메뉴 건너뛰기




Volumn 7, Issue 8, 2007, Pages 1307-1316

Antibody expression in protease-deficient strains of the methylotrophic yeast Ogataea minuta

Author keywords

Antibody; Ogataea minuta; PEP4; PRB1; Protease; YPS1

Indexed keywords

ANTIBODY; ASPARTIC ACID; GENE PRODUCT; PROTEINASE; UNCLASSIFIED DRUG; YAPSIN 1 PROTEIN;

EID: 35448981512     PISSN: 15671356     EISSN: 15671364     Source Type: Journal    
DOI: 10.1111/j.1567-1364.2007.00291.x     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 0027159334 scopus 로고
    • Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. Similarity to the mammalian pro-opiomelanocortin-converting enzyme
    • Azaryan AV, Wong M, Friedman TC, Cawley NX, Estivariz FE, Chen HC Loh YP (1993) Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. Similarity to the mammalian pro-opiomelanocortin-converting enzyme. J Biol Chem 268 : 11968 11975.
    • (1993) J Biol Chem , vol.268 , pp. 11968-11975
    • Azaryan, A.V.1    Wong, M.2    Friedman, T.C.3    Cawley, N.X.4    Estivariz, F.E.5    Chen, H.C.6    Loh, Y.P.7
  • 3
    • 1542367699 scopus 로고    scopus 로고
    • Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures
    • Bardor M, Loutelier-Bourhis C, Paccalet1 T et al 2003) Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures. Plant Biotechnol J 1 : 451 462.
    • (2003) Plant Biotechnol J , vol.1 , pp. 451-462
    • Bardor, M.1    Loutelier-Bourhis, C.2    Paccalet, T.3
  • 4
    • 0036320668 scopus 로고    scopus 로고
    • Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae
    • Bonangelino CJ, Chavez EM Bonifacino JS (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13 : 2486 2501.
    • (2002) Mol Biol Cell , vol.13 , pp. 2486-2501
    • Bonangelino, C.J.1    Chavez, E.M.2    Bonifacino, J.S.3
  • 5
    • 0033662863 scopus 로고    scopus 로고
    • Production of full-length human pre-elafin, an elastase specific inhibitor, from yeast requires the absence of a functional yapsin 1 (Yps1p) endoprotease
    • Bourbonnais Y, Larouche C Tremblay GM (2000) Production of full-length human pre-elafin, an elastase specific inhibitor, from yeast requires the absence of a functional yapsin 1 (Yps1p) endoprotease. Protein Expr Purif 20 : 485 491.
    • (2000) Protein Expr Purif , vol.20 , pp. 485-491
    • Bourbonnais, Y.1    Larouche, C.2    Tremblay, G.M.3
  • 6
    • 0030044053 scopus 로고    scopus 로고
    • Specificity and kinetic studies on the cleavage of various prohormone mono- and paired-basic residue sites by yeast aspartic protease 3
    • Cawley NX, Chen HC, Beinfeld MC Loh YP (1996) Specificity and kinetic studies on the cleavage of various prohormone mono- and paired-basic residue sites by yeast aspartic protease 3. J Biol Chem 271 : 4168 4176.
    • (1996) J Biol Chem , vol.271 , pp. 4168-4176
    • Cawley, N.X.1    Chen, H.C.2    Beinfeld, M.C.3    Loh, Y.P.4
  • 7
    • 0032516807 scopus 로고    scopus 로고
    • Multiple sorting pathways between the late Golgi and the vacuole in yeast
    • Conibear E Stevens TH (1998) Multiple sorting pathways between the late Golgi and the vacuole in yeast. Biochim Biophys Acta 1404 : 211 230.
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 211-230
    • Conibear, E.1    Stevens, T.H.2
  • 8
    • 0032521638 scopus 로고    scopus 로고
    • Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway
    • Copley KS, Alm SM, Schooley DA Courchesne WE (1998) Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway. Biochem J 330 : 1333 1340.
    • (1998) Biochem J , vol.330 , pp. 1333-1340
    • Copley, K.S.1    Alm, S.M.2    Schooley, D.A.3    Courchesne, W.E.4
  • 9
    • 0030962901 scopus 로고    scopus 로고
    • Novel Golgi to vacuole delivery pathway in yeast: Identification of a sorting determinant and required transport component
    • Cowles CR, Snyder WB, Burd CG Emr SD (1997) Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component. EMBO J 16 : 2769 2782.
