메뉴 건너뛰기




Volumn 3, Issue , 2013, Pages

Knockout of an endogenous mannosyltransferase increases the homogeneity of glycoproteins produced in Pichia pastoris

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; GLYCOPROTEIN; MANNOSE BINDING LECTIN; MANNOSYLTRANSFERASE; POLYSACCHARIDE; RECOMBINANT PROTEIN;

EID: 84888260046     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep03279     Document Type: Article
Times cited : (62)

References (54)
  • 2
    • 0032790856 scopus 로고    scopus 로고
    • High-yield secretion of recombinant gelatins by Pichia pastoris
    • DOI 10.1002/(SICI)1097-0061(199908) 15:11<1087::AID-YEA436>3.0. CO;2-F
    • Werten,M.W., van den Bosch, T. J., Wind, R. D.,Mooibroek, H. & deWolf, F. A. High-yield secretion of recombinant gelatins by Pichia pastoris. Yeast 15, 1087-1096 (1999). (Pubitemid 29387023)
    • (1999) Yeast , vol.15 , Issue.11 , pp. 1087-1096
    • Werten, M.W.T.1    Van Den Bosch, T.J.2    Wind, R.D.3    Mooibroek, H.4    De Wolf, F.A.5
  • 3
  • 4
    • 0036669602 scopus 로고    scopus 로고
    • Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris
    • DOI 10.1016/S0958-1669(02)00330-0
    • Lin-Cereghino, G. P., Lin-Cereghino, J., Ilgen, C. & Cregg, J. M. Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris. Curr. Opin. Biotechnol. 13, 329-332 (2002). (Pubitemid 35254090)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.4 , pp. 329-332
    • Cereghino G.P.Lin1    Cereghino, J.L.2    Ilgen, C.3    Cregg, J.M.4
  • 5
    • 0345497769 scopus 로고
    • Effects of glycosylation on protein function
    • Parekh, R. B. Effects of glycosylation on protein function. Curr. Opin. Struct. Biol. 1, 750-754 (1991). (Pubitemid 121002422)
    • (1991) Current Opinion in Structural Biology , vol.1 , Issue.5 , pp. 750-754
    • Parekh, R.B.1
  • 6
    • 24944582121 scopus 로고    scopus 로고
    • Development of a S cerevisiae whole cell biocatalyst for in vitro sialylation of oligosaccharides
    • DOI 10.1016/j.jbiotec.2005.04.010, PII S0168165605001914
    • Ryckaert, S., Martens, V., De Vusser, K. & Contreras, R. Development of a S. cerevisiae whole cell biocatalyst for in vitro sialylation of oligosaccharides. J. Biotechnol. 119, 379-388 (2005). (Pubitemid 41330756)
    • (2005) Journal of Biotechnology , vol.119 , Issue.4 , pp. 379-388
    • Ryckaert, S.1    Martens, V.2    Vusser, K.D.3    Contreras, R.4
  • 7
    • 13444262282 scopus 로고    scopus 로고
    • The humanization of N-glycosylation pathways in yeast
    • DOI 10.1038/nrmicro1087
    • Wildt, S. & Gerngross, T. U. The humanization of N-glycosylation pathways in yeast. Nat. Rev. Microbiol. 3, 119-128 (2005). (Pubitemid 40207593)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.2 , pp. 119-128
    • Wildt, S.1    Gerngross, T.U.2
  • 8
    • 36149001292 scopus 로고    scopus 로고
    • Glycosylation engineering in yeast: The advent of fully humanized yeast
    • DOI 10.1016/j.copbio.2007.09.001, PII S0958166907001139, Expression Technologies / Tissue and Cell Engineering
    • Hamilton, S. R. & Gerngross, T. U. Glycosylation engineering in yeast: the advent of fully humanized yeast. Curr. Opin. Biotechnol. 18, 387-392 (2007). (Pubitemid 350116586)
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.5 , pp. 387-392
    • Hamilton, S.R.1    Gerngross, T.U.2
  • 9
    • 77955558145 scopus 로고    scopus 로고
    • Engineering of glycosylation in yeast and other fungi: Current state and perspectives
    • De Pourcq, K., De Schutter, K. & Callewaert, N. Engineering of glycosylation in yeast and other fungi: current state and perspectives. Appl. Microbiol. Biotechnol. 87, 1617-1631 (2010).
