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 1
- 238000002887 multiple sequence alignment Methods 0.000 description 1
- 239000003471 mutagenic agent Substances 0.000 description 1
- 231100000707 mutagenic chemical Toxicity 0.000 description 1
- 230000003505 mutagenic effect Effects 0.000 description 1
- AEMBWNDIEFEPTH-UHFFFAOYSA-N n-tert-butyl-n-ethylnitrous amide Chemical compound CCN(N=O)C(C)(C)C AEMBWNDIEFEPTH-UHFFFAOYSA-N 0.000 description 1
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 1
- 238000002414 normal-phase solid-phase extraction Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 229910052697 platinum Inorganic materials 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000009877 rendering Methods 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000000717 sertoli cell Anatomy 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- BEOOHQFXGBMRKU-UHFFFAOYSA-N sodium cyanoborohydride Chemical compound [Na+].[B-]C#N BEOOHQFXGBMRKU-UHFFFAOYSA-N 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 230000009469 supplementation Effects 0.000 description 1
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 210000003501 vero cell Anatomy 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- 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
-
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2863—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for growth factors, growth regulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2866—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for cytokines, lymphokines, interferons
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- 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
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01271—GDP-L-fucose synthase (1.1.1.271)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/10—Immunoglobulins specific features characterized by their source of isolation or production
- C07K2317/14—Specific host cells or culture conditions, e.g. components, pH or temperature
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/52—Improvements relating to the production of bulk chemicals using catalysts, e.g. selective catalysts
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Cell Biology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US18340009P | 2009-06-02 | 2009-06-02 | |
| US61/183,400 | 2009-06-02 | ||
| US34885810P | 2010-05-27 | 2010-05-27 | |
| US61/348,858 | 2010-05-27 | ||
| PCT/US2010/036914 WO2010141478A1 (en) | 2009-06-02 | 2010-06-01 | Fucosylation-deficient cells |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2764370A1 CA2764370A1 (en) | 2010-12-09 |
| CA2764370C true CA2764370C (en) | 2018-08-21 |
Family
ID=42338231
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2764370A Active CA2764370C (en) | 2009-06-02 | 2010-06-01 | Fucosylation-deficient cells |
Country Status (16)
| Country | Link |
|---|---|
| US (8) | US8409838B2 (OSRAM) |
| EP (3) | EP2438171B1 (OSRAM) |
| JP (4) | JP5744856B2 (OSRAM) |
| KR (2) | KR101641526B1 (OSRAM) |
| CN (1) | CN102459603B (OSRAM) |
| AU (1) | AU2010256753B2 (OSRAM) |
| BR (1) | BRPI1010035A2 (OSRAM) |
| CA (1) | CA2764370C (OSRAM) |
| DK (3) | DK2438171T3 (OSRAM) |
| ES (2) | ES2527173T3 (OSRAM) |
| HU (1) | HUE038596T2 (OSRAM) |
| IL (1) | IL216624A (OSRAM) |
