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Volumn 14, Issue 1, 2015, Pages

In vivo production of a novel glycoconjugate vaccine against Shigella flexneri 2a in recombinant Escherichia coli: Identification of stimulating factors for in vivo glycosylation

Author keywords

Glycoconjugate vaccine; High cell density culture; Process optimization; Recombinant E. coli; Shigella flexneri 2a

Indexed keywords

BACTERIAL ENZYME; BACTERIAL POLYSACCHARIDE; BACTERIAL PROTEIN; CARBOHYDRATE DERIVATIVE; CARRIER PROTEIN; EXOTOXIN; EXOTOXIN A PROTEIN; FACTOR A; GLYCAN DERIVATIVE; GLYCOCONJUGATE; MAGNESIUM ION; MONOSACCHARIDE; N ACETYLGLUCOSAMINE; N GLYCAN; O POLYSACCHARIDE; OLIGOSACCHARYLTRANSFERASE PGLB; RECOMBINANT GLYCOCONJUGATE VACCINE; RECOMBINANT VACCINE; SHIGELLA VACCINE; UNCLASSIFIED DRUG; RECOMBINANT PROTEIN;

EID: 84924113151     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/s12934-015-0195-7     Document Type: Article
Times cited : (46)

References (66)
  • 2
    • 19344366789 scopus 로고    scopus 로고
    • Shigellosis
    • Niyogi SK. Shigellosis. J Microbiol. 2005;43(2):133-43.
    • (2005) J Microbiol , vol.43 , Issue.2 , pp. 133-143
    • Niyogi, S.K.1
  • 3
    • 34250353445 scopus 로고    scopus 로고
    • Clinical trials of Shigella vaccines: two steps forward and one step back on a long, hard road
    • Levine MM, Kotloff KL, Barry EM, Pasetti MF, Sztein MB. Clinical trials of Shigella vaccines: two steps forward and one step back on a long, hard road. Nat Rev Microbiol. 2007;5(7):540-53.
    • (2007) Nat Rev Microbiol , vol.5 , Issue.7 , pp. 540-553
    • Levine, M.M.1    Kotloff, K.L.2    Barry, E.M.3    Pasetti, M.F.4    Sztein, M.B.5
  • 4
    • 84863780625 scopus 로고    scopus 로고
    • Two live attenuated Shigella flexneri 2a strains WRSf2G12 and WRSf2G15: a new combination of gene deletions for 2nd generation live attenuated vaccine candidates
    • Ranallo RT, Fonseka S, Boren TL, Bedford LA, Kaminski RW, Thakkar S, et al. Two live attenuated Shigella flexneri 2a strains WRSf2G12 and WRSf2G15: a new combination of gene deletions for 2nd generation live attenuated vaccine candidates. Vaccine. 2012;30(34):5159-71.
    • (2012) Vaccine , vol.30 , Issue.34 , pp. 5159-5171
    • Ranallo, R.T.1    Fonseka, S.2    Boren, T.L.3    Bedford, L.A.4    Kaminski, R.W.5    Thakkar, S.6
  • 5
    • 84887764371 scopus 로고    scopus 로고
    • Protective immunity by oral immunization with heat-killed Shigella strains in a guinea pig colitis model
    • Barman S, Koley H, Ramamurthy T, Chakrabarti MK, Shinoda S, Nair GB, et al. Protective immunity by oral immunization with heat-killed Shigella strains in a guinea pig colitis model. Microbiol Immunol. 2013;57(11):762-71.
    • (2013) Microbiol Immunol , vol.57 , Issue.11 , pp. 762-771
    • Barman, S.1    Koley, H.2    Ramamurthy, T.3    Chakrabarti, M.K.4    Shinoda, S.5    Nair, G.B.6
  • 6
    • 84891700000 scopus 로고    scopus 로고
    • Characterization of a novel fusion protein of IpaB and IpaD of Shigella and its potential as a pan-Shigella vaccine
    • Martinez-Becerra FJ, Chen X, Dickenson NE, Choudhari SP, Harrison K, Clements JD, et al. Characterization of a novel fusion protein of IpaB and IpaD of Shigella and its potential as a pan-Shigella vaccine. Infect Immun. 2013;81(12):4470-7.