    • (1997) EMBO J , vol.16 , pp. 2769-2782
    • Cowles, C.R.1    Snyder, W.B.2    Burd, C.G.3    Emr, S.D.4
  • 10
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino JL Cregg JM (2000) Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol Rev 24 : 45 66.
    • (2000) FEMS Microbiol Rev , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 11
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes in Pichia pastoris
    • Cregg JM, Vedvick TS Raschke WC (1993) Recent advances in the expression of foreign genes in Pichia pastoris. Biotechnology (New York) 11 : 905 910.
    • (1993) Biotechnology (New York) , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.C.3
  • 13
    • 0025899125 scopus 로고
    • Antibody quantitation in seconds using affinity perfusion chromatography
    • Fulton SP, Meys M, Varady L, Jansen R Afeyan NB (1991) Antibody quantitation in seconds using affinity perfusion chromatography. Biotechniques 11 : 226 231.
    • (1991) Biotechniques , vol.11 , pp. 226-231
    • Fulton, S.P.1    Meys, M.2    Varady, L.3    Jansen, R.4    Afeyan, N.B.5
  • 14
    • 33744499696 scopus 로고    scopus 로고
    • Engineering of Pichia pastoris for improved production of antibody fragments
    • Gasser B, Maurer M, Gach J, Kunert R Mattanovich D (2006) Engineering of Pichia pastoris for improved production of antibody fragments. Biotechnol Bioeng 94 : 353 361.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 353-361
    • Gasser, B.1    Maurer, M.2    Gach, J.3    Kunert, R.4    Mattanovich, D.5
  • 15
    • 0031610415 scopus 로고    scopus 로고
    • Generation of protease-deficient strains and their use in heterologous protein expression
    • Gleeson MA, White CE, Meininger DP Komives EA (1998) Generation of protease-deficient strains and their use in heterologous protein expression. Methods Mol Biol 103 : 81 94.
    • (1998) Methods Mol Biol , vol.103 , pp. 81-94
    • Gleeson, M.A.1    White, C.E.2    Meininger, D.P.3    Komives, E.A.4
  • 17
    • 0031898857 scopus 로고    scopus 로고
    • Production of a diverse repertoire of human antibodies in genetically engineered mice
    • Ishida I, Yoshida H Tomizuka K (1998) Production of a diverse repertoire of human antibodies in genetically engineered mice. Microbiol Immunol 42 : 143 150.
    • (1998) Microbiol Immunol , vol.42 , pp. 143-150
    • Ishida, I.1    Yoshida, H.2    Tomizuka, K.3
  • 18
    • 28844482726 scopus 로고    scopus 로고
    • Glycosylation of human IgG antibodies: Relevance to therapeutic applications
    • pp. Research Signpost, Kerala, India.
    • Jefferis R Pandalai SG (2002) Glycosylation of human IgG antibodies: relevance to therapeutic applications. Recent Research Developments in Immunology. Vol. 4, Part II, pp. 769 780. Research Signpost, Kerala, India.
    • (2002) Recent Research Developments in Immunology. Vol. 4, Part II , pp. 769-780
    • Jefferis, R.1    Pandalai, S.G.2
  • 19
    • 0142232284 scopus 로고    scopus 로고
    • The production of antibody fragments and antibody fusion proteins by yeasts and filamentous fungi
    • doi:.
    • Joosten V, Lokman C, Van Den Hondel CA Punt PJ (2003) The production of antibody fragments and antibody fusion proteins by yeasts and filamentous fungi. Microb Cell Fact 2 : 1. doi :.
    • (2003) Microb Cell Fact , vol.2 , pp. 1
    • Joosten, V.1    Lokman, C.2    Van Den Hondel, C.A.3    Punt, P.J.4
  • 20
    • 33646724042 scopus 로고    scopus 로고
    • Comparison of cell lines for stable production of fucose-negative antibodies with enhanced ADCC
    • Kanda Y, Yamane-Ohnuki N, Sakai N et al 2006) Comparison of cell lines for stable production of fucose-negative antibodies with enhanced ADCC. Biotechnol Bioeng 94 : 680 688.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 680-688
    • Kanda, Y.1    Yamane-Ohnuki, N.2    Sakai, N.3    Al, E.4
  • 21
    • 0031715175 scopus 로고    scopus 로고
