ES2660227T3 - Sistema biosintético que produce polisacáridos inmunogénicos en células procariotas - Google Patents
Sistema biosintético que produce polisacáridos inmunogénicos en células procariotas Download PDFInfo
- Publication number
- ES2660227T3 ES2660227T3 ES10831896.5T ES10831896T ES2660227T3 ES 2660227 T3 ES2660227 T3 ES 2660227T3 ES 10831896 T ES10831896 T ES 10831896T ES 2660227 T3 ES2660227 T3 ES 2660227T3
- Authority
- ES
- Spain
- Prior art keywords
- galnac
- coli
- glcnac
- und
- gene
- 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
- 150000004676 glycans Chemical class 0.000 title abstract description 14
- 229920001282 polysaccharide Polymers 0.000 title abstract description 13
- 239000005017 polysaccharide Substances 0.000 title abstract description 13
- 230000002163 immunogen Effects 0.000 title description 4
- 230000001851 biosynthetic effect Effects 0.000 title description 3
- 210000001236 prokaryotic cell Anatomy 0.000 title 1
- 241000588724 Escherichia coli Species 0.000 abstract description 41
- 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 abstract description 31
- 108090000623 proteins and genes Proteins 0.000 abstract description 28
- 102000004169 proteins and genes Human genes 0.000 abstract description 17
- 241000589875 Campylobacter jejuni Species 0.000 abstract description 6
- 150000001413 amino acids Chemical class 0.000 abstract description 5
- 150000002632 lipids Chemical class 0.000 abstract description 5
- 108091035707 Consensus sequence Proteins 0.000 abstract description 4
- 108700023372 Glycosyltransferases Proteins 0.000 abstract description 4
- 102000051366 Glycosyltransferases Human genes 0.000 abstract description 4
- 108700014210 glycosyltransferase activity proteins Proteins 0.000 abstract description 4
- 108010089072 Dolichyl-diphosphooligosaccharide-protein glycotransferase Proteins 0.000 abstract description 3
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 abstract description 3
- 108090000992 Transferases Proteins 0.000 abstract description 2
- 102000004357 Transferases Human genes 0.000 abstract description 2
- 108020004707 nucleic acids Proteins 0.000 abstract 2
- 102000039446 nucleic acids Human genes 0.000 abstract 2
- 150000007523 nucleic acids Chemical class 0.000 abstract 2
- 229920001542 oligosaccharide Polymers 0.000 abstract 2
- 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 abstract 1
- NTXGVHCCXVHYCL-RDQGWRCRSA-N all-trans-undecaprenyl diphosphate Chemical compound CC(C)=CCC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\COP(O)(=O)OP(O)(O)=O NTXGVHCCXVHYCL-RDQGWRCRSA-N 0.000 abstract 1
- 150000002482 oligosaccharides Chemical class 0.000 abstract 1
- OVRNDRQMDRJTHS-KEWYIRBNSA-N N-acetyl-D-galactosamine Chemical compound CC(=O)N[C@H]1C(O)O[C@H](CO)[C@H](O)[C@@H]1O OVRNDRQMDRJTHS-KEWYIRBNSA-N 0.000 description 31
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 20
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 16
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 16
- OVRNDRQMDRJTHS-RTRLPJTCSA-N N-acetyl-D-glucosamine Chemical compound CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-RTRLPJTCSA-N 0.000 description 16
- 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 description 16
- 101150075171 Gne gene Proteins 0.000 description 15
- 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 13
- 210000004027 cell Anatomy 0.000 description 13
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 12
- 239000000427 antigen Substances 0.000 description 12
- 102000036639 antigens Human genes 0.000 description 11
- 108091007433 antigens Proteins 0.000 description 11
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 10
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 9
- 102100039847 Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 Human genes 0.000 description 9
- 229930186217 Glycolipid Natural products 0.000 description 9
- 101000887519 Homo sapiens Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 Proteins 0.000 description 9