| PL (3) | PL2438171T3 (OSRAM) |
| SG (1) | SG176251A1 (OSRAM) |
| TW (1) | TWI513818B (OSRAM) |
| WO (1) | WO2010141478A1 (OSRAM) |
Families Citing this family (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20140161782A1 (en) | 2008-06-09 | 2014-06-12 | Targazyme, Inc. | Augmentation of cell therapy efficacy including treatment with alpha 1-3 fucoslytransferase |
| JP5744856B2 (ja) | 2009-06-02 | 2015-07-08 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドＲｅｇｅｎｅｒｏｎ Ｐｈａｒｍａｃｅｕｔｉｃａｌｓ， Ｉｎｃ． | フコシル化欠損細胞 |
| JP2014509850A (ja) | 2011-03-06 | 2014-04-24 | メルク セロノ ソシエテ アノニム | 低フコース細胞株およびその使用 |
| WO2013013013A2 (en) * | 2011-07-21 | 2013-01-24 | Alnylam Pharmaceuticals, Inc. | Compositions and methods for producing modified glycoproteins |
| TW201823460A (zh) | 2012-05-29 | 2018-07-01 | 美商再生元醫藥公司 | 生產細胞株增強子 |
| EP2722673B1 (en) | 2012-10-17 | 2017-07-12 | Hexal AG | Improved method of mapping glycans of glycoproteins |
| AR095196A1 (es) | 2013-03-15 | 2015-09-30 | Regeneron Pharma | Medio de cultivo celular libre de suero |
| WO2015033343A1 (en) | 2013-09-03 | 2015-03-12 | Yissum Research Development Company Of The Hebrew University Of Jerusalem Ltd. | Compositions and methods for expressing recombinant polypeptides |
| US20150093782A1 (en) * | 2013-10-01 | 2015-04-02 | The University Of Wyoming | Compositions and methods for reducing fucosylation of glycoproteins in insect cells and methods of use thereof for production of recombinant glycoproteins |
| MA39313B1 (fr) | 2014-03-11 | 2018-12-31 | Regeneron Pharma | Anticorps anti-egfrviii et leurs utilisations dans le traitement de divers cancers |
| EP4083066A3 (en) * | 2014-05-30 | 2023-02-08 | New England Biolabs, Inc. | Deglycosylation reagents and methods |
| US20170121673A1 (en) * | 2014-07-07 | 2017-05-04 | Targazyme, Inc. | Manufacture and Cryopreservation of Fucosylated Cells for Therapeutic Use |
| CN105671109B (zh) * | 2014-11-20 | 2019-08-23 | 中国人民解放军军事医学科学院生物工程研究所 | 用糖基工程酵母制备具有动物细胞糖基化修饰流感血凝素糖蛋白的方法 |
| TWI710573B (zh) | 2015-01-26 | 2020-11-21 | 美商再生元醫藥公司 | 抗伊波拉病毒醣蛋白之人類抗體 |
| TWI797060B (zh) | 2015-08-04 | 2023-04-01 | 美商再生元醫藥公司 | 補充牛磺酸之細胞培養基及用法 |
| WO2017079165A1 (en) | 2015-11-02 | 2017-05-11 | Genentech, Inc. | Methods of making fucosylated and afucosylated forms of a protein |
| MX2018008447A (es) | 2016-01-06 | 2019-05-30 | Oncobiologics Inc | Modulacion de especies afucosilados en una composicion de anticuerpo monoclonal. |
| MX2018009341A (es) | 2016-02-03 | 2019-05-15 | Oncobiologics Inc | Formulaciones tamponadas para una mayor estabilidad de anticuerpos. |
| AR109451A1 (es) | 2016-04-20 | 2018-12-12 | Regeneron Pharma | Composiciones y métodos para preparar anticuerpos basados en el uso de loci mejoradores de expresión |
| WO2017184831A1 (en) | 2016-04-20 | 2017-10-26 | Regeneron Pharmaceuticals, Inc. | Compositions and methods for making antibodies based on use of an expression-enhancing locus |
| EP3339444A1 (en) * | 2016-12-20 | 2018-06-27 | Mabxience Research, S.L. | Method for obtaining a glycoprotein with an increased percentage of afucosylated glycans |
| CN111954719B (zh) | 2018-03-26 | 2025-07-18 | 美国安进公司 | 细胞培养物中产生的抗体的总去岩藻糖基化糖型 |
| US20210317499A1 (en) * | 2018-08-29 | 2021-10-14 | United Biopharma Inc. | Afucosylated antibodies and manufacture thereof |