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 1617-1631
    • De Pourcq, K.1    De Schutter, K.2    Callewaert, N.3
  • 10
    • 2442661971 scopus 로고    scopus 로고
    • In vivo synthesis of mammalian-like, hybrid-type N-glycans in Pichia pastoris
    • Vervecken,W. et al. In vivo synthesis of mammalian-like, hybrid-type N-glycans in Pichia pastoris. Appl. Environ. Microbiol. 70, 2639-2646 (2004).
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2639-2646
    • Verveckenw1
  • 11
    • 0026625118 scopus 로고
    • Isolation of new temperature-sensitive mutants of Saccharomyces cerevisiae deficient in mannose outer chain elongation
    • Nagasu, T. et al. Isolation of new temperature-sensitive mutants of Saccharomyces cerevisiae deficient in mannose outer chain elongation. Yeast 8, 535-547 (1992).
    • (1992) Yeast , vol.8 , pp. 535-547
    • Nagasu, T.1
  • 12
    • 0026749963 scopus 로고
    • OCH1 encodes a novel membrane bound mannosyltransferase: Outer chain elongation of asparagine-linked oligosaccharides
    • Nakayama, K., Nagasu, T., Shimma, Y., Kuromitsu, J. & Jigami, Y. OCH1 encodes a novel membrane bound mannosyltransferase: outer chain elongation of asparagine-linked oligosaccharides. EMBO J. 11, 2511-2519 (1992).
    • (1992) EMBO J. , vol.11 , pp. 2511-2519
    • Nakayama, K.1    Nagasu, T.2    Shimma, Y.3    Kuromitsu, J.4    Jigami, Y.5
  • 14
    • 44349164573 scopus 로고    scopus 로고
    • Identification of a new family of genes involved in beta-1,2- mannosylation of glycans in Pichia pastoris and Candida albicans
    • Mille, C. et al. Identification of a new family of genes involved in beta-1,2-mannosylation of glycans in Pichia pastoris and Candida albicans. J. Biol. Chem. 283, 9724-9736 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 9724-9736
    • Mille, C.1
  • 15
    • 0742324902 scopus 로고    scopus 로고
    • Horseradish peroxidase: A modern view of a classic enzyme
    • DOI 10.1016/j.phytochem.2003.10.022
    • Veitch, N. C. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry 65, 249-259 (2004). (Pubitemid 38147341)
    • (2004) Phytochemistry , vol.65 , Issue.3 , pp. 249-259
    • Veitch, N.C.1
  • 16
    • 79952100002 scopus 로고    scopus 로고
    • A dynamic method based on the specific substrate uptake rate to set up a feeding strategy for Pichia pastoris
    • Dietzsch, C., Spadiut, O. & Herwig, C. A dynamic method based on the specific substrate uptake rate to set up a feeding strategy for Pichia pastoris. Microb. Cell Fact. 10, 14-22 (2011).
    • (2011) Microb. Cell Fact. , vol.10 , pp. 14-22
    • Dietzsch, C.1    Spadiut, O.2    Herwig, C.3
  • 17
    • 0034088553 scopus 로고    scopus 로고
    • Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris
    • Morawski, B. et al. Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris. Protein Eng. 13, 377-384 (2000). (Pubitemid 30339361)
    • (2000) Protein Engineering , vol.13 , Issue.5 , pp. 377-384
    • Morawski, B.1    Lin, Z.2    Cirino, P.3    Joo, H.4    Bandara, G.5    Arnold, F.H.6
  • 18
    • 84863090270 scopus 로고    scopus 로고
    • Deletion of the Pichia pastoris KU70 homologue facilitates platform strain generation for gene expression and synthetic biology
    • Näätsaari, L. et al. Deletion of the Pichia pastoris KU70 homologue facilitates platform strain generation for gene expression and synthetic biology. PLoS ONE 7, e39720 (2012).