    • Efficient production of intact human parathyroid hormone in a Saccharomyces cerevisiae mutant deficient in yeast aspartic protease 3 (YAP3)
    • Kang HA, Kim SJ, Choi ES, Rhee SK Chung BH (1998) Efficient production of intact human parathyroid hormone in a Saccharomyces cerevisiae mutant deficient in yeast aspartic protease 3 (YAP3). Appl Microbiol Biotechnol 50 : 187 192.
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 187-192
    • Kang, H.A.1    Kim, S.J.2    Choi, E.S.3    Rhee, S.K.4    Chung, B.H.5
  • 22
    • 0032579311 scopus 로고    scopus 로고
    • Disruption of the Saccharomyces cerevisiae YAP3 gene reduces the proteolytic degradation of secreted recombinant human albumin
    • Kerry-Williams SM, Gilbert SC, Evans LR Balance DJ (1998) Disruption of the Saccharomyces cerevisiae YAP3 gene reduces the proteolytic degradation of secreted recombinant human albumin. Yeast 14 : 161 169.
    • (1998) Yeast , vol.14 , pp. 161-169
    • Kerry-Williams, S.M.1    Gilbert, S.C.2    Evans, L.R.3    Balance, D.J.4
  • 23
    • 0036491805 scopus 로고    scopus 로고
    • Construction of protease-deficient Candida boidinii strains useful for recombinant protein production: Cloning and disruption of proteinase a gene (PEP4) and proteinase B gene (PRBI)
    • Komeda T, Sakai Y, Kato N Kondo K (2002) Construction of protease-deficient Candida boidinii strains useful for recombinant protein production: cloning and disruption of proteinase A gene (PEP4) and proteinase B gene (PRBI). Biosci Biotechnol Biochem 66 : 628 631.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 628-631
    • Komeda, T.1    Sakai, Y.2    Kato, N.3    Kondo, K.4
  • 24
    • 33750025988 scopus 로고    scopus 로고
    • Production of Man5GlcNAc2-type sugar chain by the methylotrophic yeast Ogataea minuta
    • Kuroda K, Kobayashi K, Tsumura H, Komeda T, Chiba Y Jigami Y (2006) Production of Man5GlcNAc2-type sugar chain by the methylotrophic yeast Ogataea minuta. FEMS Yeast Res 6 : 1052 1062.
    • (2006) FEMS Yeast Res , vol.6 , pp. 1052-1062
    • Kuroda, K.1    Kobayashi, K.2    Tsumura, H.3    Komeda, T.4    Chiba, Y.5    Jigami, Y.6
  • 25
    • 32344449790 scopus 로고    scopus 로고
    • Optimization of humanized IgGs in glycoengineered Pichia pastoris
    • Li H, Sethuraman N, Stadheim TA et al 2006) Optimization of humanized IgGs in glycoengineered Pichia pastoris. Nat Biotechnol 24 : 210 215.
    • (2006) Nat Biotechnol , vol.24 , pp. 210-215
    • Li, H.1    Sethuraman, N.2    Stadheim, T.A.3    Al, E.4
  • 26
    • 10644247772 scopus 로고    scopus 로고
    • Improved secretory production of glucoamylase in Pichia pastoris by combination of genetic manipulations
    • Liu SH, Chou WI, Sheu CC Chang MD (2005) Improved secretory production of glucoamylase in Pichia pastoris by combination of genetic manipulations. Biochem Biophys Res Commun 326 : 817 824.
    • (2005) Biochem Biophys Res Commun , vol.326 , pp. 817-824
    • Liu, S.H.1    Chou, W.I.2    Sheu, C.C.3    Chang, M.D.4
  • 27
    • 14744277083 scopus 로고
    • High level expression of the humanized monoclonal antibody Campath-1H in Chinese hamster ovary cells
    • Page MJ Sydenham MA (1991) High level expression of the humanized monoclonal antibody Campath-1H in Chinese hamster ovary cells. Biotechnology (NY) 9 : 64 68.
    • (1991) Biotechnology (NY) , vol.9 , pp. 64-68
    • Page, M.J.1    Sydenham, M.A.2
  • 28
    • 0026342742 scopus 로고
    • Characterization of a K26Q site-directed mutant of human parathyroid hormone expressed in yeast
    • Reppe S, Gabrielsen OS, Olstad OK et al 1991) Characterization of a K26Q site-directed mutant of human parathyroid hormone expressed in yeast. J Biol Chem 266 : 14198 14201.
    • (1991) J Biol Chem , vol.266 , pp. 14198-14201
    • Reppe, S.1    Gabrielsen, O.S.2    Olstad, O.K.3    Al, E.4
  • 29
    • 0030939508 scopus 로고    scopus 로고