| TWI861023B (zh) | 2018-10-29 | 2024-11-11 | 日商免疫生物研究所股份有限公司 | 抗hiv抗體及其製造方法 |
| US12297451B1 (en) | 2019-10-25 | 2025-05-13 | Regeneron Pharmaceuticals, Inc. | Cell culture medium |
| IL298194A (en) | 2020-05-26 | 2023-01-01 | Regeneron Pharma | Antibodies against sars-cov2-spike glycoprotein and antigen-binding fragments |
| EP4161960A1 (en) | 2020-06-03 | 2023-04-12 | Regeneron Pharmaceuticals, Inc. | Methods for treating or preventing sars-cov-2 infections and covid-19 with anti-sars-cov-2 spike glycoprotein antibodies |
| CN112843234B (zh) * | 2021-01-20 | 2022-09-06 | 四川大学华西第二医院 | 一种调控生物机体内gdp-甘露糖的浓度的装置 |
| AU2022289365A1 (en) | 2021-06-07 | 2023-12-14 | Amgen Inc. | Using fucosidase to control afucosylation level of glycosylated proteins |
| JP2024527235A (ja) | 2021-06-22 | 2024-07-24 | リジェネロン・ファーマシューティカルズ・インコーポレイテッド | 抗ＥＧＦＲｖＩＩＩ抗体薬物コンジュゲート及びその使用 |
| KR20240046322A9 (ko) | 2021-07-14 | 2025-10-01 | 리제너론 파아마슈티컬스, 인크. | 항-sars-cov-2-스파이크 당단백질 항체 및 항원-결합 단편 |
| WO2023081434A2 (en) | 2021-11-07 | 2023-05-11 | Regeneron Pharmaceuticals, Inc. | Methods for treating or preventing sars-cov-2 infections and covid-19 with anti-sars-cov-2 spike glycoprotein antibodies |
| CN119053625A (zh) | 2022-03-02 | 2024-11-29 | 瑞泽恩制药公司 | 用于抗体生产的细胞培养方法 |
Family Cites Families (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US1006070A (en) | 1909-05-11 | 1911-10-17 | George Walter Durbrow | Method of and means for extracting micro-organisms and solids from water. |
| PT1176195E (pt) * | 1999-04-09 | 2013-07-18 | Kyowa Hakko Kirin Co Ltd | Processo para controlar a actividade de uma molécula funcional sob o ponto de vista imunológico |
| JP2001145488A (ja) | 1999-11-19 | 2001-05-29 | Natl Inst Of Advanced Industrial Science & Technology Meti | シロイヌナズナ由来のｇｄｐ−４−ケト−６−デオキシ−ｄ−マンノース−３，５−エピメラーゼ−４−レダクターゼ遺伝子 |
| FR2807767B1 (fr) | 2000-04-12 | 2005-01-14 | Lab Francais Du Fractionnement | Anticorps monoclonaux anti-d |
| EP3263702A1 (en) * | 2000-10-06 | 2018-01-03 | Kyowa Hakko Kirin Co., Ltd. | Cells producing antibody compositions |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| US20020150968A1 (en) | 2001-01-10 | 2002-10-17 | Wang Peng G. | Glycoconjugate and sugar nucleotide synthesis using solid supports |
| EP1392859B1 (en) | 2001-01-16 | 2006-05-10 | Regeneron Pharmaceuticals, Inc. | Isolating cells expressing secreted proteins |
| PL213948B1 (pl) | 2001-10-25 | 2013-05-31 | Genentech Inc | Kompozycje zawierajace glikoproteine, czasteczka kwasu nukleinowego kodujaca te glikoproteine, komórka gospodarza, sposób wytwarzania glikoproteiny, kompozycja do zastosowania do leczenia, zastosowanie kompozycji i zestaw zawierajacy kompozycje |
| KR100585140B1 (ko) | 2004-04-26 | 2006-05-30 | 삼성전자주식회사 | 와이어 본딩 장치 및 이를 이용한 반도체 패키지의 와이어본딩 방법 |
| US20060223147A1 (en) * | 2004-08-05 | 2006-10-05 | Kyowa Hakko Kogyo Co., Ltd., | Process for producing glycoprotein composition |
| CA2608818A1 (en) | 2005-06-03 | 2006-12-14 | Genentech, Inc. | Method of producing antibodies with modified fucosylation level |
| AU2007285976B2 (en) | 2006-08-14 | 2011-08-18 | Xencor, Inc | Optimized antibodies that target CD19 |
| JP2010519930A (ja) | 2007-03-07 | 2010-06-10 | グライコフィ， インコーポレイテッド | 糖タンパク質の修飾フコシル化を用いる産生 |
| EP2150617B1 (en) | 2007-06-04 | 2014-10-22 | Regeneron Pharmaceuticals, Inc. | Enhanced expression and stability regions |