    • (2012) PLoS ONE , vol.7
    • Näätsaari, L.1
  • 19
    • 34547728712 scopus 로고    scopus 로고
    • Influence of N-glycosylation on Saccharomyces cerevisiae morphology: A Golgi glycosylation mutant shows cell division defects
    • DOI 10.1007/s00284-006-0585-5
    • Zhou, J., Zhang, H., Liu, X.,Wang, P. G. & Qi, Q. Influence of N-glycosylation on Saccharomyces cerevisiae morphology: a golgi glycosylation mutant shows cell division defects. Curr. Microbiol. 55, 198-204 (2007). (Pubitemid 47237939)
    • (2007) Current Microbiology , vol.55 , Issue.3 , pp. 198-204
    • Zhou, J.1    Zhang, H.2    Liu, X.3    Wang, P.G.4    Qi, Q.5
  • 22
    • 0024286486 scopus 로고
    • Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb
    • Shibuya, N., Goldstein, I. J., Van Damme, E. J. & Peumans, W. J. Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb. J. Biol. Chem. 263, 728-734 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 728-734
    • Shibuya, N.1    Goldstein, I.J.2    Van Damme, E.J.3    Peumans, W.J.4
  • 23
    • 60349092372 scopus 로고    scopus 로고
    • Related lectins from snowdrop and maize differ in their carbohydrate-binding specificity
    • Fouquaert, E. et al. Related lectins from snowdrop and maize differ in their carbohydrate-binding specificity. Biochem. Biophys. Res. Commun. 380, 260-265 (2009).
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 260-265
    • Fouquaert, E.1
  • 24
    • 80054905919 scopus 로고    scopus 로고
    • A fast approach to determine a fed batch feeding profile for recombinant Pichia pastoris strains
    • Dietzsch, C., Spadiut, O. & Herwig, C. A fast approach to determine a fed batch feeding profile for recombinant Pichia pastoris strains. Microb. Cell Fact. 10, 85-94 (2011).
    • (2011) Microb. Cell Fact. , vol.10 , pp. 85-94
    • Dietzsch, C.1    Spadiut, O.2    Herwig, C.3
  • 25
    • 84862219036 scopus 로고    scopus 로고
    • A dynamic fed batch strategy for a Pichia pastoris mixed feed system to increase process understanding
    • Zalai, D.,Dietzsch, C.,Herwig, C. &Spadiut, O. A dynamic fed batch strategy for a Pichia pastoris mixed feed system to increase process understanding. Biotechnol. Prog. 28, 878-886 (2012).
    • (2012) Biotechnol. Prog. , vol.28 , pp. 878-886
    • Zalai, D.1    Dietzsch, C.2    Herwig, C.3    Spadiut, O.4
  • 26
    • 84856790732 scopus 로고    scopus 로고
    • Recombinant protein expression in Pichia pastoris strains with an engineered methanol utilization pathway
    • Krainer, F. W. et al. Recombinant protein expression in Pichia pastoris strains with an engineered methanol utilization pathway. Microb. Cell Fact. 11, 22-35 (2012).
    • (2012) Microb. Cell Fact. , vol.11 , pp. 22-35
    • Krainer, F.W.1
  • 27
    • 84867591027 scopus 로고    scopus 로고
    • Purification of a recombinant plant peroxidase produced in Pichia pastoris by a simple 2-step strategy
    • Spadiut, O., Rossetti, L., Dietzsch, C. & Herwig, C. Purification of a recombinant plant peroxidase produced in Pichia pastoris by a simple 2-step strategy. Protein Expr. Purif. 86, 89-97 (2012).
    • (2012) Protein Expr. Purif. , vol.86 , pp. 89-97
    • Spadiut, O.1    Rossetti, L.2    Dietzsch, C.3    Herwig, C.4
  • 28
    • 58449130510 scopus 로고    scopus 로고
    • Improving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design
    • Spadiut, O. et al. Improving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design. FEBS J. 276, 776-792 (2009).
    • (2009) FEBS J. , vol.276 , pp. 776-792
    • Spadiut, O.1
  • 29
    • 84874676617 scopus 로고    scopus 로고
    • Enhancement of the gene targeting efficiency of non-conventional yeasts by increasing genetic redundancy
    • Chen, Z. et al. Enhancement of the gene targeting efficiency of non-conventional yeasts by increasing genetic redundancy. PLoS ONE 8, e57952 (2013).
    • (2013) PLoS ONE , vol.8
    • Chen, Z.1
  • 30
    • 0015216981 scopus 로고
    • Chitin and yeast budding.Localization of chitin in yeast bud scars
    • Cabib, E. & Bowers, B. Chitin and yeast budding. Localization of chitin in yeast bud scars. J. Biol. Chem. 246, 152-159 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 152-159
    • Cabib, E.1    Bowers, B.2
  • 32
    • 84865967993 scopus 로고    scopus 로고
    • Effect of bud scars on the mechanical properties of Saccharomyces cerevisiae cell walls
    • Chaudhari, R. D., Stenson, J. D., Overton, T. W. & Thomas, C. R. Effect of bud scars on the mechanical properties of Saccharomyces cerevisiae cell walls. Chem. Eng. Sci. 84, 188-196 (2012).