- 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 9
- 230000015572 biosynthetic process Effects 0.000 description 9
- 239000012528 membrane Substances 0.000 description 9
- 239000000047 product Substances 0.000 description 9
- 235000018102 proteins Nutrition 0.000 description 9
- 108090001066 Racemases and epimerases Proteins 0.000 description 8
- 102000004879 Racemases and epimerases Human genes 0.000 description 7
- 230000002068 genetic effect Effects 0.000 description 7
- VNWKTOKETHGBQD-UHFFFAOYSA-N methane Natural products C VNWKTOKETHGBQD-UHFFFAOYSA-N 0.000 description 7
- 238000005119 centrifugation Methods 0.000 description 6
- 238000000034 method Methods 0.000 description 6
- 229910052757 nitrogen Inorganic materials 0.000 description 6
- 239000002773 nucleotide Substances 0.000 description 6
- 125000003729 nucleotide group Chemical group 0.000 description 6
- 239000013612 plasmid Substances 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 5
- 239000000284 extract Substances 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 150000002500 ions Chemical class 0.000 description 5
- 229960005486 vaccine Drugs 0.000 description 5
- 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 4
- HVCOBJNICQPDBP-UHFFFAOYSA-N 3-[3-[3,5-dihydroxy-6-methyl-4-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyoxan-2-yl]oxydecanoyloxy]decanoic acid;hydrate Chemical compound O.OC1C(OC(CC(=O)OC(CCCCCCC)CC(O)=O)CCCCCCC)OC(C)C(O)C1OC1C(O)C(O)C(O)C(C)O1 HVCOBJNICQPDBP-UHFFFAOYSA-N 0.000 description 4
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 4
- 101000887514 Escherichia coli O157:H7 N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase Proteins 0.000 description 4
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical compound C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-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
- 239000002671 adjuvant Substances 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 239000003085 diluting agent Substances 0.000 description 4
- 239000008194 pharmaceutical composition Substances 0.000 description 4
- 239000000546 pharmaceutical excipient Substances 0.000 description 4
- 229920001223 polyethylene glycol Polymers 0.000 description 4
- 238000004611 spectroscopical analysis Methods 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical group CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 3
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 3
- 101710154606 Hemagglutinin Proteins 0.000 description 3
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 3
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 3
- 101710176177 Protein A56 Proteins 0.000 description 3
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 3
- 229930006000 Sucrose Natural products 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 108010075202 UDP-glucose 4-epimerase Proteins 0.000 description 3
- 229960000583 acetic acid Drugs 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 3
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 3
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 101150002054 galE gene Proteins 0.000 description 3
- 239000000185 hemagglutinin Substances 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 230000002503 metabolic effect Effects 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000005720 sucrose Substances 0.000 description 3
- BGNGWHSBYQYVRX-UHFFFAOYSA-N 4-(dimethylamino)benzaldehyde Chemical compound CN(C)C1=CC=C(C=O)C=C1 BGNGWHSBYQYVRX-UHFFFAOYSA-N 0.000 description 2
- 238000000035 BCA protein assay Methods 0.000 description 2
- 108010023063 Bacto-peptone Proteins 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 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 2
- 241001646716 Escherichia coli K-12 Species 0.000 description 2
- 239000006391 Luria-Bertani Medium Substances 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 2
