JP2006502705A5 - - Google Patents
Download PDFInfo
- Publication number
- JP2006502705A5 JP2006502705A5 JP2004516676A JP2004516676A JP2006502705A5 JP 2006502705 A5 JP2006502705 A5 JP 2006502705A5 JP 2004516676 A JP2004516676 A JP 2004516676A JP 2004516676 A JP2004516676 A JP 2004516676A JP 2006502705 A5 JP2006502705 A5 JP 2006502705A5
- Authority
- JP
- Japan
- Prior art keywords
- gene
- pastoris
- aox1
- panel
- promoter
- 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.)
- Pending
Links
- 108090000623 proteins and genes Proteins 0.000 description 34
- 241000235058 Komagataella pastoris Species 0.000 description 33
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 22
- 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 22
- 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 22
- 102100036826 Aldehyde oxidase Human genes 0.000 description 21
- 101000928314 Homo sapiens Aldehyde oxidase Proteins 0.000 description 21
- 101150061302 och1 gene Proteins 0.000 description 21
- 239000003550 marker Substances 0.000 description 20
- 239000013598 vector Substances 0.000 description 19
- 108091026890 Coding region Proteins 0.000 description 18
- 238000004458 analytical method Methods 0.000 description 18
- 101150061183 AOX1 gene Proteins 0.000 description 17
- 230000005030 transcription termination Effects 0.000 description 14
- 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 13
- 108010004486 trans-sialidase Proteins 0.000 description 13
- 102100021771 Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase Human genes 0.000 description 11
- 239000013604 expression vector Substances 0.000 description 11
- LXJXRIRHZLFYRP-UHFFFAOYSA-N glyceraldehyde 3-phosphate Chemical compound O=CC(O)COP(O)(O)=O LXJXRIRHZLFYRP-UHFFFAOYSA-N 0.000 description 11
- 108010009689 mannosyl-oligosaccharide 1,2-alpha-mannosidase Proteins 0.000 description 11
- 108010029607 4-nitrophenyl-alpha-glucosidase Proteins 0.000 description 10
- 102100025961 Glutaminase liver isoform, mitochondrial Human genes 0.000 description 10
- 101000856993 Homo sapiens Glutaminase liver isoform, mitochondrial Proteins 0.000 description 10
- 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 9
- 229960000723 ampicillin Drugs 0.000 description 9
- 102000004169 proteins and genes Human genes 0.000 description 9
- 230000010076 replication Effects 0.000 description 9
- 108700026244 Open Reading Frames Proteins 0.000 description 8
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 8
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 8
- 238000003556 assay Methods 0.000 description 8
- 210000004027 cell Anatomy 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- 241000499912 Trichoderma reesei Species 0.000 description 7
- 238000000034 method Methods 0.000 description 7
- 108010070113 alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase I Proteins 0.000 description 6
- 230000004927 fusion Effects 0.000 description 6
- 230000035897 transcription Effects 0.000 description 6
- 238000013518 transcription Methods 0.000 description 6
- OSKIPPQETUTOMW-YHLOVPAPSA-N N-[(2R,3R,4R,5S,6R)-5-[(2S,3R,4R,5S,6R)-3-Acetamido-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5S,6R)-3-[(2S,3S,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-[[(2S,3S,4S,5R,6R)-6-[[(2S,3S,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxymethyl]-3,5-dihydroxy-4-[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxymethyl]-3,5-dihydroxyoxan-2-yl]oxy-4-hydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-2,4-dihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide Chemical compound O[C@@H]1[C@@H](NC(=O)C)[C@H](O)O[C@H](CO)[C@H]1O[C@H]1[C@H](NC(C)=O)[C@@H](O)[C@H](O[C@@H]2[C@H]([C@@H](O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O)[C@H](O)[C@@H](CO[C@@H]3[C@H]([C@@H](O[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O)[C@H](O)[C@@H](CO[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O)O3)O)O2)O)[C@@H](CO)O1 OSKIPPQETUTOMW-YHLOVPAPSA-N 0.000 description 5