    • (2012) Chem. Eng. Sci. , vol.84 , pp. 188-196
    • Chaudhari, R.D.1    Stenson, J.D.2    Overton, T.W.3    Thomas, C.R.4
  • 33
    • 33645120423 scopus 로고    scopus 로고
    • Cell wall assembly in Saccharomyces cerevisiae
    • DOI 10.1128/MMBR.00038-05
    • Lesage, G.&Bussey,H. Cell wall assembly in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 70, 317-343 (2006). (Pubitemid 43895030)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.2 , pp. 317-343
    • Lesage, G.1    Bussey, H.2
  • 34
    • 20544439767 scopus 로고    scopus 로고
    • Features and functions of covalently linked proteins in fungal cell walls
    • DOI 10.1016/j.fgb.2005.04.002, PII S1087184505000654
    • De Groot, P. W. J., Ram, A. F. & Klis, F. M. Features and functions of covalently linked proteins in fungal cell walls. Fungal Genet. Biol. 42, 657-675 (2005). (Pubitemid 40848637)
    • (2005) Fungal Genetics and Biology , vol.42 , Issue.8 , pp. 657-675
    • De Groot, P.W.J.1    Ram, A.F.2    Klis, F.M.3
  • 35
    • 33645121842 scopus 로고    scopus 로고
    • Cell wall construction in Saccharomyces cerevisiae
    • Klis, F. M., Boorsma, A. & De Groot, P. W. J. Cell wall construction in Saccharomyces cerevisiae. Yeast 23, 185-202 (2006).
    • (2006) Yeast , vol.23 , pp. 185-202
    • Klis, F.M.1    Boorsma, A.2    De Groot, P.W.J.3
  • 37
    • 83255189440 scopus 로고    scopus 로고
    • The fine specificity of mannose-binding and galactose-binding lectins revealed using outlier motif analysis of glycan array data
    • Maupin, K. A., Liden, D. & Haab, B. B. The fine specificity of mannose-binding and galactose-binding lectins revealed using outlier motif analysis of glycan array data. Glycobiology 22, 160-169 (2012).
    • (2012) Glycobiology , vol.22 , pp. 160-169
    • Maupin, K.A.1    Liden, D.2    Haab, B.B.3
  • 38
    • 80052647770 scopus 로고    scopus 로고
    • Metabolism of free oligosaccharides is facilitated in the och1D mutant of Saccharomyces cerevisiae
    • Hirayama, H. & Suzuki, T. Metabolism of free oligosaccharides is facilitated in the och1D mutant of Saccharomyces cerevisiae. Glycobiology 21, 1341-1348 (2011).
    • (2011) Glycobiology , vol.21 , pp. 1341-1348
    • Hirayama, H.1    Suzuki, T.2
  • 39
    • 0027445432 scopus 로고
    • Structure of the N-linked oligosaccharides that show the complete loss of α-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae
    • Nakanishi-Shindo, Y., Nakayama, K., Tanaka, A., Toda, Y. & Jigami, Y. Structure of the N-linked oligosaccharides that show the complete loss of alpha-1,6-polymannose outer chain from och1, och1 mnn1, and och1mnn1 alg3 mutants of Saccharomyces cerevisiae. J. Biol. Chem. 268, 26338-26345 (1993). (Pubitemid 23361707)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.35 , pp. 26338-26345
    • Nakanishi-Shindo, Y.1    Nakayama, K.-I.2    Tanaka, A.3    Toda, Y.4    Jigami, Y.5
  • 40
    • 54849404679 scopus 로고    scopus 로고
    • Pichia surface display: Display of proteins on the surface of glycoengineered Pichia pastoris strains
    • Jacobs, P. P. et al. Pichia surface display: display of proteins on the surface of glycoengineered Pichia pastoris strains. Biotechnol. Lett. 30, 2173-2181 (2008).
    • (2008) Biotechnol. Lett. , vol.30 , pp. 2173-2181
    • Jacobs, P.P.1
  • 41
    • 0004265596 scopus 로고    scopus 로고
    • John Wiley & Sons, Inc. doi:10.1002/0471142727
    • Current Protocols In Molecular Biology. (John Wiley & Sons, Inc., 2001). doi:10.1002/0471142727.