| JP5662149B2 (ja) | 2008-08-13 | 2015-01-28 | 協和発酵キリン株式会社 | 遺伝子組換えプロテインｓ組成物 |
| JP5744856B2 (ja) | 2009-06-02 | 2015-07-08 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドＲｅｇｅｎｅｒｏｎ Ｐｈａｒｍａｃｅｕｔｉｃａｌｓ， Ｉｎｃ． | フコシル化欠損細胞 |
| JP2014509850A (ja) | 2011-03-06 | 2014-04-24 | メルク セロノ ソシエテ アノニム | 低フコース細胞株およびその使用 |
-
2010
- 2010-06-01 JP JP2012514045A patent/JP5744856B2/ja not_active Expired - Fee Related
- 2010-06-01 TW TW099117652A patent/TWI513818B/zh not_active IP Right Cessation
- 2010-06-01 AU AU2010256753A patent/AU2010256753B2/en not_active Ceased
- 2010-06-01 US US12/791,637 patent/US8409838B2/en active Active
- 2010-06-01 BR BRPI1010035-0A patent/BRPI1010035A2/pt not_active Application Discontinuation
- 2010-06-01 KR KR1020147007025A patent/KR101641526B1/ko not_active Expired - Fee Related
- 2010-06-01 CN CN2010800294912A patent/CN102459603B/zh not_active Expired - Fee Related
- 2010-06-01 ES ES10721096.5T patent/ES2527173T3/es active Active
- 2010-06-01 EP EP10721096.5A patent/EP2438171B1/en active Active
- 2010-06-01 PL PL10721096T patent/PL2438171T3/pl unknown
- 2010-06-01 PL PL17192430T patent/PL3279326T3/pl unknown
- 2010-06-01 DK DK10721096.5T patent/DK2438171T3/en active
- 2010-06-01 EP EP17192430.1A patent/EP3279326B1/en active Active
- 2010-06-01 ES ES14179885.0T patent/ES2661074T3/es active Active
- 2010-06-01 SG SG2011087517A patent/SG176251A1/en unknown
- 2010-06-01 WO PCT/US2010/036914 patent/WO2010141478A1/en not_active Ceased
- 2010-06-01 CA CA2764370A patent/CA2764370C/en active Active
- 2010-06-01 DK DK17192430.1T patent/DK3279326T3/da active
- 2010-06-01 DK DK14179885.0T patent/DK2808393T3/en active
- 2010-06-01 HU HUE14179885A patent/HUE038596T2/hu unknown
- 2010-06-01 PL PL14179885T patent/PL2808393T3/pl unknown
- 2010-06-01 EP EP14179885.0A patent/EP2808393B1/en active Active
- 2010-06-01 KR KR1020117031320A patent/KR101441437B1/ko not_active Expired - Fee Related
-
2011
- 2011-11-27 IL IL216624A patent/IL216624A/en active IP Right Grant
-
2013
- 2013-02-28 US US13/779,952 patent/US9206455B2/en active Active
-
2014
- 2014-12-12 JP JP2014251541A patent/JP2015051021A/ja not_active Withdrawn
-
2015
- 2015-12-08 US US14/963,178 patent/US9550823B2/en active Active
-
2016
- 2016-03-07 JP JP2016043151A patent/JP6211642B2/ja not_active Expired - Fee Related
- 2016-10-14 JP JP2016202634A patent/JP2017006147A/ja active Pending
- 2016-12-14 US US15/378,670 patent/US10006070B2/en active Active
-
2018
- 2018-05-23 US US15/987,286 patent/US20190024129A1/en not_active Abandoned
-
2019
- 2019-08-30 US US16/556,334 patent/US20200080124A1/en not_active Abandoned
-
2021
- 2021-05-04 US US17/307,255 patent/US11560550B2/en active Active
-
2022
- 2022-12-15 US US18/066,303 patent/US12054751B2/en active Active
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US12054751B2 (en) | Fucosylation-deficient cells | |
| AU2015282354B2 (en) | Fucosylation-deficient cells | |
| AU2012100020A6 (en) | Fucosylation-deficient cells | |
| AU2014200152B2 (en) | Fucosylation-deficient cells | |
| HK1249547B (en) | Fucosylation-deficient cells | |
| HK1198180B (en) | Fucosylation-deficient cells | |
| HK1163745B (en) | Fucosylation-deficient cells |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20150320 |