JP2009537165A5 - - Google Patents
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- JP2009537165A5 JP2009537165A5 JP2009511529A JP2009511529A JP2009537165A5 JP 2009537165 A5 JP2009537165 A5 JP 2009537165A5 JP 2009511529 A JP2009511529 A JP 2009511529A JP 2009511529 A JP2009511529 A JP 2009511529A JP 2009537165 A5 JP2009537165 A5 JP 2009537165A5
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- 239000002773 nucleotide Substances 0.000 claims description 285
- 125000003729 nucleotide group Chemical group 0.000 claims description 285
- 150000001413 amino acids Chemical class 0.000 claims description 94
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 73
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 73
- 239000012634 fragment Substances 0.000 claims description 26
- 102000039446 nucleic acids Human genes 0.000 claims description 5
- 108020004707 nucleic acids Proteins 0.000 claims description 5
- 150000007523 nucleic acids Chemical class 0.000 claims description 5
- 238000000034 method Methods 0.000 claims description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 2
- 229920001184 polypeptide Polymers 0.000 claims 72
- 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 3
- 101000652822 Rattus norvegicus CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase Proteins 0.000 claims 3
- 239000011543 agarose gel Substances 0.000 description 11
- 230000003197 catalytic effect Effects 0.000 description 10
- 108090000623 proteins and genes Proteins 0.000 description 8
- 108090000790 Enzymes Proteins 0.000 description 7
- 108091008146 restriction endonucleases Proteins 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 5
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 5
- 230000014509 gene expression Effects 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 102100029954 Sialic acid synthase Human genes 0.000 description 4
- 108090000141 Sialyltransferases Proteins 0.000 description 4
- 102000003838 Sialyltransferases Human genes 0.000 description 4
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 description 4
- 210000004027 cell Anatomy 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 210000004897 n-terminal region Anatomy 0.000 description 4
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 description 4
- 125000005630 sialyl group Chemical group 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 3
- TXCIAUNLDRJGJZ-BILDWYJOSA-N CMP-N-acetyl-beta-neuraminic acid Chemical compound O1[C@@H]([C@H](O)[C@H](O)CO)[C@H](NC(=O)C)[C@@H](O)C[C@]1(C(O)=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(N=C(N)C=C2)=O)O1 TXCIAUNLDRJGJZ-BILDWYJOSA-N 0.000 description 2
- 108700023372 Glycosyltransferases Proteins 0.000 description 2
- 241000282414 Homo sapiens Species 0.000 description 2
- 108090000856 Lyases Proteins 0.000 description 2
- 102000004317 Lyases Human genes 0.000 description 2
- 102100033341 N-acetylmannosamine kinase Human genes 0.000 description 2
- 108010069465 N-acylneuraminate-9-phosphate synthase Proteins 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 210000005220 cytoplasmic tail Anatomy 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 229940060155 neuac Drugs 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- UHDGCWIWMRVCDJ-UHFFFAOYSA-N 1-beta-D-Xylofuranosyl-NH-Cytosine Natural products O=C1N=C(N)C=CN1C1C(O)C(O)C(CO)O1 UHDGCWIWMRVCDJ-UHFFFAOYSA-N 0.000 description 1
- 101710136191 Beta-galactoside alpha-2,6-sialyltransferase 1 Proteins 0.000 description 1
- 102100029945 Beta-galactoside alpha-2,6-sialyltransferase 1 Human genes 0.000 description 1