- 108010068204 Peptide Elongation Factors Proteins 0.000 description 5
- 238000010276 construction Methods 0.000 description 5
- 230000002779 inactivation Effects 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 108090000765 processed proteins & peptides Proteins 0.000 description 5
- 230000005029 transcription elongation Effects 0.000 description 5
- 101150006240 AOX2 gene Proteins 0.000 description 4
- 101150005709 ARG4 gene Proteins 0.000 description 4
- 101150004278 CYC1 gene Proteins 0.000 description 4
- 108010007528 Cytochromes c1 Proteins 0.000 description 4
- 102100039371 ER lumen protein-retaining receptor 1 Human genes 0.000 description 4
- 108090000288 Glycoproteins Proteins 0.000 description 4
- 102000003886 Glycoproteins Human genes 0.000 description 4
- 101710154606 Hemagglutinin Proteins 0.000 description 4
- 101000812437 Homo sapiens ER lumen protein-retaining receptor 1 Proteins 0.000 description 4
- 102100024295 Maltase-glucoamylase Human genes 0.000 description 4
- 108010054377 Mannosidases Proteins 0.000 description 4
- 102000001696 Mannosidases Human genes 0.000 description 4
- 101000615943 Mus musculus Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB Proteins 0.000 description 4
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 4
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 4
- 101710176177 Protein A56 Proteins 0.000 description 4
- FYGDTMLNYKFZSV-DZOUCCHMSA-N alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-D-Glcp Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)O[C@H](O[C@@H]2[C@H](OC(O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-DZOUCCHMSA-N 0.000 description 4
- 108010028144 alpha-Glucosidases Proteins 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 101150073818 gap gene Proteins 0.000 description 4
- 239000000185 hemagglutinin Substances 0.000 description 4
- 108010083819 mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase Proteins 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 230000009466 transformation Effects 0.000 description 4
- SBKVPJHMSUXZTA-MEJXFZFPSA-N (2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-5-amino-2-[[2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoyl]amino]-5-oxopentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]amino]-4-methylsulfanylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoic acid Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 SBKVPJHMSUXZTA-MEJXFZFPSA-N 0.000 description 3
- 102000004856 Lectins Human genes 0.000 description 3
- 108090001090 Lectins Proteins 0.000 description 3
- DINOPBPYOCMGGD-VEDJBHDQSA-N Man(a1-2)Man(a1-2)Man(a1-3)[Man(a1-2)Man(a1-3)[Man(a1-2)Man(a1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc Chemical compound O[C@@H]1[C@@H](NC(=O)C)C(O)O[C@H](CO)[C@H]1O[C@H]1[C@H](NC(C)=O)[C@@H](O)[C@H](O[C@H]2[C@H]([C@@H](O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O)[C@H](O)[C@@H](CO[C@@H]3[C@H]([C@@H](O[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O)[C@H](O)[C@@H](CO[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O[C@@H]4[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O)O3)O)O2)O)[C@@H](CO)O1 DINOPBPYOCMGGD-VEDJBHDQSA-N 0.000 description 3