- 230000004988 N-glycosylation Effects 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 210000001744 T-lymphocyte Anatomy 0.000 description 2
- XCCTYIAWTASOJW-UHFFFAOYSA-N UDP-Glc Natural products OC1C(O)C(COP(O)(=O)OP(O)(O)=O)OC1N1C(=O)NC(=O)C=C1 XCCTYIAWTASOJW-UHFFFAOYSA-N 0.000 description 2
- 108010070691 UDP-N-acetylglucosamine 4-epimerase Proteins 0.000 description 2
- 102100021436 UDP-glucose 4-epimerase Human genes 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- 238000005903 acid hydrolysis reaction Methods 0.000 description 2
- 238000013019 agitation Methods 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 229940024606 amino acid Drugs 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000005947 deacylation reaction Methods 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000006345 epimerization reaction Methods 0.000 description 2
- 238000007654 immersion Methods 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 238000004949 mass spectrometry Methods 0.000 description 2
- GBMDVOWEEQVZKZ-UHFFFAOYSA-N methanol;hydrate Chemical compound O.OC GBMDVOWEEQVZKZ-UHFFFAOYSA-N 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 150000005846 sugar alcohols Chemical class 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- XSYUPRQVAHJETO-WPMUBMLPSA-N (2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-amino-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidaz Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(O)=O)C1=CN=CN1 XSYUPRQVAHJETO-WPMUBMLPSA-N 0.000 description 1
- 101150033839 4 gene Proteins 0.000 description 1
- UDZMHVWZLRBHMW-UHFFFAOYSA-N 4-(4-aminophenyl)aniline;periodic acid Chemical compound OI(=O)(=O)=O.C1=CC(N)=CC=C1C1=CC=C(N)C=C1 UDZMHVWZLRBHMW-UHFFFAOYSA-N 0.000 description 1
- AEOBEOJCBAYXBA-UHFFFAOYSA-N A2P5P Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(O)=O)C(O)C1OP(O)(O)=O AEOBEOJCBAYXBA-UHFFFAOYSA-N 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 101150017040 I gene Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 108091006036 N-glycosylated proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 241001138501 Salmonella enterica Species 0.000 description 1
- 241000607766 Shigella boydii Species 0.000 description 1
- 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 1
- 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 description 1
- 230000009471 action Effects 0.000 description 1
- 239000004480 active ingredient Substances 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
- JDGPQNJYYADFKP-UHFFFAOYSA-N aniline;n-phenylaniline Chemical compound NC1=CC=CC=C1.C=1C=CC=CC=1NC1=CC=CC=C1 JDGPQNJYYADFKP-UHFFFAOYSA-N 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000006696 biosynthetic metabolic pathway Effects 0.000 description 1
- 229910021538 borax Inorganic materials 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
- 239000002775 capsule Substances 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 150000001793 charged compounds Chemical class 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- RPKLZQLYODPWTM-KBMWBBLPSA-N cholanoic acid Chemical compound C1CC2CCCC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@@H](CCC(O)=O)C)[C@@]1(C)CC2 RPKLZQLYODPWTM-KBMWBBLPSA-N 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000000875 corresponding effect Effects 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 230000020176 deacylation Effects 0.000 description 1
- 229940009976 deoxycholate Drugs 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 229920002672 di-trans,poly-cis-Undecaprenol Polymers 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 239000000386 donor Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 150000002327 glycerophospholipids Chemical class 0.000 description 1
- 239000000348 glycosyl donor Substances 0.000 description 1
- 108091005608 glycosylated proteins Proteins 0.000 description 1
