메뉴 건너뛰기




Volumn 74, Issue 2, 2008, Pages 446-453

Efficient antibody production upon suppression of O mannosylation in the yeast Ogataea minuta

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN-BINDING ACTIVITY; ENDOPLASMIC RETICULUM;

EID: 38349141228     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02106-07     Document Type: Article
Times cited : (40)

References (45)
  • 1
    • 27144457668 scopus 로고    scopus 로고
    • Upping the ante on antibodies
    • Baker, M. 2005. Upping the ante on antibodies. Nat. Biotechnol. 23:1065-1072.
    • (2005) Nat. Biotechnol , vol.23 , pp. 1065-1072
    • Baker, M.1
  • 2
    • 0022536233 scopus 로고
    • Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas
    • Bole, D. G., L. M. Hendershot, and J. F. Kearney. 1986. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J. Cell Biol. 102:1558-1566.
    • (1986) J. Cell Biol , vol.102 , pp. 1558-1566
    • Bole, D.G.1    Hendershot, L.M.2    Kearney, J.F.3
  • 3
    • 34248376466 scopus 로고    scopus 로고
    • Transcriptional and physiological adaptation to defective protein-O-mannosylation in Candida albicans
    • Cantero, P. D., C. Lengsfeld, S. K. Prill, M. Subanović, E. Román, J. Pla, and J. F. Ernst. 2007. Transcriptional and physiological adaptation to defective protein-O-mannosylation in Candida albicans. Mol. Microbiol. 64:1115-1128.
    • (2007) Mol. Microbiol , vol.64 , pp. 1115-1128
    • Cantero, P.D.1    Lengsfeld, C.2    Prill, S.K.3    Subanović, M.4    Román, E.5    Pla, J.6    Ernst, J.F.7
  • 4
    • 0035313152 scopus 로고    scopus 로고
    • Therapeutic antibody expression technology
    • Chadd, H. E., and S. M. Chamow. 2001. Therapeutic antibody expression technology. Curr. Opin. Biotechnol. 12:188-194.
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 188-194
    • Chadd, H.E.1    Chamow, S.M.2
  • 5
    • 0032500528 scopus 로고    scopus 로고
    • Production of human compatible high mannose-type (Man5GlcNAc2) sugar chains in Saccharomyces cerevisiae
    • Chiba, Y., M. Suzuki, S. Yoshida, A. Yoshida, H. Ikenaga, M. Takeuchi, Y. Jigami, and E. Ichishima. 1998. Production of human compatible high mannose-type (Man5GlcNAc2) sugar chains in Saccharomyces cerevisiae. J. Biol. Chem. 273:26298-26304.
    • (1998) J. Biol. Chem , vol.273 , pp. 26298-26304
    • Chiba, Y.1    Suzuki, M.2    Yoshida, S.3    Yoshida, A.4    Ikenaga, H.5    Takeuchi, M.6    Jigami, Y.7    Ichishima, E.8
  • 7
    • 3543069439 scopus 로고    scopus 로고
    • An optimized fermentation process for high-level production of a single-chain Fv antibody fragment in Pichia pastoris
    • Damascene, L. M., I. Pla, H. J. Chang, L. Cohen, G. Ritter, L. J. Old, and C. A. Batt. 2004. An optimized fermentation process for high-level production of a single-chain Fv antibody fragment in Pichia pastoris. Protein Expr. Purif. 37:18-26.
    • (2004) Protein Expr. Purif , vol.37 , pp. 18-26
    • Damascene, L.M.1    Pla, I.2    Chang, H.J.3    Cohen, L.4    Ritter, G.5    Old, L.J.6    Batt, C.A.7
  • 8
    • 33846841181 scopus 로고    scopus 로고
    • Cooverexpression of chaperones for enhanced secretion of a single-chain antibody fragment in Pichia pastoris
    • Damasceno, L. M., K. A. Anderson, G. Ritter, J. M. Cregg, L. J. Old, and C. A. Batt. 2007. Cooverexpression of chaperones for enhanced secretion of a single-chain antibody fragment in Pichia pastoris. Appl. Microbiol. Biotechnol. 74:381-389.
