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Volumn 30, Issue , 2014, Pages 205-210

Escherichia coli as a glycoprotein production host: Recent developments and challenges

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; GLYCAN; GLYCOPROTEIN; OLIGOSACCHARYLTRANSFERASE; RECOMBINANT PROTEIN; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84907270784     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2014.07.006     Document Type: Review
Times cited : (21)

References (49)
  • 1
    • 84892170718 scopus 로고    scopus 로고
    • What's fueling the biotech engine-2012 to 2013
    • Aggarwal S. What's fueling the biotech engine-2012 to 2013. Nat Biotechnol 2014, 32:32-39.
    • (2014) Nat Biotechnol , vol.32 , pp. 32-39
    • Aggarwal, S.1
  • 2
    • 77955713515 scopus 로고    scopus 로고
    • N-Linked glycoengineering for human therapeutic proteins in bacteria
    • Pandhal J., Wright P.C. N-Linked glycoengineering for human therapeutic proteins in bacteria. Biotechnol Lett 2010, 32:1189-1198.
    • (2010) Biotechnol Lett , vol.32 , pp. 1189-1198
    • Pandhal, J.1    Wright, P.C.2
  • 3
    • 75149183678 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins: an effective strategy to optimize efficacy
    • Solá R.J., Griebenow K. Glycosylation of therapeutic proteins: an effective strategy to optimize efficacy. BioDrugs 2011, 24:9-21.
    • (2011) BioDrugs , vol.24 , pp. 9-21
    • Solá, R.J.1    Griebenow, K.2
  • 4
    • 43149096504 scopus 로고    scopus 로고
    • N-glycosylation as novel strategy to improve pharmacokinetic properties of bispecific single-chain diabodies
    • Stork R., Zettlitz K.A., Müller D., Rether M., Hanisch F.-G., Kontermann R.E. N-glycosylation as novel strategy to improve pharmacokinetic properties of bispecific single-chain diabodies. J Biol Chem 2008, 283:7804-7812.
    • (2008) J Biol Chem , vol.283 , pp. 7804-7812
    • Stork, R.1    Zettlitz, K.A.2    Müller, D.3    Rether, M.4    Hanisch, F.-G.5    Kontermann, R.E.6
  • 5
    • 78650656127 scopus 로고    scopus 로고
    • Fc-glycosylation influences Fcγ receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12
    • Forthal D.N., Gach J.S., Landucci G., Jez J., Strasser R., Kunert R., Steinkellner H. Fc-glycosylation influences Fcγ receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12. J Immunol 2010, 185:6876-6882.
    • (2010) J Immunol , vol.185 , pp. 6876-6882
    • Forthal, D.N.1    Gach, J.S.2    Landucci, G.3    Jez, J.4    Strasser, R.5    Kunert, R.6    Steinkellner, H.7
  • 6
    • 34247565506 scopus 로고    scopus 로고
    • Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
    • Varki A. Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins. Nature 2007, 446:1023-1029.
    • (2007) Nature , vol.446 , pp. 1023-1029
    • Varki, A.1
  • 7
    • 84856389498 scopus 로고    scopus 로고
    • CHO cells in biotechnology for production of recombinant proteins: current state and further potential
    • Kim J.Y., Kim Y-G., Lee G.M. CHO cells in biotechnology for production of recombinant proteins: current state and further potential. Appl Microbiol Biotechnol 2012, 93:917-930.
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 917-930
    • Kim, J.Y.1    Kim, Y.-G.2    Lee, G.M.3
  • 9
    • 84899972272 scopus 로고    scopus 로고
    • Development of recombinant Chinese hamster ovary cell lines for therapeutic protein production
    • Noh S.M., Sathyamurthy M., Lee G.M. Development of recombinant Chinese hamster ovary cell lines for therapeutic protein production. Curr Opin Chem Eng 2013, 2:391-397.