    • (2013) Infect Immun , vol.81 , Issue.12 , pp. 4470-4477
    • Martinez-Becerra, F.J.1    Chen, X.2    Dickenson, N.E.3    Choudhari, S.P.4    Harrison, K.5    Clements, J.D.6
  • 7
    • 79960758250 scopus 로고    scopus 로고
    • Outer membrane protein A (OmpA) of Shigella flexneri 2a, induces protective immune response in a mouse model
    • Pore D, Mahata N, Pal A, Chakrabarti MK. Outer membrane protein A (OmpA) of Shigella flexneri 2a, induces protective immune response in a mouse model. PLoS One. 2011;6(7):e22663.
    • (2011) PLoS One , vol.6 , Issue.7 , pp. e22663
    • Pore, D.1    Mahata, N.2    Pal, A.3    Chakrabarti, M.K.4
  • 8
    • 80052307654 scopus 로고    scopus 로고
    • Safety and immunogenicity of an intranasal Shigella flexneri 2a Invaplex 50 vaccine
    • Riddle MS, Kaminski RW, Williams C, Porter C, Baqar S, Kordis A, et al. Safety and immunogenicity of an intranasal Shigella flexneri 2a Invaplex 50 vaccine. Vaccine. 2011;29(40):7009-19.
    • (2011) Vaccine , vol.29 , Issue.40 , pp. 7009-7019
    • Riddle, M.S.1    Kaminski, R.W.2    Williams, C.3    Porter, C.4    Baqar, S.5    Kordis, A.6
  • 9
    • 61449158708 scopus 로고    scopus 로고
    • A synthetic carbohydrate-protein conjugate vaccine candidate against Shigella flexneri 2a infection
    • Phalipon A, Tanguy M, Grandjean C, Guerreiro C, Belot F, Cohen D, et al. A synthetic carbohydrate-protein conjugate vaccine candidate against Shigella flexneri 2a infection. J Immunol. 2009;182(4):2241-7.
    • (2009) J Immunol , vol.182 , Issue.4 , pp. 2241-2247
    • Phalipon, A.1    Tanguy, M.2    Grandjean, C.3    Guerreiro, C.4    Belot, F.5    Cohen, D.6
  • 10
    • 0345735943 scopus 로고    scopus 로고
    • Immunology of bacterial polysaccharide antigens
    • Weintraub A. Immunology of bacterial polysaccharide antigens. Carbohydr Res. 2003;338:2539-47.
    • (2003) Carbohydr Res , vol.338 , pp. 2539-2547
    • Weintraub, A.1
  • 11
    • 77952303422 scopus 로고    scopus 로고
    • How Bacterial Carbohydrates Influence the Adaptive Immune System
    • Avci FY, Kasper DL. How Bacterial Carbohydrates Influence the Adaptive Immune System. Annu Rev Immunol. 2010;28:107-30.
    • (2010) Annu Rev Immunol. , vol.28 , pp. 107-130
    • Avci, F.Y.1    Kasper, D.L.2
  • 12
    • 10144223600 scopus 로고    scopus 로고
    • Safety and immunogenicity of investigational Shigella conjugate vaccines in Israeli volunteers
    • Cohen D, Ashkenazi S, Green M, Lerman Y, Slepon R, Robin G, et al. Safety and immunogenicity of investigational Shigella conjugate vaccines in Israeli volunteers. Infect Immun. 1996;64(10):4074-7.
    • (1996) Infect Immun , vol.64 , Issue.10 , pp. 4074-4077
    • Cohen, D.1    Ashkenazi, S.2    Green, M.3    Lerman, Y.4    Slepon, R.5    Robin, G.6
  • 13
    • 70350070727 scopus 로고    scopus 로고
    • Preparation of bacterial polysaccharide-protein conjugates: analytical and manufacturing challenges
    • Frasch CE. Preparation of bacterial polysaccharide-protein conjugates: analytical and manufacturing challenges. Vaccine. 2009;27(46):6468-70.
    • (2009) Vaccine , vol.27 , Issue.46 , pp. 6468-6470
    • Frasch, C.E.1
  • 14
    • 0011928107 scopus 로고    scopus 로고
    • N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli
    • Wacker M, Linton D, Hitchen PG, Nita-Lazar M, Haslam SM, North SJ, et al. N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli. Science. 2002;298(5599):1790-3.