- 102000035122 glycosylated proteins Human genes 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000005040 ion trap Methods 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 239000011344 liquid material Substances 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 238000001466 metabolic labeling Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 239000012074 organic phase Substances 0.000 description 1
- 238000004816 paper chromatography Methods 0.000 description 1
- 238000005192 partition Methods 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 229920002704 polyhistidine Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 239000012056 semi-solid material Substances 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 0.000 description 1
- 235000010339 sodium tetraborate Nutrition 0.000 description 1
- 239000011343 solid material Substances 0.000 description 1
- 239000002195 soluble material Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 238000000638 solvent extraction Methods 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 150000004044 tetrasaccharides Chemical class 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- IEDVJHCEMCRBQM-UHFFFAOYSA-N trimethoprim Chemical compound COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 IEDVJHCEMCRBQM-UHFFFAOYSA-N 0.000 description 1
- 229960001082 trimethoprim Drugs 0.000 description 1
- BSVBQGMMJUBVOD-UHFFFAOYSA-N trisodium borate Chemical compound [Na+].[Na+].[Na+].[O-]B([O-])[O-] BSVBQGMMJUBVOD-UHFFFAOYSA-N 0.000 description 1
- 101150100260 wcaM gene Proteins 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/02—Bacterial antigens
- A61K39/025—Enterobacteriales, e.g. Enterobacter
- A61K39/0258—Escherichia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/02—Bacterial antigens
- A61K39/025—Enterobacteriales, e.g. Enterobacter
- A61K39/0283—Shigella
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/385—Haptens or antigens, bound to carriers
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/62—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being a protein, peptide or polyamino acid
- A61K47/64—Drug-peptide, drug-protein or drug-polyamino acid conjugates, i.e. the modifying agent being a peptide, protein or polyamino acid which is covalently bonded or complexed to a therapeutically active agent
- A61K47/646—Drug-peptide, drug-protein or drug-polyamino acid conjugates, i.e. the modifying agent being a peptide, protein or polyamino acid which is covalently bonded or complexed to a therapeutically active agent the entire peptide or protein drug conjugate elicits an immune response, e.g. conjugate vaccines
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial 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
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/60—Medicinal preparations containing antigens or antibodies characteristics by the carrier linked to the antigen
- A61K2039/6031—Proteins
- A61K2039/6068—Other bacterial proteins, e.g. OMP
-
- 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
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Epidemiology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Mycology (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Virology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Organic Chemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Medicinal Preparation (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US272931P | 2001-03-02 | ||
| US27293109P | 2009-11-19 | 2009-11-19 | |
| PCT/US2010/002980 WO2011062615A1 (en) | 2009-11-19 | 2010-11-16 | Biosynthetic system that produces immunogenic polysaccharides in prokaryotic cells |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2660227T3 true ES2660227T3 (es) | 2018-03-21 |
Family
ID=44059888
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES10831896.5T Active ES2660227T3 (es) | 2009-11-19 | 2010-11-16 | Sistema biosintético que produce polisacáridos inmunogénicos en células procariotas |
Country Status (20)
| Country | Link |
|---|---|
| US (2) | US8846342B2 (enExample) |