    • (2013) Curr Opin Chem Eng , vol.2 , pp. 391-397
    • Noh, S.M.1    Sathyamurthy, M.2    Lee, G.M.3
  • 11
    • 58049214870 scopus 로고    scopus 로고
    • Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation
    • Faridmoayer A., Fentabil M.a., Haurat M.F., Yi W., Woodward R., Wang P.G., Feldman M.F. Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation. J Biol Chem 2008, 283:34596-34604.
    • (2008) J Biol Chem , vol.283 , pp. 34596-34604
    • Faridmoayer, A.1    Fentabil, M.2    Haurat, M.F.3    Yi, W.4    Woodward, R.5    Wang, P.G.6    Feldman, M.F.7
  • 12
    • 85067738266 scopus 로고    scopus 로고
    • Exploitation of bacterial N-linked glycosylation to develop a novel recombinant glycoconjugate vaccine against Francisella tularensis
    • Cuccui J., Thomas R. Exploitation of bacterial N-linked glycosylation to develop a novel recombinant glycoconjugate vaccine against Francisella tularensis. Open Biol 2013, 3.
    • (2013) Open Biol , pp. 3
    • Cuccui, J.1    Thomas, R.2
  • 15
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: sweeter than ever
    • Nothaft H., Szymanski C.M. Protein glycosylation in bacteria: sweeter than ever. Nat Rev Microbiol 2010, 8:765-778.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 16
    • 84874871322 scopus 로고    scopus 로고
    • Bacterial protein N-glycosylation: new perspectives and applications
    • Nothaft H., Szymanski C.M. Bacterial protein N-glycosylation: new perspectives and applications. J Biol Chem 2013, 288:6912-6920.
    • (2013) J Biol Chem , vol.288 , pp. 6912-6920
    • Nothaft, H.1    Szymanski, C.M.2
  • 21
    • 30544435865 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli
    • Zhang G., Brokx S., Weiner J.H. Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli. Nat Biotechnol 2006, 24:100-104.
    • (2006) Nat Biotechnol , vol.24 , pp. 100-104
    • Zhang, G.1    Brokx, S.2    Weiner, J.H.3
  • 23
    • 15944393490 scopus 로고    scopus 로고
    • The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation
    • Nita-Lazar M., Wacker M., Schegg B., Amber S., Aebi M. The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology 2005, 15:361-367.
    • (2005) Glycobiology , vol.15 , pp. 361-367
    • Nita-Lazar, M.1    Wacker, M.2    Schegg, B.3    Amber, S.4    Aebi, M.5
  • 24
    • 79952000705 scopus 로고    scopus 로고
    • Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo
    • Schwarz F., Lizak C., Fan Y-Y., Fleurkens S., Kowarik M., Aebi M. Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo. Glycobiology 2011, 21:45-54.
    • (2011) Glycobiology , vol.21 , pp. 45-54
    • Schwarz, F.1    Lizak, C.2    Fan, Y.-Y.3    Fleurkens, S.4    Kowarik, M.5    Aebi, M.6
  • 25
    • 79956083561 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements
    • Ielmini M.V., Feldman M.F. Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements. Glycobiology 2011, 21:734-742.
    • (2011) Glycobiology , vol.21 , pp. 734-742
    • Ielmini, M.V.1    Feldman, M.F.2
  • 26
    • 84895432250 scopus 로고    scopus 로고
    • Recent advances in discovery, heterologous expression, and molecular engineering of cyclodextrin glycosyltransferase for versatile applications
    • Han R., Li J., Shin H.-D., Chen R.R., Du G., Liu L., Chen J. Recent advances in discovery, heterologous expression, and molecular engineering of cyclodextrin glycosyltransferase for versatile applications. Biotechnol Adv 2013, 10.1016/j.biotechadv.2013.12.004.