    • (2002) Science , vol.298 , Issue.5599 , pp. 1790-1793
    • Wacker, M.1    Linton, D.2    Hitchen, P.G.3    Nita-Lazar, M.4    Haslam, S.M.5    North, S.J.6
  • 15
    • 33646482093 scopus 로고    scopus 로고
    • Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems
    • Wacker M, Feldman MF, Callewaert N, Kowarik M, Clarke BR, Pohl NL, et al. Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems. Proc Natl Acad Sci USA. 2006;103(18):7088-93.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.18 , pp. 7088-7093
    • Wacker, M.1    Feldman, M.F.2    Callewaert, N.3    Kowarik, M.4    Clarke, B.R.5    Pohl, N.L.6
  • 17
    • 84883140604 scopus 로고    scopus 로고
    • Exploitation of bacterial N-linked glycosylation to develop a novel recombinant glycoconjugate vaccine against Francisella tularensis
    • Cuccui J, Thomas RM, Moule MG, D'Elia RV, Laws TR, Mills DC, et al. Exploitation of bacterial N-linked glycosylation to develop a novel recombinant glycoconjugate vaccine against Francisella tularensis. Open Biol. 2013;3(5):130002.
    • (2013) Open Biol , vol.3 , Issue.5 , pp. 130002
    • Cuccui, J.1    Thomas, R.M.2    Moule, M.G.3    D'Elia, R.V.4    Laws, T.R.5    Mills, D.C.6
  • 19
    • 84856080497 scopus 로고    scopus 로고
    • Exploiting the Campylobacter jejuni protein glycosylation system for glycoengineering vaccines and diagnostic tools directed against brucellosis
    • Iwashkiw JA, Fentabil MA, Faridmoayer A, Mills DC, Peppler M, Czibener C, et al. Exploiting the Campylobacter jejuni protein glycosylation system for glycoengineering vaccines and diagnostic tools directed against brucellosis. Microb Cell Fact. 2012;11:13.
    • (2012) Microb Cell Fact , vol.11 , pp. 13
    • Iwashkiw, J.A.1    Fentabil, M.A.2    Faridmoayer, A.3    Mills, D.C.4    Peppler, M.5    Czibener, C.6
  • 20
    • 84878884180 scopus 로고    scopus 로고
    • Engineering, conjugation, and immunogenicity assessment of Escherichia coli O121 O antigen for its potential use as a typhoid vaccine component
    • Wetter M, Kowarik M, Steffen M, Carranza P, Corradin G, Wacker M. Engineering, conjugation, and immunogenicity assessment of Escherichia coli O121 O antigen for its potential use as a typhoid vaccine component. Glycoconj J. 2013;30(5):511-22.
    • (2013) Glycoconj J , vol.30 , Issue.5 , pp. 511-522
    • Wetter, M.1    Kowarik, M.2    Steffen, M.3    Carranza, P.4    Corradin, G.5    Wacker, M.6
  • 21
    • 84880799462 scopus 로고    scopus 로고
    • Inverse metabolic engineering to improve Escherichia coli as an N-glycosylation host
    • Pandhal J, Woodruff LB, Jaffe S, Desai P, Ow SY, Noirel J, et al. Inverse metabolic engineering to improve Escherichia coli as an N-glycosylation host. Biotechnol Bioeng. 2013;110(9):2482-93.
    • (2013) Biotechnol Bioeng , vol.110 , Issue.9 , pp. 2482-2493
    • Pandhal, J.1    Woodruff, L.B.2    Jaffe, S.3    Desai, P.4    Ow, S.Y.5    Noirel, J.6
  • 22
  • 23
    • 79952580842 scopus 로고    scopus 로고
    • Improving N-glycosylation efficiency in Escherichia coli using shotgun proteomics, metabolic network analysis, and selective reaction monitoring
    • Pandhal J, Ow SY, Noirel J, Wright PC. Improving N-glycosylation efficiency in Escherichia coli using shotgun proteomics, metabolic network analysis, and selective reaction monitoring. Biotechnol Bioeng. 2011;108(4):902-12.