- 108010038049 Mating Factor Proteins 0.000 description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 description 3
- 101150050575 URA3 gene Proteins 0.000 description 3
- 210000002421 cell wall Anatomy 0.000 description 3
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 3
- 239000002523 lectin Substances 0.000 description 3
- 108010066476 ribonuclease B Proteins 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 2
- 101150069554 HIS4 gene Proteins 0.000 description 2
- 101001079065 Homo sapiens Ras-related protein Rab-1A Proteins 0.000 description 2
- 108010087568 Mannosyltransferases Proteins 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 102000006010 Protein Disulfide-Isomerase Human genes 0.000 description 2
- 102100028191 Ras-related protein Rab-1A Human genes 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 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 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 239000012491 analyte Substances 0.000 description 2
- 102000007478 beta-N-Acetylhexosaminidases Human genes 0.000 description 2
- 108010085377 beta-N-Acetylhexosaminidases Proteins 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 238000000799 fluorescence microscopy Methods 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 230000006801 homologous recombination Effects 0.000 description 2
- 238000002744 homologous recombination Methods 0.000 description 2
- 206010022000 influenza Diseases 0.000 description 2
- 230000004807 localization Effects 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 210000004940 nucleus Anatomy 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 108020003519 protein disulfide isomerase Proteins 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- 101150033853 ypt-1 gene Proteins 0.000 description 2
- VRYALKFFQXWPIH-RANCGNPWSA-N (3r,4s,5r)-3,4,5,6-tetrahydroxy-2-tritiohexanal Chemical compound O=CC([3H])[C@@H](O)[C@H](O)[C@H](O)CO VRYALKFFQXWPIH-RANCGNPWSA-N 0.000 description 1
- YYYARFHFWYKNLF-UHFFFAOYSA-N 4-[(2,4-dimethylphenyl)diazenyl]-3-hydroxynaphthalene-2,7-disulfonic acid Chemical compound CC1=CC(C)=CC=C1N=NC1=C(O)C(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=C12 YYYARFHFWYKNLF-UHFFFAOYSA-N 0.000 description 1
- 101150061009 C1 gene Proteins 0.000 description 1
- 108010052832 Cytochromes Proteins 0.000 description 1
- 102000018832 Cytochromes Human genes 0.000 description 1
- 101100239628 Danio rerio myca gene Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 230000005526 G1 to G0 transition Effects 0.000 description 1
- 102000006722 Mannosyltransferases Human genes 0.000 description 1
- 241000235648 Pichia Species 0.000 description 1
- 101900248848 Saccharomyces cerevisiae Transcription elongation factor 1 Proteins 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 241000223259 Trichoderma Species 0.000 description 1
- 240000001417 Vigna umbellata Species 0.000 description 1
- 235000011453 Vigna umbellata Nutrition 0.000 description 1
- 238000013096 assay test Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 108020001778 catalytic domains Proteins 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000000432 density-gradient centrifugation Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000010185 immunofluorescence analysis Methods 0.000 description 1
- 238000010820 immunofluorescence microscopy Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 210000000633 nuclear envelope Anatomy 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 239000007981 phosphate-citrate buffer Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000004611 spectroscopical analysis Methods 0.000 description 1