    • (2013) Biotechnol Adv
    • Han, R.1    Li, J.2    Shin, H.-D.3    Chen, R.R.4    Du, G.5    Liu, L.6    Chen, J.7
  • 27
    • 84875970481 scopus 로고    scopus 로고
    • Mechanism of bacterial oligosaccharyltransferase: in vitro quantification of sequon binding and catalysis
    • Gerber S., Lizak C., Michaud G., Bucher M., Darbre T., Aebi M., Reymond J-L., Locher K.P. Mechanism of bacterial oligosaccharyltransferase: in vitro quantification of sequon binding and catalysis. J Biol Chem 2013, 288:8849-8861.
    • (2013) J Biol Chem , vol.288 , pp. 8849-8861
    • Gerber, S.1    Lizak, C.2    Michaud, G.3    Bucher, M.4    Darbre, T.5    Aebi, M.6    Reymond, J.-L.7    Locher, K.P.8
  • 28
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak C., Gerber S., Numao S., Aebi M., Locher K.P. X-ray structure of a bacterial oligosaccharyltransferase. Nature 2011, 474:350-355.
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 29
    • 84866514981 scopus 로고    scopus 로고
    • Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB
    • Ihssen J., Kowarik M., Wiesli L., Reiss R., Wacker M., Thöny-Meyer L. Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB. BMC Biotechnol 2012, 12:67.
    • (2012) BMC Biotechnol , vol.12 , pp. 67
    • Ihssen, J.1    Kowarik, M.2    Wiesli, L.3    Reiss, R.4    Wacker, M.5    Thöny-Meyer, L.6
  • 31
    • 0033565256 scopus 로고    scopus 로고
    • Increased immunogenicity of tumor vaccines complexed with anti-gal: studies in knockout mice for αlpha1,3Galactosyltransferase
    • Latemple D.C., Abrams J.T., Zhang S.Y. Increased immunogenicity of tumor vaccines complexed with anti-gal: studies in knockout mice for αlpha1,3Galactosyltransferase. Cancer Res 1999, 59:3417-3423.
    • (1999) Cancer Res , vol.59 , pp. 3417-3423
    • Latemple, D.C.1    Abrams, J.T.2    Zhang, S.Y.3
  • 32
    • 33748155285 scopus 로고    scopus 로고
    • Bacterial glycans: key mediators of diverse host immune responses
    • Comstock L.E., Kasper D.L. Bacterial glycans: key mediators of diverse host immune responses. Cell 2006, 126:847-850.
    • (2006) Cell , vol.126 , pp. 847-850
    • Comstock, L.E.1    Kasper, D.L.2
  • 35
    • 22144450662 scopus 로고    scopus 로고
    • Highly efficient endoglycosidase-catalyzed synthesis of glycopeptides using oligosaccharide oxazolines as donor substrates
    • Li B., Zeng Y., Hauser S., Song H., Wang L-X. Highly efficient endoglycosidase-catalyzed synthesis of glycopeptides using oligosaccharide oxazolines as donor substrates. J Am Chem Soc 2005, 127:9692-9693.
    • (2005) J Am Chem Soc , vol.127 , pp. 9692-9693
    • Li, B.1    Zeng, Y.2    Hauser, S.3    Song, H.4    Wang, L.-X.5
  • 36
    • 0021759093 scopus 로고
    • Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway
    • Couto J., Huffaker T., Robbins P. Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway. J Biol Chem 1984, 259:378-382.
    • (1984) J Biol Chem , vol.259 , pp. 378-382
    • Couto, J.1    Huffaker, T.2    Robbins, P.3
  • 37
    • 33747128154 scopus 로고    scopus 로고
    • In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis
    • O'Reilly M., Zhang G., Imperiali B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 2006, 14:9593-9603.
    • (2006) Biochemistry , vol.14 , pp. 9593-9603
    • O'Reilly, M.1    Zhang, G.2    Imperiali, B.3
  • 38
    • 44649191755 scopus 로고    scopus 로고
    • Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase
    • Wang X., Weldeghiorghis T., Zhang G. Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase. Structure 2008, 16:965-975.