    • (2011) Biotechnol Bioeng , vol.108 , Issue.4 , pp. 902-912
    • Pandhal, J.1    Ow, S.Y.2    Noirel, J.3    Wright, P.C.4
  • 24
    • 27844581254 scopus 로고    scopus 로고
    • Production of recombinant proteins by high cell density culture of Escherichia coli
    • Choi JH, Keum KC, Lee SY. Production of recombinant proteins by high cell density culture of Escherichia coli. Chemical Engineering Science. 2006;61(3):876-85.
    • (2006) Chemical Engineering Science , vol.61 , Issue.3 , pp. 876-885
    • Choi, J.H.1    Keum, K.C.2    Lee, S.Y.3
  • 25
    • 0029874193 scopus 로고    scopus 로고
    • High cell-density culture of Escherichia coli
    • Lee SY. High cell-density culture of Escherichia coli. Trends Biotechnol. 1996;14(3):98-105.
    • (1996) Trends Biotechnol , vol.14 , Issue.3 , pp. 98-105
    • Lee, S.Y.1
  • 26
    • 84862659885 scopus 로고    scopus 로고
    • Recent developments in bacterial protein glycan coupling technology and glycoconjugate vaccine design
    • Terra VS, Mills DC, Yates LE, Abouelhadid S, Cuccui J, Wren BW. Recent developments in bacterial protein glycan coupling technology and glycoconjugate vaccine design. J Med Microbiol. 2012;61:919-26.
    • (2012) J Med Microbiol , vol.61 , pp. 919-926
    • Terra, V.S.1    Mills, D.C.2    Yates, L.E.3    Abouelhadid, S.4    Cuccui, J.5    Wren, B.W.6
  • 27
    • 0025975993 scopus 로고
    • The lipopolysaccharide of Shigella bacteria as a virulence factor
    • Lindberg AA, Karnell A, Weintraub A. The lipopolysaccharide of Shigella bacteria as a virulence factor. Rev Infect Dis. 1991;13 Suppl 4:S279-84.
    • (1991) Rev Infect Dis , vol.13 , pp. S279-S284
    • Lindberg, A.A.1    Karnell, A.2    Weintraub, A.3
  • 30
    • 22144455041 scopus 로고    scopus 로고
    • Enhanced trehalose production improves growth of Escherichia coli under osmotic stress
    • Purvis JE, Yomano LP, Ingram LO. Enhanced trehalose production improves growth of Escherichia coli under osmotic stress. Appl Environ Microbiol. 2005;71(7):3761-9.
    • (2005) Appl Environ Microbiol , vol.71 , Issue.7 , pp. 3761-3769
    • Purvis, J.E.1    Yomano, L.P.2    Ingram, L.O.3
  • 31
    • 77955426727 scopus 로고    scopus 로고
    • Functional characterization of trehalose biosynthesis genes from E. coli: an osmolyte involved in stress tolerance
    • Joseph TC, Rajan LA, Thampuran N, James R. Functional characterization of trehalose biosynthesis genes from E. coli: an osmolyte involved in stress tolerance. Mol Biotechnol. 2010;46(1):20-5.
    • (2010) Mol Biotechnol , vol.46 , Issue.1 , pp. 20-25
    • Joseph, T.C.1    Rajan, L.A.2    Thampuran, N.3    James, R.4
  • 32
    • 0027166941 scopus 로고
    • Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression
    • Strom AR, Kaasen I. Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression. Mol Microbiol. 1993;8(2):205-10.
    • (1993) Mol Microbiol , vol.8 , Issue.2 , pp. 205-210
    • Strom, A.R.1    Kaasen, I.2
  • 33
    • 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, et al. Mechanism of bacterial oligosaccharyltransferase: in vitro quantification of sequon binding and catalysis. J Biol Chem. 2013;288(13):8849-61.
    • (2013) J Biol Chem , vol.288 , Issue.13 , pp. 8849-8861
    • Gerber, S.1    Lizak, C.2    Michaud, G.3    Bucher, M.4    Darbre, T.5    Aebi, M.6
  • 34
    • 0019570379 scopus 로고
    • N-Glycosylation of yeast proteins. Characterization of the solubilized oligosaccharyl transferase
    • Sharma CB, Lehle L, Tanner W. N-Glycosylation of yeast proteins. Characterization of the solubilized oligosaccharyl transferase. Eur J Biochem. 1981;116(1):101-8.