    • Enhancement of protein secretion in Saccharomyces cerevisiae by overproduction of Sso protein, a late-acting component of the secretory machinery
    • Ruohonen L, Toikkanen J, Tieaho V, Outola M, Soderlund H Keranen S (1997) Enhancement of protein secretion in Saccharomyces cerevisiae by overproduction of Sso protein, a late-acting component of the secretory machinery. Yeast 13 : 337 351.
    • (1997) Yeast , vol.13 , pp. 337-351
    • Ruohonen, L.1    Toikkanen, J.2    Tieaho, V.3    Outola, M.4    Soderlund, H.5    Keranen, S.6
  • 30
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa T, Nakamura K, Yamane N et al 2003) The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J Biol Chem 278 : 3466 3473.
    • (2003) J Biol Chem , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Al, E.4
  • 31
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • Shusta EV, Raines RT, Pluckthun A Wittrup KD (1998) Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nat Biotechnol 16 : 773 777.
    • (1998) Nat Biotechnol , vol.16 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Pluckthun, A.3    Wittrup, K.D.4
  • 32
    • 0031408332 scopus 로고    scopus 로고
    • The yeast adaptor protein complex, AP-3, is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole
    • Stepp JD, Huang K Lemmon SK (1997) The yeast adaptor protein complex, AP-3, is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole. J Cell Biol 139 : 1761 1774.
    • (1997) J Cell Biol , vol.139 , pp. 1761-1774
    • Stepp, J.D.1    Huang, K.2    Lemmon, S.K.3
  • 33
    • 0034513796 scopus 로고    scopus 로고
    • Transport of proteins to the yeast vacuole: Autophagy, cytoplasm-to-vacuole targeting, and role of the vacuole in degradation
    • Teter SA Klionsky DJ (2000) Transport of proteins to the yeast vacuole: autophagy, cytoplasm-to-vacuole targeting, and role of the vacuole in degradation. Semin Cell Dev Biol 11 : 173 179.
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 173-179
    • Teter, S.A.1    Klionsky, D.J.2
  • 34
    • 0037899300 scopus 로고    scopus 로고
    • The beta subunit of the Sec61p endoplasmic reticulum translocon interacts with the exocyst complex in Saccharomyces cerevisiae
    • Toikkanen JH, Miller KJ, Soderlund H, Jantti J Keranen S (2003) The beta subunit of the Sec61p endoplasmic reticulum translocon interacts with the exocyst complex in Saccharomyces cerevisiae. J Biol Chem 278 : 20946 20953.
    • (2003) J Biol Chem , vol.278 , pp. 20946-20953
    • Toikkanen, J.H.1    Miller, K.J.2    Soderlund, H.3    Jantti, J.4    Keranen, S.5
  • 35
    • 6344238954 scopus 로고    scopus 로고
    • Kluyveromyces lactis SSO1 and SEB1 genes are functional in Saccharomyces cerevisiae and enhance production of secreted proteins when overexpressed
    • Toikkanen JH, Sundqvist L Keranen S (2004) Kluyveromyces lactis SSO1 and SEB1 genes are functional in Saccharomyces cerevisiae and enhance production of secreted proteins when overexpressed. Yeast 21 : 1045 1055.
    • (2004) Yeast , vol.21 , pp. 1045-1055
    • Toikkanen, J.H.1    Sundqvist, L.2    Keranen, S.3
  • 36
    • 0029692438 scopus 로고    scopus 로고
    • Review: Biosynthesis and function of yeast vacuolar proteases
    • Van Den Hazel HB, Kielland-Brandt MC Winther JR (1996) Review: biosynthesis and function of yeast vacuolar proteases. Yeast 12 : 1 16.
    • (1996) Yeast , vol.12 , pp. 1-16
    • Van Den Hazel, H.B.1    Kielland-Brandt, M.C.2    Winther, J.R.3
  • 37
    • 2442640723 scopus 로고    scopus 로고
    • Characterization of humanized antibodies secreted by Aspergillus niger
    • Ward M, Lin C, Victoria DC et al 2004) Characterization of humanized antibodies secreted by Aspergillus niger. Appl Environ Microbiol 70 : 2567 2576.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 2567-2576
    • Ward, M.1    Lin, C.2    Victoria, D.C.3    Al, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.