- 230000004960 subcellular localization Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
- 239000007221 ypg medium Substances 0.000 description 1
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US10/185,475 US7252933B2 (en) | 2002-06-26 | 2002-06-26 | Protein glycosylation modification in methylotrophic yeast |
| PCT/EP2003/006711 WO2004003194A2 (en) | 2002-06-26 | 2003-06-25 | Protein glycosylation modification in pichia pastoris |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2006502705A JP2006502705A (ja) | 2006-01-26 |
| JP2006502705A5 true JP2006502705A5 (https=) | 2006-04-27 |
Family
ID=29999263
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2004516676A Pending JP2006502705A (ja) | 2002-06-26 | 2003-06-25 | ピキアパストリス（Ｐｉｃｈｉａｐａｓｔｏｒｉｓ）におけるタンパク質グリコシル化修飾 |
Country Status (10)
| Country | Link |
|---|---|
| US (2) | US7252933B2 (https=) |
| EP (2) | EP2302047A1 (https=) |
| JP (1) | JP2006502705A (https=) |
| KR (1) | KR101047167B1 (https=) |
| AU (1) | AU2003238051B2 (https=) |
| CA (1) | CA2490268C (https=) |
| IL (2) | IL165717A0 (https=) |
| MX (1) | MXPA04012983A (https=) |
| NO (1) | NO20050410L (https=) |
| WO (1) | WO2004003194A2 (https=) |
Families Citing this family (34)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7625756B2 (en) * | 2000-06-28 | 2009-12-01 | GycoFi, Inc. | Expression of class 2 mannosidase and class III mannosidase in lower eukaryotic cells |
| US7449308B2 (en) | 2000-06-28 | 2008-11-11 | Glycofi, Inc. | Combinatorial DNA library for producing modified N-glycans in lower eukaryotes |
| US7598055B2 (en) | 2000-06-28 | 2009-10-06 | Glycofi, Inc. | N-acetylglucosaminyltransferase III expression in lower eukaryotes |
| US7863020B2 (en) | 2000-06-28 | 2011-01-04 | Glycofi, Inc. | Production of sialylated N-glycans in lower eukaryotes |
| EP1294910B1 (en) * | 2000-06-30 | 2008-11-19 | VIB vzw | Protein glycosylation modification in pichia pastoris |
| US7332299B2 (en) | 2003-02-20 | 2008-02-19 | Glycofi, Inc. | Endomannosidases in the modification of glycoproteins in eukaryotes |
| US7507573B2 (en) * | 2003-11-14 | 2009-03-24 | Vib, Vzw | Modification of protein glycosylation in methylotrophic yeast |
| WO2006026992A1 (en) * | 2004-09-07 | 2006-03-16 | Novozymes A/S | Altered structure of n-glycans in a fungus |
| EP1934605B1 (en) * | 2005-09-22 | 2014-03-26 | Prosci Incorporated | Glycosylated polypeptides produced in yeast mutants and methods of use thereof |
| KR101105718B1 (ko) | 2005-10-27 | 2012-01-17 | 한국생명공학연구원 | 돌리칠 포스페이트 만노스 의존알파-1,3-만노실트랜스퍼라제를 코딩하는 한세눌라폴리모르파 기원의 신규 유전자와 상기 유전자가 결손된한세눌라 폴리모르파 변이주를 이용한 재조합 당단백질생산 방법 |
| FR2912154B1 (fr) * | 2007-02-02 | 2012-11-02 | Glycode | Levures genetiquement modifiees pour la production de glycoproteines homogenes |
| CA2887752C (en) * | 2007-04-03 | 2020-03-24 | Vib Vzw | Glycosylation of molecules |
| EP2435476A4 (en) * | 2009-05-27 | 2013-04-17 | Synageva Biopharma Corp | ANTIBODIES OBTAINED FROM BIRDS |
| KR102000383B1 (ko) | 2009-09-29 | 2019-07-15 | 유니버시테이트 젠트 | 만노스-1-포스포-6-만노스 결합의 포스포-6-만노스로의 가수분해 |
| EP2494050A4 (en) * | 2009-10-30 | 2013-10-30 | Merck Sharp & Dohme | GRANULOCYTIC COLONY STIMULATING FACTOR MADE IN GLYCOENGINEERED PICHIA PASTORIS |
| US20130011875A1 (en) * | 2009-10-30 | 2013-01-10 | Merck Sharpe & Dohme Corp | Methods for the production of recombinant proteins with improved secretion efficiencies |