- TXCIAUNLDRJGJZ-UHFFFAOYSA-N CMP-N-acetyl neuraminic acid Natural products O1C(C(O)C(O)CO)C(NC(=O)C)C(O)CC1(C(O)=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(N=C(N)C=C2)=O)O1 TXCIAUNLDRJGJZ-UHFFFAOYSA-N 0.000 description 1
- 102100029962 CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase Human genes 0.000 description 1
- 101710136075 CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase Proteins 0.000 description 1
- HOEWKBQADMRCLO-UIUGZIMDSA-N CMP-N-glycoloyl-beta-neuraminic acid Chemical compound O=C1N=C(N)C=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)O[C@@]2(O[C@H]([C@H](NC(=O)CO)[C@@H](O)C2)[C@H](O)[C@H](O)CO)C(O)=O)O1 HOEWKBQADMRCLO-UIUGZIMDSA-N 0.000 description 1
- 108010013423 CMPacetylneuraminate monooxygenase Proteins 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- UHDGCWIWMRVCDJ-PSQAKQOGSA-N Cytidine Natural products O=C1N=C(N)C=CN1[C@@H]1[C@@H](O)[C@@H](O)[C@H](CO)O1 UHDGCWIWMRVCDJ-PSQAKQOGSA-N 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 102000051366 Glycosyltransferases Human genes 0.000 description 1
- 101000863864 Homo sapiens Beta-galactoside alpha-2,6-sialyltransferase 1 Proteins 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 101710179749 N-acetylmannosamine kinase Proteins 0.000 description 1
- 108010035265 N-acetylneuraminate synthase Proteins 0.000 description 1
- SQVRNKJHWKZAKO-LUWBGTNYSA-N N-acetylneuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)CC(O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-LUWBGTNYSA-N 0.000 description 1
- 108010029147 N-acylmannosamine kinase Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 101710178100 Probable UDP-N-acetylglucosamine 2-epimerase Proteins 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- 101710086464 Putative UDP-N-acetylglucosamine 2-epimerase Proteins 0.000 description 1
- 101000863866 Rattus norvegicus Beta-galactoside alpha-2,6-sialyltransferase 1 Proteins 0.000 description 1
- 108091006161 SLC17A5 Proteins 0.000 description 1
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- 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 1
- 101710091363 UDP-N-acetylglucosamine 2-epimerase Proteins 0.000 description 1
- 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 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000003796 beauty Effects 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 125000001314 canonical amino-acid group Chemical group 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 238000004624 confocal microscopy Methods 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- UHDGCWIWMRVCDJ-ZAKLUEHWSA-N cytidine Chemical compound O=C1N=C(N)C=CN1[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O1 UHDGCWIWMRVCDJ-ZAKLUEHWSA-N 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 108700014210 glycosyltransferase activity proteins Proteins 0.000 description 1
- 102000045442 glycosyltransferase activity proteins Human genes 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 210000004898 n-terminal fragment Anatomy 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 230000010474 transient expression Effects 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP06290843 | 2006-05-24 | ||
| PCT/EP2007/055070 WO2007135194A2 (en) | 2006-05-24 | 2007-05-24 | Preparation and uses of gene sequences encoding chimerical glycosyltransferases with optimized glycosylation activity |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2009537165A JP2009537165A (ja) | 2009-10-29 |
| JP2009537165A5 true JP2009537165A5 (https=) | 2010-07-15 |
Family
ID=36659871
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2009511529A Pending JP2009537165A (ja) | 2006-05-24 | 2007-05-24 | 最適化されたグリコシル化活性を有するキメラ・グリコシルトランスフェラーゼをコードする遺伝子配列の製造及び使用 |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US8993297B2 (https=) |