| EP (1) | EP2501406B8 (enExample) |
| JP (2) | JP5968784B2 (enExample) |
| KR (1) | KR101855380B1 (enExample) |
| CN (1) | CN102724997B (enExample) |
| AU (1) | AU2010322454B2 (enExample) |
| CA (1) | CA2780487C (enExample) |
| CY (1) | CY1119995T1 (enExample) |
| DK (1) | DK2501406T3 (enExample) |
| ES (1) | ES2660227T3 (enExample) |
| HR (1) | HRP20180338T1 (enExample) |
| HU (1) | HUE038456T2 (enExample) |
| IL (1) | IL219733A (enExample) |
| LT (1) | LT2501406T (enExample) |
| NO (1) | NO2501406T3 (enExample) |
| PL (1) | PL2501406T3 (enExample) |
| PT (1) | PT2501406T (enExample) |
| SI (1) | SI2501406T1 (enExample) |
| TR (1) | TR201803015T4 (enExample) |
| WO (1) | WO2011062615A1 (enExample) |
Families Citing this family (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK1481057T3 (da) * | 2002-03-07 | 2006-05-15 | Eidgenoess Tech Hochschule | System og fremgangsmåde til fremstilling af rekombinante glycosylerede proteiner i en prokaryot vært |
| NO2501406T3 (enExample) * | 2009-11-19 | 2018-05-19 | ||
| EP2742355B1 (en) * | 2011-08-12 | 2018-12-19 | The Governors of the University of Alberta | Method of diagnosing bacterial infections using bacterial glycoproteins |
| CA2879272A1 (en) | 2012-07-16 | 2014-01-23 | Robert G.K. DONALD | Saccharides and uses thereof |
| US20150353940A1 (en) | 2013-08-05 | 2015-12-10 | Absci, Llc | Vectors for use in an inducible coexpression system |
| EP2724730A1 (en) | 2012-10-29 | 2014-04-30 | Institut Pasteur | Glycoconjugates and their use as potential vaccines against infection by Shigella Flexneri |
| HUE038915T2 (hu) | 2013-01-17 | 2018-12-28 | Arsanis Biosciences Gmbh | MDR E. colira fajlagos antitest |
| GB201301085D0 (en) * | 2013-01-22 | 2013-03-06 | London School Hygiene & Tropical Medicine | Glycoconjugate Vaccine |
| BR112016007727A8 (pt) * | 2013-10-11 | 2018-01-30 | Glycovaxyn Ag | célula hospedeira, e, método para produzir uma proteína n-glicosilada. |
| NZ723328A (en) | 2014-02-24 | 2018-01-26 | Glycovaxyn Ag | Compositions comprising e. coli o25b antigen, uses thereof and methods of manufacture |
| MX378857B (es) * | 2014-04-17 | 2025-03-10 | Glaxosmithkline Biologicals Sa | Celulas huespedes modificadas y usos de las mismas. |
| KR101629656B1 (ko) * | 2014-10-24 | 2016-06-14 | 충남대학교산학협력단 | 면역증강효과를 갖는 수용성 다당체 및 이를 함유하는 조성물 |
| SI3240895T1 (sl) * | 2014-12-30 | 2022-04-29 | Glaxosmithkline Biologicals S.A. | Sestavki in postopki za glikozilacijo proteinov |
| TWI715617B (zh) | 2015-08-24 | 2021-01-11 | 比利時商葛蘭素史密斯克藍生物品公司 | 對抗腸道外病原性大腸桿菌之免疫保護之方法及組合物 |
| GB201518668D0 (en) | 2015-10-21 | 2015-12-02 | Glaxosmithkline Biolog Sa | Immunogenic Comosition |
| EP3384018A1 (en) | 2015-11-30 | 2018-10-10 | Limmatech Biologics AG | Methods of producing glycosylated proteins |
| GB201610599D0 (en) | 2016-06-17 | 2016-08-03 | Glaxosmithkline Biologicals Sa | Immunogenic Composition |
| AR109621A1 (es) | 2016-10-24 | 2018-12-26 | Janssen Pharmaceuticals Inc | Formulaciones de vacunas contra glucoconjugados de expec |
| GB201711635D0 (en) | 2017-07-19 | 2017-08-30 | Glaxosmithkline Biologicals Sa | Immunogenic composition |
| GB201721582D0 (en) | 2017-12-21 | 2018-02-07 | Glaxosmithkline Biologicals Sa | S aureus antigens and immunogenic compositions |
| GB201721576D0 (en) | 2017-12-21 | 2018-02-07 | Glaxosmithkline Biologicals Sa | Hla antigens and glycoconjugates thereof |
| JP7551618B2 (ja) | 2018-12-12 | 2024-09-17 | グラクソスミスクライン バイオロジカルズ ソシエテ アノニム | Ｏ－結合型グリコシル化のための修飾キャリアタンパク質 |
| CR20210522A (es) | 2019-03-18 | 2021-12-17 | Janssen Pharmaceuticals Inc | Bioconjugados de antígenos–polisacáridos de e. coli, métodos de producción y métodos de utilización de los mismos |
| IL286467B2 (en) | 2019-03-18 | 2026-02-01 | Janssen Pharmaceuticals Inc | Methods for producing bioconjugates of polysaccharides E. coli o-antigen, preparations thereof and methods for using them |
| EP3770269A1 (en) | 2019-07-23 | 2021-01-27 | GlaxoSmithKline Biologicals S.A. | Quantification of bioconjugate glycosylation |