| WO2011061629A2 (en) * | 2009-11-19 | 2011-05-26 | Oxyrane Uk Limited | Yeast strains producing mammalian-like complex n-glycans |
| US9347050B2 (en) | 2010-09-29 | 2016-05-24 | Oxyrane Uk Limited | Mannosidases capable of uncapping mannose-1-phospho-6-mannose linkages and demannosylating phosphorylated N-glycans and methods of facilitating mammalian cellular uptake of glycoproteins |
| CA2812872C (en) | 2010-09-29 | 2021-08-03 | Oxyrane Uk Limited | De-mannosylation of phosphorylated n-glycans |
| WO2012170292A1 (en) * | 2011-06-07 | 2012-12-13 | Merck Sharp & Dohme Corp. | Modulation of metabolic pathways for improving bioprocess performance and secreted protein productivity of yeast |
| CN104024849A (zh) | 2011-08-12 | 2014-09-03 | 生命科技公司 | 用于高通量聚糖分析的装置、方法、计算机程序产品和试剂盒 |
| EP3628326B1 (en) | 2012-03-15 | 2024-02-28 | Oxyrane UK Limited | Methods and materials for treatment of pompe's disease |
| US9764006B2 (en) | 2012-12-10 | 2017-09-19 | The General Hospital Corporation | Bivalent IL-2 fusion toxins |
| US9944689B2 (en) | 2013-03-07 | 2018-04-17 | The General Hospital Corporation | Human CTLA4 mutants and use thereof |
| WO2015100058A1 (en) * | 2013-12-23 | 2015-07-02 | Research Corporation Technologies, Inc. | Pichia pastoris surface display system |
| SG11201700446XA (en) | 2014-07-21 | 2017-02-27 | Glykos Finland Oy | Production of glycoproteins with mammalian-like n-glycans in filamentous fungi |
| WO2016077457A1 (en) | 2014-11-11 | 2016-05-19 | Clara Foods Co. | Methods and compositions for egg white protein production |
| JP2021534763A (ja) * | 2018-08-21 | 2021-12-16 | クララ フーズ カンパニー | 微生物におけるタンパク質のグリコシル化の修飾 |
| EP3931330A4 (en) | 2019-02-25 | 2023-03-15 | Ginkgo Bioworks, Inc. | BIOSYNTHESIS OF CANNABINOIDS AND CANNABINOID PRECURSORS |
| KR20220034848A (ko) | 2019-07-11 | 2022-03-18 | 클라라 푸드즈 컴퍼니 | 단백질 조성물 및 이의 섭취 가능한 제품 |
| US12096784B2 (en) | 2019-07-11 | 2024-09-24 | Clara Foods Co. | Protein compositions and consumable products thereof |
| US10927360B1 (en) | 2019-08-07 | 2021-02-23 | Clara Foods Co. | Compositions comprising digestive enzymes |
| WO2022108839A1 (en) * | 2020-11-17 | 2022-05-27 | Ginkgo Bioworks, Inc. | Synthetic methanol inducible promoters and uses thereof |
| US11639515B2 (en) * | 2021-05-21 | 2023-05-02 | Taixing Dongsheng Bio-Tech Co., Ltd | Genetically engineered strain for producing porcine myoglobin and food-grade fermentation and purification thereof |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US137134A (en) * | 1873-03-25 | Improvement in locomotive spark-arresters | ||
| US4879231A (en) | 1984-10-30 | 1989-11-07 | Phillips Petroleum Company | Transformation of yeasts of the genus pichia |
| US4855231A (en) | 1984-10-30 | 1989-08-08 | Phillips Petroleum Company | Regulatory region for heterologous gene expression in yeast |
| US4837148A (en) | 1984-10-30 | 1989-06-06 | Phillips Petroleum Company | Autonomous replication sequences for yeast strains of the genus pichia |
| US4882279A (en) | 1985-10-25 | 1989-11-21 | Phillips Petroleum Company | Site selective genomic modification of yeast of the genus pichia |
| US4818700A (en) | 1985-10-25 | 1989-04-04 | Phillips Petroleum Company | Pichia pastoris argininosuccinate lyase gene and uses thereof |
| US4812405A (en) | 1986-02-18 | 1989-03-14 | Phillips Petroleum Company | Double auxotrophic mutants of Pichia pastoris and methods for preparation |
| US4929555A (en) | 1987-10-19 | 1990-05-29 | Phillips Petroleum Company | Pichia transformation |
| US5080522A (en) | 1988-12-13 | 1992-01-14 | Shafirkin David I | Device for locking and sealing of objects |