    • (2007) Appl. Microbiol. Biotechnol , vol.74 , pp. 381-389
    • Damasceno, L.M.1    Anderson, K.A.2    Ritter, G.3    Cregg, J.M.4    Old, L.J.5    Batt, C.A.6
  • 9
    • 17644422480 scopus 로고    scopus 로고
    • Cysteines in CH1 underlie retention of unassembled Ig heavy chains
    • Elkabetz, Y., Y. Argon, and S. Bar-Nun. 2005. Cysteines in CH1 underlie retention of unassembled Ig heavy chains. J. Biol. Chem. 280:14402-14412.
    • (2005) J. Biol. Chem , vol.280 , pp. 14402-14412
    • Elkabetz, Y.1    Argon, Y.2    Bar-Nun, S.3
  • 10
    • 33847613926 scopus 로고    scopus 로고
    • Process economics of industrial monoclonal antibody manufacture
    • Farid, S. S. 2007. Process economics of industrial monoclonal antibody manufacture. J. Chromatogr. B 848:8-18.
    • (2007) J. Chromatogr. B , vol.848 , pp. 8-18
    • Farid, S.S.1
  • 11
    • 0029933905 scopus 로고    scopus 로고
    • Defective threonine-linked glycosylation of human insulin-like growth factor in mutants of the yeast Saccharomyces cerevisiae
    • Finck, M., N. Bergmann, B. Janssen, and J. F. Ernst. 1996. Defective threonine-linked glycosylation of human insulin-like growth factor in mutants of the yeast Saccharomyces cerevisiae. Glycobiology 6:313-320.
    • (1996) Glycobiology , vol.6 , pp. 313-320
    • Finck, M.1    Bergmann, N.2    Janssen, B.3    Ernst, J.F.4
  • 12
    • 0037472394 scopus 로고    scopus 로고
    • Production of antibodies in plants and their use for global health
    • Fischer, R., R. M. Twyman, and S. Schillberg. 2003. Production of antibodies in plants and their use for global health. Vaccine 21:820-825.
    • (2003) Vaccine , vol.21 , pp. 820-825
    • Fischer, R.1    Twyman, R.M.2    Schillberg, S.3
  • 14
    • 33744499696 scopus 로고    scopus 로고
    • Engineering of Pichia pastoris for improved production of antibody fragments
    • Gasser, B., M. Maurer, J. Gach, R. Kunert, and D. Mattanovich. 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
    • 33846126638 scopus 로고    scopus 로고
    • Antibody production with yeasts and filamentous fungi: On the road to large scale?
    • Gasser, B., and D. Mattanovich. 2007. Antibody production with yeasts and filamentous fungi: on the road to large scale? Biotechnol. Lett. 29:201-212.
    • (2007) Biotechnol. Lett , vol.29 , pp. 201-212
    • Gasser, B.1    Mattanovich, D.2
  • 16
    • 0029954105 scopus 로고    scopus 로고
    • The PMT gene family: Protein O-glycosylation in Saccharomyces cerevisiae is vital
    • Gentzsch, M., and W. Tanner. 1996. The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital. EMBO J. 15:5752-5759.
    • (1996) EMBO J , vol.15 , pp. 5752-5759
    • Gentzsch, M.1    Tanner, W.2
  • 17
    • 0038823596 scopus 로고    scopus 로고
    • Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves
    • Girrbach, V., and S. Strahl. 2003. Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves. J. Biol. Chem. 278:12554-12562.
    • (2003) J. Biol. Chem , vol.278 , pp. 12554-12562
    • Girrbach, V.1    Strahl, S.2
  • 18
    • 34347327263 scopus 로고    scopus 로고
    • Protein O-glycosylation in fungi: Diverse structures and multiple functions
    • Goto, M. 2007. Protein O-glycosylation in fungi: diverse structures and multiple functions. Biosci. Biotechnol. Biochem. 71:1415-1427.