| CA3185719A1 (en) | 2020-06-18 | 2021-12-23 | Glaxosmithkline Biologicals Sa | Shigella-tetravalent (shigella4v) bioconjugate |
| US20230226175A1 (en) | 2020-06-25 | 2023-07-20 | Glaxosmithkline Biologicals Sa | Modified exotoxin a proteins |
| PE20231385A1 (es) | 2020-09-17 | 2023-09-12 | Janssen Pharmaceuticals Inc | Composiciones de vacunas multivalentes y usos de las mismas |
| CN112877246B (zh) * | 2021-02-23 | 2022-01-18 | 山东省滨州畜牧兽医研究院 | 一种高效制备霍乱弧菌菌影的方法 |
| CN115747239A (zh) * | 2021-09-03 | 2023-03-07 | 上海交通大学 | 用于表达黏蛋白型o-糖基化蛋白的原核载体和系统、黏蛋白型o-糖基化蛋白的制备方法 |
| EP4452308A1 (en) | 2021-12-22 | 2024-10-30 | GlaxoSmithKline Biologicals S.A. | Vaccine |
| GB202302579D0 (en) | 2023-02-23 | 2023-04-12 | Glaxosmithkline Biologicals Sa | Immunogenic composition |
| WO2025172892A1 (en) | 2024-02-16 | 2025-08-21 | Glaxosmithkline Biologicals Sa | Modified proteins and methods |
Family Cites Families (38)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS60142915A (ja) * | 1983-12-28 | 1985-07-29 | Lion Corp | 口腔用組成物 |
| EP0170204B1 (de) | 1984-08-01 | 1991-09-25 | BOEHRINGER INGELHEIM INTERNATIONAL GmbH | Neue genetische Sequenzen, die durch sie codierten Interferon-Peptide vom Typ I und diese sie produzierende Organismen |
| US5242809A (en) * | 1986-02-28 | 1993-09-07 | Smithkline Beecham Corporation | Gal operon of streptomyces |
| US5643758A (en) | 1987-03-10 | 1997-07-01 | New England Biolabs, Inc. | Production and purification of a protein fused to a binding protein |
| US5665559A (en) * | 1989-05-18 | 1997-09-09 | The United States Of America As Represented By The Secretary Of The Navy | Production of monoclonal antibodies to bacteroides gingivalis by hybridoma BGII, VF9/2D |
| US5280113A (en) * | 1989-08-16 | 1994-01-18 | Monsanto Company | Method for producing synthetic N-linked glycoconjugates |
| AU6663294A (en) | 1993-05-14 | 1994-12-12 | Upjohn Company, The | Cloned dna encoding a udp-galnac:polypeptide,n-acetylgalactos aminyltransferase |
| US6365723B1 (en) * | 1998-12-04 | 2002-04-02 | Wisconsin Alumni Research Foundation | Sequences of E. coli O157 |
| US6503744B1 (en) | 1999-02-01 | 2003-01-07 | National Research Council Of Canada | Campylobacter glycosyltransferases for biosynthesis of gangliosides and ganglioside mimics |
| EP1399538A2 (en) | 1999-03-02 | 2004-03-24 | Human Genome Sciences, Inc. | Engineering intracellular sialylation pathways |
| NZ522320A (en) | 2000-05-12 | 2007-03-30 | Neose Technologies Inc | In vitro modification of glycosylation patterns of recombinant glycopeptides |
| EP2028275A3 (en) | 2000-06-30 | 2009-05-06 | VIB vzw | Protein glycosylation modification in pichia pastoris |
| US20040067557A1 (en) * | 2000-12-21 | 2004-04-08 | Tetsuo Endo | Process for producing udp-n-acetylgalactosamine and sacciiaride containing n-acetylgalactosamine |
| US20020132320A1 (en) * | 2001-01-10 | 2002-09-19 | Wang Peng George | Glycoconjugate synthesis using a pathway-engineered organism |
| US20020150968A1 (en) * | 2001-01-10 | 2002-10-17 | Wang Peng G. | Glycoconjugate and sugar nucleotide synthesis using solid supports |
| US6696814B2 (en) | 2001-07-09 | 2004-02-24 | Tyco Electronics Corporation | Microprocessor for controlling the speed and frequency of a motor shaft in a power tool |
| US7265085B2 (en) * | 2001-10-10 | 2007-09-04 | Neose Technologies, Inc. | Glycoconjugation methods and proteins/peptides produced by the methods |
| US7541043B2 (en) * | 2002-01-16 | 2009-06-02 | The United States Of America As Represented By The Department Of Health And Human Services | Vaccine for protection against Shigella sonnei disease |
| JP4727927B2 (ja) * | 2002-03-07 | 2011-07-20 | アイトゲネシシェ・テッヒニシェ・ホーホシューレ・チューリッヒ | 原核宿主における組換えグリコシル化タンパク質産生のためのシステムおよび方法 |
| DK1481057T3 (da) | 2002-03-07 | 2006-05-15 | Eidgenoess Tech Hochschule | System og fremgangsmåde til fremstilling af rekombinante glycosylerede proteiner i en prokaryot vært |
| CN1671722A (zh) | 2002-08-01 | 2005-09-21 | 加拿大国家研究院 | 弯曲菌的聚糖和糖肽 |