| WO1992009694A2 (en) | 1990-11-30 | 1992-06-11 | Hsc Research And Development Limited Partnership | CLONING OF UDP-N-ACETYLGLUCOSAMINE:α-3-D-MANNOSIDE β-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE I |
| US5358967A (en) | 1993-07-06 | 1994-10-25 | Rohm And Haas Company | Wool protecting compositons and methods |
| US5834251A (en) * | 1994-12-30 | 1998-11-10 | Alko Group Ltd. | Methods of modifying carbohydrate moieties |
| DE60032370T2 (de) | 1999-08-19 | 2007-10-11 | Kirin Beer K.K. | Hefevarianten und verfahren zur herstellung von glykoprotein enthaltenden zuckerketten vom säugetiertyp |
| ES2252261T3 (es) * | 2000-06-28 | 2006-05-16 | Glycofi, Inc. | Metodos para producir glicoproteinas modificadas. |
| EP1294910B1 (en) | 2000-06-30 | 2008-11-19 | VIB vzw | Protein glycosylation modification in pichia pastoris |
-
2002
- 2002-06-26 IL IL16571702A patent/IL165717A0/xx unknown
- 2002-06-26 US US10/185,475 patent/US7252933B2/en not_active Expired - Lifetime
-
2003
- 2003-06-25 AU AU2003238051A patent/AU2003238051B2/en not_active Expired
- 2003-06-25 WO PCT/EP2003/006711 patent/WO2004003194A2/en not_active Ceased
- 2003-06-25 KR KR1020047021319A patent/KR101047167B1/ko not_active Expired - Lifetime
- 2003-06-25 JP JP2004516676A patent/JP2006502705A/ja active Pending
- 2003-06-25 EP EP10011710A patent/EP2302047A1/en not_active Ceased
- 2003-06-25 CA CA2490268A patent/CA2490268C/en not_active Expired - Lifetime
- 2003-06-25 EP EP03735682A patent/EP1516048A2/en not_active Withdrawn
- 2003-06-25 MX MXPA04012983A patent/MXPA04012983A/es active IP Right Grant
-
2004
- 2004-12-12 IL IL165717A patent/IL165717A/en active IP Right Grant
-
2005
- 2005-01-25 NO NO20050410A patent/NO20050410L/no unknown
-
2007
- 2007-07-13 US US11/827,998 patent/US8883445B2/en not_active Expired - Fee Related
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2006502705A5 (https=) | ||
| US9359628B2 (en) | Protein glycosylation modification in methylotrophic yeast | |
| US8883445B2 (en) | Protein glycosylation modification in methylotrophic yeast | |
| JP4794455B2 (ja) | メチロトローフ酵母における蛋白質グリコシル化の修飾 | |
| EP1505149B1 (en) | Methylotroph yeast producing mammalian type sugar chain | |
| JP6407872B2 (ja) | 主に均一なグリカン構造を生成するためのピキア・パストリス（Ｐｉｃｈｉａｐａｓｔｏｒｉｓ）株 | |
| JP2004501642A (ja) | 改変された糖タンパク質を生成するための方法 | |
| AU2001277658A1 (en) | Protein glycosylation modification in pichia pastoris | |
| US20130040897A1 (en) | Glycosylation of proteins in host cells | |
| Kainz et al. | N-glycan modification in Aspergillus species | |
| Oh et al. | Glycoengineering of the methylotrophic yeast Hansenula polymorpha for the production of glycoproteins with trimannosyl core N‐glycan by blocking core oligosaccharide assembly | |
| CN104066841B (zh) | 表达载体和蛋白质的制造方法 | |
| JP5885191B2 (ja) | 糖鎖改変酵母及びそれを用いた糖タンパク質の製造方法 | |
| CN1918297B (zh) | 编码α1,6-甘露糖基转移酶的新的多形汉逊氏酵母基因和用同一基因有缺陷的多形汉逊氏酵母突变株生产重组糖蛋白的方法 | |
| US8003349B2 (en) | YLMPO1 gene derived from yarrowia lipolytica and a process for preparing a glycoprotein not being mannosylphosphorylated by using a mutated yarrowia lipolytica in which YLMPO1 gene is disrupted | |
| EP3788164A1 (en) | Recombinant organisms and methods for producing glycomolecules with high glycan occupancy | |
| WO2004003205A1 (en) | Hansenula polymorpha mutant strains with defect in outer chain biosynthesis and the production of recombinant glycoproteins using the same strains | |
| Barnay-Verdier et al. | New components of Yarrowia lipolytica Golgi multi-protein complexes containing the α-1, 6-mannosyltransferases YlMnn9p and YlAnl1p |