    • (2001) Current Protocols in Molecular Biology
  • 42
    • 79960399934 scopus 로고    scopus 로고
    • High-quality genome sequence of Pichia pastoris CBS7435
    • Küberl, A. et al. High-quality genome sequence of Pichia pastoris CBS7435. J. Biotechnol. 154, 312-320 (2011).
    • (2011) J. Biotechnol. , vol.154 , pp. 312-320
    • Küberl, A.1
  • 43
    • 3042661951 scopus 로고    scopus 로고
    • Rapid isolation of yeast genomic DNA: Bust n9 Grab
    • Harju, S., Fedosyuk, H. & Peterson, K. R. Rapid isolation of yeast genomic DNA: Bust n9 Grab. BMC Biotechnol. 4, 8-13 (2004).
    • (2004) BMC Biotechnol. , vol.4 , pp. 8-13
    • Harju, S.1    Fedosyuk, H.2    Peterson, K.R.3
  • 45
    • 67349270900 scopus 로고    scopus 로고
    • Enzymatic assembly of DNA molecules up to several hundred kilobases
    • Gibson, D. G. et al. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods 6, 343-345 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 343-345
    • Gibson, D.G.1
  • 46
    • 77951228730 scopus 로고    scopus 로고
    • Stepwise engineering of a Pichia pastoris D-amino acid oxidase whole cell catalyst
    • Abad, S. et al. Stepwise engineering of a Pichia pastoris D-amino acid oxidase whole cell catalyst. Microb. Cell Fact. 9, 24-35 (2010).
    • (2010) Microb. Cell Fact. , vol.9 , pp. 24-35
    • Abad, S.1
  • 47
    • 5444226007 scopus 로고    scopus 로고
    • Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena
    • DOI 10.1016/j.femsyr.2004.06.016, PII S1567135604001023
    • Weis, R. et al. Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena. FEMS Yeast Res. 5, 179-89 (2004). (Pubitemid 39360920)
    • (2004) FEMS Yeast Research , vol.5 , Issue.2 , pp. 179-189
    • Weis, R.1    Luiten, R.2    Skranc, W.3    Schwab, H.4    Wubbolts, M.5    Glieder, A.6
  • 48
    • 77950671924 scopus 로고    scopus 로고
    • Real-time PCR-based determination of gene copy numbers in Pichia pastoris
    • Abad, S. et al. Real-time PCR-based determination of gene copy numbers in Pichia pastoris. Biotechnol. J. 5, 413-420 (2010).
    • (2010) Biotechnol. J. , vol.5 , pp. 413-420
    • Abad, S.1
  • 49
    • 84856269227 scopus 로고    scopus 로고
    • Isomeric analysis of oligomannosidic N-glycans and their dolichollinked precursors
    • Pabst, M. et al. Isomeric analysis of oligomannosidic N-glycans and their dolichollinked precursors. Glycobiology 22, 389-399 (2012).
    • (2012) Glycobiology , vol.22 , pp. 389-399
    • Pabst, M.1
  • 50
    • 79952048840 scopus 로고    scopus 로고
    • A combinatorial genetic library approach to target heterologous glycosylation enzymes to the endoplasmic reticulum or the Golgi apparatus of Pichia pastoris
    • Nett, J. H. et al. A combinatorial genetic library approach to target heterologous glycosylation enzymes to the endoplasmic reticulum or the Golgi apparatus of Pichia pastoris. Yeast 28, 237-252 (2011).
    • (2011) Yeast , vol.28 , pp. 237-252
    • Nett, J.H.1
  • 52
    • 61449242817 scopus 로고    scopus 로고
    • Engineering complex-type N-glycosylation in Pichia pastoris using GlycoSwitch technology
    • Jacobs, P. P., Geysens, S., Vervecken, W., Contreras, R. & Callewaert, N. Engineering complex-type N-glycosylation in Pichia pastoris using GlycoSwitch technology. Nat. Protoc. 4, 58-70 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 58-70
    • Jacobs, P.P.1    Geysens, S.2    Vervecken, W.3    Contreras, R.4    Callewaert, N.5
  • 54
    • 81855168315 scopus 로고    scopus 로고
    • Elimination of b-mannose glycan structures in Pichia pastoris
    • Hopkins, D. et al. Elimination of b-mannose glycan structures in Pichia pastoris. Glycobiology 21, 1616-1626 (2011).
    • (2011) Glycobiology , vol.21 , pp. 1616-1626
    • Hopkins, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.