| EP2657251B1 (en) | 2004-05-24 | 2018-03-21 | The Government of The United States of America, as represented by The Secretary, Department of Health and Human Services | Live, oral vaccine for protection against Shigella dysenteriae serotype 1 |
| JP5235657B2 (ja) * | 2005-03-24 | 2013-07-10 | バイオジェネリックス ゲーエムベーハー | 原核生物における可溶性活性真核生物グリコシルトランスフェラーゼの発現 |
| ES2535084T3 (es) | 2005-05-11 | 2015-05-05 | Eth Zurich | Proteínas N-glicosiladas recombinantes procedentes de células procariotas |
| US20070202578A1 (en) * | 2005-08-26 | 2007-08-30 | Centre National De La Recherche Scientifique (Cnrs) | Production of globosides oligosaccharides using metabolically engineered microorganisms |
| WO2009089154A2 (en) * | 2008-01-03 | 2009-07-16 | Cornell Research Foundation, Inc. | Glycosylated protein expression in prokaryotes |
| CN102037004A (zh) * | 2008-01-08 | 2011-04-27 | 生物种属学股份公司 | 使用寡糖基转移酶的多肽的糖缀合 |
| SI2257307T1 (sl) * | 2008-02-20 | 2018-09-28 | Glaxosmithkline Biologicals S.A. | Biokonjugati, izdelani iz rekombinantnih N-glikoziliranih proteinov iz prokariontskih celic |
| CN102365359B (zh) * | 2009-03-27 | 2014-10-29 | 瑞士联邦苏黎世技术大学 | 呈递空肠弯曲杆菌n-聚糖或其衍生物的肠沙门氏菌 |
| GB0915403D0 (en) * | 2009-09-04 | 2009-10-07 | London School Hygiene & Tropical Medicine | Protein glycosylation |
| NO2501406T3 (enExample) * | 2009-11-19 | 2018-05-19 | ||
| CA2789505C (en) * | 2010-02-11 | 2017-12-05 | The Governors Of The University Of Alberta | N-linked glycan compounds |
| WO2011138361A1 (en) * | 2010-05-06 | 2011-11-10 | Glycovaxyn | Capsular gram-positive bacteria bioconjugate vaccines |
| WO2012027850A1 (en) * | 2010-09-03 | 2012-03-08 | Christine Szymanski | Peptide containing multiple n-linked glycosylation sequons |
| WO2013019625A2 (en) * | 2011-07-29 | 2013-02-07 | The University Of Wyoming | Methods of using a bacterial glcnac-6-p 2'-epimerase to promote sialylation of glycoconjugates |
| CA2847621A1 (en) * | 2011-09-06 | 2013-03-14 | Glycovaxyn Ag | Bioconjugate vaccines made in prokaryotic cells |
| EP2917351B1 (en) * | 2012-11-07 | 2018-12-19 | GlaxoSmithKline Biologicals S.A. | Production of recombinant vaccine in e. coli by enzymatic conjugation |
| GB201301085D0 (en) * | 2013-01-22 | 2013-03-06 | London School Hygiene & Tropical Medicine | Glycoconjugate Vaccine |
-
2010
- 2010-11-16 NO NO10831896A patent/NO2501406T3/no unknown
- 2010-11-16 PL PL10831896T patent/PL2501406T3/pl unknown
- 2010-11-16 DK DK10831896.5T patent/DK2501406T3/en active
- 2010-11-16 CN CN201080061239.XA patent/CN102724997B/zh active Active
- 2010-11-16 CA CA2780487A patent/CA2780487C/en active Active
- 2010-11-16 KR KR1020127015728A patent/KR101855380B1/ko active Active
- 2010-11-16 EP EP10831896.5A patent/EP2501406B8/en active Active
- 2010-11-16 HU HUE10831896A patent/HUE038456T2/hu unknown
- 2010-11-16 TR TR2018/03015T patent/TR201803015T4/tr unknown
- 2010-11-16 SI SI201031641T patent/SI2501406T1/en unknown
- 2010-11-16 LT LTEP10831896.5T patent/LT2501406T/lt unknown
- 2010-11-16 AU AU2010322454A patent/AU2010322454B2/en active Active
- 2010-11-16 US US13/510,859 patent/US8846342B2/en active Active
- 2010-11-16 HR HRP20180338TT patent/HRP20180338T1/hr unknown
- 2010-11-16 WO PCT/US2010/002980 patent/WO2011062615A1/en not_active Ceased
- 2010-11-16 ES ES10831896.5T patent/ES2660227T3/es active Active
- 2010-11-16 PT PT108318965T patent/PT2501406T/pt unknown
- 2010-11-16 JP JP2012539870A patent/JP5968784B2/ja active Active
-
2012
- 2012-05-10 IL IL219733A patent/IL219733A/en active IP Right Grant
-
2014
- 2014-08-18 US US14/462,261 patent/US9764018B2/en active Active
-
2016
- 2016-07-06 JP JP2016133786A patent/JP2017018098A/ja active Pending
-
2018
- 2018-03-02 CY CY20181100264T patent/CY1119995T1/el unknown
Also Published As
| Publication number | Publication date |
|---|---|
| EP2501406A1 (en) | 2012-09-26 |
| IL219733A (en) | 2017-08-31 |
| CA2780487C (en) | 2019-05-21 |
| DK2501406T3 (en) | 2018-02-26 |
| JP2013511520A (ja) | 2013-04-04 |