| EP (1) | EP2019864B1 (https=) |
| JP (1) | JP2009537165A (https=) |
| AT (1) | ATE516346T1 (https=) |
| CA (1) | CA2653104C (https=) |
| DK (1) | DK2019864T3 (https=) |
| ES (1) | ES2368267T3 (https=) |
| PL (1) | PL2019864T3 (https=) |
| PT (1) | PT2019864E (https=) |
| WO (1) | WO2007135194A2 (https=) |
Families Citing this family (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2908407C (en) | 2013-05-29 | 2022-06-14 | F. Hoffmann-La Roche Ag | Quantitative control of sialylation |
| EP3017057B1 (en) | 2013-07-05 | 2019-10-02 | F.Hoffmann-La Roche Ag | Process for the mono- and bi-sialylation of glycoproteins employing n-terminally truncated beta-galactoside alpha-2,6-sialyltransferase mutants |
| EP2821482A1 (en) * | 2013-07-05 | 2015-01-07 | Roche Diagniostics GmbH | N-terminally truncated glycosyltransferases |
| EP2824176A1 (en) | 2013-07-11 | 2015-01-14 | Siamed'xpress | Methods for producing sialylated therapeutic proteins |
| US9616114B1 (en) | 2014-09-18 | 2017-04-11 | David Gordon Bermudes | Modified bacteria having improved pharmacokinetics and tumor colonization enhancing antitumor activity |
| WO2016102436A1 (en) * | 2014-12-22 | 2016-06-30 | F. Hoffmann-La Roche Ag | Cmp-dependent sialidase activity |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| PL240405B1 (pl) * | 2017-07-24 | 2022-03-28 | Zakl Farmaceutyczne Polpharma Spolka Akcyjna | Przeciwciało monoklonalne oraz sposób jego otrzymywania |
| BR112022013071A2 (pt) * | 2020-01-06 | 2022-09-20 | Igm Biosciences Inc | Moléculas de ligação multiméricas altamente sialiladas |
| WO2023141513A2 (en) * | 2022-01-19 | 2023-07-27 | The Regents Of The University Of California | Functionalized human milk oligosaccharides and methods for producing them |
| WO2025088103A1 (en) * | 2023-10-26 | 2025-05-01 | Inbiose N.V. | Production of a sialylated compound |
| WO2025088102A1 (en) * | 2023-10-26 | 2025-05-01 | Inbiose N.V. | PRODUCTION OF A SIALYLATED OLIGOSACCHARIDE COMPRISING GAL-β1,3-[NEU5AC-A2,6]-HEXNAC-R |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ATE374816T1 (de) | 1996-08-02 | 2007-10-15 | Austin Research Inst | Verbesserte nukleinsäuren, welche für eine chimäre glycosyltransferase kodieren |
| US7244601B2 (en) * | 1997-12-15 | 2007-07-17 | National Research Council Of Canada | Fusion proteins for use in enzymatic synthesis of oligosaccharides |
| US7598055B2 (en) * | 2000-06-28 | 2009-10-06 | Glycofi, Inc. | N-acetylglucosaminyltransferase III expression in lower eukaryotes |
| ES2252261T3 (es) | 2000-06-28 | 2006-05-16 | Glycofi, Inc. | Metodos para producir glicoproteinas modificadas. |
| AU2002352253A1 (en) * | 2001-12-18 | 2003-06-30 | Bayer Healthcare Ag | Regulation of human sialyltransferase |
| US7569376B2 (en) * | 2002-05-03 | 2009-08-04 | Neose Technologies, Inc. | Fucosyltransferase fusion protein |
-
2007
- 2007-05-24 ES ES07729499T patent/ES2368267T3/es active Active
- 2007-05-24 EP EP07729499A patent/EP2019864B1/en not_active Not-in-force
- 2007-05-24 PT PT07729499T patent/PT2019864E/pt unknown
- 2007-05-24 DK DK07729499.9T patent/DK2019864T3/da active
- 2007-05-24 AT AT07729499T patent/ATE516346T1/de active
- 2007-05-24 PL PL07729499T patent/PL2019864T3/pl unknown
- 2007-05-24 WO PCT/EP2007/055070 patent/WO2007135194A2/en not_active Ceased
- 2007-05-24 US US12/301,914 patent/US8993297B2/en not_active Expired - Fee Related
- 2007-05-24 JP JP2009511529A patent/JP2009537165A/ja active Pending
- 2007-05-24 CA CA2653104A patent/CA2653104C/en not_active Expired - Fee Related
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