    • (2007) Biosci. Biotechnol. Biochem , vol.71 , pp. 1415-1427
    • Goto, M.1
  • 19
    • 0035163285 scopus 로고    scopus 로고
    • O-mannosylation protects mutant alpha-factor precursor from endoplasmic reticulum-associated degradation
    • Harty, C., S. Strahl, and K. Römisch. 2001. O-mannosylation protects mutant alpha-factor precursor from endoplasmic reticulum-associated degradation. Mol. Biol. Cell 12:1093-1101.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1093-1101
    • Harty, C.1    Strahl, S.2    Römisch, K.3
  • 21
    • 34249950624 scopus 로고    scopus 로고
    • Membrane association is a determinant for substrate recognition by PMT4 protein O-mannosyltransferases
    • Hutzler, J., M. Schmid, T. Bernard, B. Henrissat, and S. Strahl. 2007. Membrane association is a determinant for substrate recognition by PMT4 protein O-mannosyltransferases. Proc. Natl. Acad. Sci. USA 104:7827-7832.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7827-7832
    • Hutzler, J.1    Schmid, M.2    Bernard, T.3    Henrissat, B.4    Strahl, S.5
  • 22
    • 0036750868 scopus 로고    scopus 로고
    • Decreased protein expression and intermittent recoveries in BiP levels result from cellular stress during heterologous protein expression in Saccharomyces cerevisiae
    • Kauffman, K. J., E. M. Pridgen, F. J. Doyle III, P. S. Dhurjati, and A. S. Robinson. 2002. Decreased protein expression and intermittent recoveries in BiP levels result from cellular stress during heterologous protein expression in Saccharomyces cerevisiae. Biotechnol. Prog. 18:942-950.
    • (2002) Biotechnol. Prog , vol.18 , pp. 942-950
    • Kauffman, K.J.1    Pridgen, E.M.2    Doyle III, F.J.3    Dhurjati, P.S.4    Robinson, A.S.5
  • 24
    • 33750025988 scopus 로고    scopus 로고
    • Production of Man5GlcNAc2-type sugar chain by the methylotrophic yeast Ogataea minuta
    • Kuroda, K., K. Kobayashi, H. Tsumura, T. Komeda, Y. Chiba, and Y. Jigami. 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
  • 26
    • 0346993670 scopus 로고    scopus 로고
    • Aberrant processing of the WSC family and Mid2p cell surface sensors results in cell death of Saccharomyces cerevisiae O-mannosylation mutants
    • Lommel, M., M. Bagnat, and S. Strahl. 2004. Aberrant processing of the WSC family and Mid2p cell surface sensors results in cell death of Saccharomyces cerevisiae O-mannosylation mutants. Mol. Cell. Biol. 24:46-57.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 46-57
    • Lommel, M.1    Bagnat, M.2    Strahl, S.3
  • 27
    • 0347635516 scopus 로고    scopus 로고
    • Demonstration of mammalian protein O-mannosyltransferase activity: Coexpression of POMT1 and POMT2 required for enzymatic activity
    • Manya, H., A. Chiba, A. Yoshida, X. Wang, Y. Chiba, Y. Jigami, R. U. Margolis, and T. Endo. 2004. Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity. Proc. Natl. Acad. Sci. USA 101:500-505.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 500-505
    • Manya, H.1    Chiba, A.2    Yoshida, A.3    Wang, X.4    Chiba, Y.5    Jigami, Y.6    Margolis, R.U.7    Endo, T.8
  • 29
    • 9644294223 scopus 로고    scopus 로고
    • Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast
    • Nakatsukasa, K., S. Okada, K. Umebayashi, R. Fukuda, S. Nishikawa, and T. Endo. 2004. Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast. J. Biol. Chem. 279:49762-49772.
    • (2004) J. Biol. Chem , vol.279 , pp. 49762-49772
    • Nakatsukasa, K.1    Okada, S.2    Umebayashi, K.3    Fukuda, R.4    Nishikawa, S.5    Endo, T.6
  • 30
    • 0032768391 scopus 로고    scopus 로고
    • High-level secretory expression of immunologically active intact antibody from the yeast Pichia pastoris
    • Ogunjimi, A. A., J. M. Chandler, C. M. Gooding, A. Recinos III, and P. V. Choudary. 1999. High-level secretory expression of immunologically active intact antibody from the yeast Pichia pastoris. Biotechnol. Lett. 21:561-567.