| HUE038456T2 (hu) | 2018-10-29 |
| JP5968784B2 (ja) | 2016-08-10 |
| EP2501406B8 (en) | 2018-01-24 |
| EP2501406B1 (en) | 2017-12-20 |
| AU2010322454B2 (en) | 2016-05-19 |
| US20150190492A1 (en) | 2015-07-09 |
| CA2780487A1 (en) | 2011-05-26 |
| LT2501406T (lt) | 2018-03-26 |
| KR101855380B1 (ko) | 2018-05-08 |
| JP2017018098A (ja) | 2017-01-26 |
| NO2501406T3 (enExample) | 2018-05-19 |
| SI2501406T1 (en) | 2018-03-30 |
| HRP20180338T1 (hr) | 2018-04-06 |
| US9764018B2 (en) | 2017-09-19 |
| AU2010322454A1 (en) | 2012-06-07 |
| TR201803015T4 (tr) | 2018-03-21 |
| CN102724997A (zh) | 2012-10-10 |
| IL219733A0 (en) | 2012-07-31 |
| US8846342B2 (en) | 2014-09-30 |
| EP2501406A4 (en) | 2013-04-24 |
| WO2011062615A1 (en) | 2011-05-26 |
| CY1119995T1 (el) | 2018-12-12 |
| KR20120102086A (ko) | 2012-09-17 |
| PT2501406T (pt) | 2018-02-21 |
| US20130028926A1 (en) | 2013-01-31 |
| CN102724997B (zh) | 2016-09-21 |
| PL2501406T3 (pl) | 2018-05-30 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EP2501406B1 (en) | Biosynthetic system that produces immunogenic polysaccharides in prokaryotic cells | |
| US12365930B2 (en) | Method for rapid in vitro synthesis of glycoproteins via recombinant production of N-glycosylated proteins in prokaryotic cell lysates | |
| Karlyshev et al. | Analysis of Campylobacter jejuni capsular loci reveals multiple mechanisms for the generation of structural diversity and the ability to form complex heptoses | |
| Schoenhofen et al. | Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways | |
| ES2650799T3 (es) | Bacteria que produce condroitina y procedimiento de producción de condroitina | |
| Monteiro | Helicobacter pylori: a wolf in sheep's clothing: the glycotype families of Helicobacter pylori lipopolysaccharides expressing histo-blood groups: structure, biosynthesis, and role in pathogenesis | |
| Rush et al. | A novel epimerase that converts GlcNAc-PP-undecaprenol to GalNAc-PP-undecaprenol in Escherichia coli O157 | |
| BR112020001628A2 (pt) | sialiltransferases e uso das mesmas na produção de oligossacarídeos sialilados | |
| Logan et al. | Novel biosynthetic functions of lipopolysaccharide rfaJ homologs from Helicobacter pylori | |
| Shao et al. | Sequence of Escherichia coli O128 antigen biosynthesis cluster and functional identification of an α-1, 2-fucosyltransferase | |
| Vinogradov et al. | Structure determination of Streptococcus suis serotype 9 capsular polysaccharide and assignment of functions of the cps locus genes involved in its biosynthesis | |
| Melamed et al. | Biosynthesis of the Pseudomonas aeruginosa common polysaccharide antigen by D-Rhamnosyltransferases WbpX and WbpY | |
| US20220145343A1 (en) | Materials and methods for the preparation of bacterial capsular polysaccharides | |
| AU2009316239B2 (en) | Vaccine strains of Brachyspira hyodysenteriae | |
| JP2025108479A (ja) | ラムノース－多糖 | |
| ES2554172T3 (es) | Biosíntesis de ácido CMP-legionamínico a partir de fructosa-6-P | |
| EP4010467B1 (en) | Mutated pglb oligosaccharyltransferase enzymes | |
| US11891598B2 (en) | Means and methods for producing phosphate containing capsular polysaccharides | |
| Liang et al. | One-pot multienzyme-catalyzed assembly of pentasaccharide repeating units from Group B Streptococcus capsular polysaccharides and their related oligosaccharide derivatives | |
| EP4168040A1 (en) | Shigella-tetravalent (shigella4v) bioconjugate | |
| Sharma | Characterization of the Biosynthetic Pathway of Capsular Polysaccharide A in Bacteroides fragilis | |
| Sharma | Biosynthesis of the immunomodulatory molecule capsular polysaccharide a from Bacteroides fragilis | |
| Zhang et al. | Probing a sialyltransferase’s recognition domain to prepare α (2, 8)-linked oligosialosides and analogs | |
| ES2267285T3 (es) | Alfa 2,8/2.,9-polisialiltranferasa. | |
| Tiralongo et al. | Sialic acid derivatives, analogues, and mimetics as biological probes and inhibitors of sialic acid recognizing proteins |