    • (2008) Structure , vol.16 , pp. 965-975
    • Wang, X.1    Weldeghiorghis, T.2    Zhang, G.3
  • 39
    • 68449103617 scopus 로고    scopus 로고
    • Stabilized gene duplication enables long-term selection-free heterologous pathway expression
    • Tyo K.E.J., Ajikumar P.K., Stephanopoulos G. Stabilized gene duplication enables long-term selection-free heterologous pathway expression. Nat Biotechnol 2009, 27:760-765.
    • (2009) Nat Biotechnol , vol.27 , pp. 760-765
    • Tyo, K.E.J.1    Ajikumar, P.K.2    Stephanopoulos, G.3
  • 43
    • 68949206409 scopus 로고    scopus 로고
    • Applying mass spectrometry-based proteomics to genetics, genomics and network biology
    • Gstaiger M., Aebersold R. Applying mass spectrometry-based proteomics to genetics, genomics and network biology. Nat Rev Genet 2009, 10:617-627.
    • (2009) Nat Rev Genet , vol.10 , pp. 617-627
    • Gstaiger, M.1    Aebersold, R.2
  • 44
    • 84884368148 scopus 로고    scopus 로고
    • Western blots versus selected reaction monitoring assays: time to turn the tables?
    • Aebersold R., Burlingame A.L., Bradshaw R.A. Western blots versus selected reaction monitoring assays: time to turn the tables?. Mol Cell Proteomics 2013, 12:2381-2382.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 2381-2382
    • Aebersold, R.1    Burlingame, A.L.2    Bradshaw, R.A.3
  • 45
    • 84877619420 scopus 로고    scopus 로고
    • Quantitative LC-MS-MRM analysis of site-specific glycoforms of haptoglobin in liver disease
    • Sanda M., Pompach P., Brnakova Z. Quantitative LC-MS-MRM analysis of site-specific glycoforms of haptoglobin in liver disease. Mol Cell Proteomics 2013, 12:1294-1305.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 1294-1305
    • Sanda, M.1    Pompach, P.2    Brnakova, Z.3
  • 46
    • 84864762633 scopus 로고    scopus 로고
    • Quantification of glycopeptides by multiple reaction monitoring LC-MS/MS
    • Song E., Pyreddy S., Mechref Y. Quantification of glycopeptides by multiple reaction monitoring LC-MS/MS. Rapid Commun Mass Spectrom 2013, 26:1941-1954.
    • (2013) Rapid Commun Mass Spectrom , vol.26 , pp. 1941-1954
    • Song, E.1    Pyreddy, S.2    Mechref, Y.3
  • 47
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Biotechnology 1979, 76:4350-4354.
    • (1979) Biotechnology , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 48
    • 84862808990 scopus 로고    scopus 로고
    • A lectin-coupled, multiple reaction monitoring based quantitative analysis of human plasma glycoproteins by mass spectrometry
    • Ahn Y.H., Shin P.M., Ji E.S., Kim H., Yoo J.S. A lectin-coupled, multiple reaction monitoring based quantitative analysis of human plasma glycoproteins by mass spectrometry. Anal Bioanal Chem 2012, 402:2101-2112.
    • (2012) Anal Bioanal Chem , vol.402 , pp. 2101-2112
    • Ahn, Y.H.1    Shin, P.M.2    Ji, E.S.3    Kim, H.4    Yoo, J.S.5
  • 49
    • 61849105469 scopus 로고    scopus 로고
    • Mass spectrometry based targeted protein quantification: methods and applications
    • Pan S., Aebersold R., Chen R. Mass spectrometry based targeted protein quantification: methods and applications. J Proteome Res 2009, 8:787-797.
    • (2009) J Proteome Res , vol.8 , pp. 787-797
    • Pan, S.1    Aebersold, R.2    Chen, R.3


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