    • (1999) Biotechnol. Lett , vol.21 , pp. 561-567
    • Ogunjimi, A.A.1    Chandler, J.M.2    Gooding, C.M.3    Recinos III, A.4    Choudary, P.V.5
  • 33
    • 13144261712 scopus 로고    scopus 로고
    • PMT family of Candida albicans: Five protein mannosyltransferase isoforms affect growth, morphogenesis and antifungal resistance
    • Prill, S. K., B. Klinkert, C. Timpel, C. A. Gale, K. Schröppel, and J. F. Ernst. 2005. PMT family of Candida albicans: five protein mannosyltransferase isoforms affect growth, morphogenesis and antifungal resistance. Mol. Microbiol. 55:546-560.
    • (2005) Mol. Microbiol , vol.55 , pp. 546-560
    • Prill, S.K.1    Klinkert, B.2    Timpel, C.3    Gale, C.A.4    Schröppel, K.5    Ernst, J.F.6
  • 34
    • 0028587240 scopus 로고
    • Subcellular localization of the UDP-N-acetyl-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland
    • Roth, J., Y. Wang, A. E. Eckhardt, and R. L. Hill. 1994. Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Proc. Natl. Acad. Sci. USA 91:8935-8939.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8935-8939
    • Roth, J.1    Wang, Y.2    Eckhardt, A.E.3    Hill, R.L.4
  • 35
    • 0031843028 scopus 로고    scopus 로고
    • Increased carotenoid production by the food yeast Candida utilis through metabolic engineering of the isoprenoid pathway
    • Shimada, H., K. Kondo, P. D. Fraser, Y. Miura, T. Saito, and N. Misawa. 1998. Increased carotenoid production by the food yeast Candida utilis through metabolic engineering of the isoprenoid pathway. Appl. Environ. Microbiol. 64:2676-2680.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 2676-2680
    • Shimada, H.1    Kondo, K.2    Fraser, P.D.3    Miura, Y.4    Saito, T.5    Misawa, N.6
  • 36
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • Shusta, E. V., R. T. Raines, A. Plückthun, and K. D. Wittrup. 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    Plückthun, A.3    Wittrup, K.D.4
  • 40
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers, K. J., C. K. Patil, L. Wodicka, D. T. Lockhart, J. S. Weissman, and P. Walter. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101:249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.T.4    Weissman, J.S.5    Walter, P.6
  • 42
    • 6344223348 scopus 로고    scopus 로고
    • Weber, Y., S. K. Prill, and J. F. Ernst. 2004. Pmt-mediated O mannosylation stabilizes an essential component of the secretory apparatus, Sec20p, in Candida albicans. Eukaryot. Cell 3:1164-1168.
    • Weber, Y., S. K. Prill, and J. F. Ernst. 2004. Pmt-mediated O mannosylation stabilizes an essential component of the secretory apparatus, Sec20p, in Candida albicans. Eukaryot. Cell 3:1164-1168.
  • 45
    • 27144529555 scopus 로고    scopus 로고
    • Zhu, L., M. C. van de Lavoir, J. Albanese, D. O. Beenhouwer, P. M. Cardarelli, S. Cuison, D. F. Deng, S. Deshpande, J. H. Diamond, L. Green, E. L. Halk, B. S. Heyer, R. M. Kay, A. Kerchner, P. A. Leighton, C. M. Mather, S. L. Morrison, Z. L. Nikolov, D. B. Passmore, A. Pradas-Monne, B. T. Preston, V. S. Rangan, M. Shi, M. Srinivasan, S. G. White, P. Winters-Digiacinto, S. Wong, W. Zhou, and R. J. Etches. 2005. Production of human monoclonal antibody in eggs of chimeric chickens. Nat. Biotechnol. 23:1159-1169.
    • Zhu, L., M. C. van de Lavoir, J. Albanese, D. O. Beenhouwer, P. M. Cardarelli, S. Cuison, D. F. Deng, S. Deshpande, J. H. Diamond, L. Green, E. L. Halk, B. S. Heyer, R. M. Kay, A. Kerchner, P. A. Leighton, C. M. Mather, S. L. Morrison, Z. L. Nikolov, D. B. Passmore, A. Pradas-Monne, B. T. Preston, V. S. Rangan, M. Shi, M. Srinivasan, S. G. White, P. Winters-Digiacinto, S. Wong, W. Zhou, and R. J. Etches. 2005. Production of human monoclonal antibody in eggs of chimeric chickens. Nat. Biotechnol. 23:1159-1169.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.