    • (1981) Eur J Biochem , vol.116 , Issue.1 , pp. 101-108
    • Sharma, C.B.1    Lehle, L.2    Tanner, W.3
  • 35
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak C, Gerber S, Numao S, Aebi M, Locher KP. X-ray structure of a bacterial oligosaccharyltransferase. Nature. 2011;474(7351):350-5.
    • (2011) Nature , vol.474 , Issue.7351 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 36
    • 0344242080 scopus 로고    scopus 로고
    • High-level production of human leptin by fed-batch cultivation of recombinant Escherichia coli and its purification
    • Jeong KJ, Lee SY. High-level production of human leptin by fed-batch cultivation of recombinant Escherichia coli and its purification. Appl Environ Microbiol. 1999;65(7):3027-32.
    • (1999) Appl Environ Microbiol , vol.65 , Issue.7 , pp. 3027-3032
    • Jeong, K.J.1    Lee, S.Y.2
  • 37
    • 34248232580 scopus 로고    scopus 로고
    • From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni
    • Chen MM, Glover KJ, Imperiali B. From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni. Biochemistry. 2007;46(18):5579-85.
    • (2007) Biochemistry , vol.46 , Issue.18 , pp. 5579-5585
    • Chen, M.M.1    Glover, K.J.2    Imperiali, B.3
  • 38
    • 20044393802 scopus 로고    scopus 로고
    • Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli
    • Feldman MF, Wacker M, Hernandez M, Hitchen PG, Marolda CL, Kowarik M, et al. Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli. Proc Natl Acad Sci USA. 2005;102(8):3016-21.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.8 , pp. 3016-3021
    • Feldman, M.F.1    Wacker, M.2    Hernandez, M.3    Hitchen, P.G.4    Marolda, C.L.5    Kowarik, M.6
  • 39
    • 84899056813 scopus 로고    scopus 로고
    • Prevention of Staphylococcus aureus infections by glycoprotein vaccines synthesized in Escherichia coli
    • Wacker M, Wang L, Kowarik M, Dowd M, Lipowsky G, Faridmoayer A, et al. Prevention of Staphylococcus aureus infections by glycoprotein vaccines synthesized in Escherichia coli. J Infect Dis. 2014;209(10):1551-61.
    • (2014) J Infect Dis , vol.209 , Issue.10 , pp. 1551-1561
    • Wacker, M.1    Wang, L.2    Kowarik, M.3    Dowd, M.4    Lipowsky, G.5    Faridmoayer, A.6
  • 40
    • 0017133605 scopus 로고
    • Somatic antigens of Shigella - structural investigation on o-specific polysaccharide chain of Shigella dysenteriae type-1 lipopolysaccharide
    • Dmitriev BA, Knirel YA, Kochetkov NK, Hofman IL. Somatic antigens of Shigella - structural investigation on o-specific polysaccharide chain of Shigella dysenteriae type-1 lipopolysaccharide. Eur J Biochem. 1976;66(3):559-66.
    • (1976) Eur J Biochem , vol.66 , Issue.3 , pp. 559-566
    • Dmitriev, B.A.1    Knirel, Y.A.2    Kochetkov, N.K.3    Hofman, I.L.4
  • 41
    • 0021763029 scopus 로고
    • Structural studies of the o-specific side-chain of the lipopolysaccharide from Escherichia coli o-7
    • Lvov VL, Shashkov AS, Dmitriev BA, Kochetkov NK, Jann B, Jann K. Structural studies of the o-specific side-chain of the lipopolysaccharide from Escherichia coli o-7. Carbohydr Res. 1984;126(2):249-59.
    • (1984) Carbohydr Res , vol.126 , Issue.2 , pp. 249-259
    • Lvov, V.L.1    Shashkov, A.S.2    Dmitriev, B.A.3    Kochetkov, N.K.4    Jann, B.5    Jann, K.6
  • 42
    • 84874275407 scopus 로고    scopus 로고
    • Batch production of a silk-elastin-like protein in E. coli BL21 (DE3): key parameters for optimisation
    • Collins T, Azevedo-Silva J, da Costa A, Branca F, Machado R, Casal M. Batch production of a silk-elastin-like protein in E. coli BL21 (DE3): key parameters for optimisation. Microb Cell Fact. 2013;12:21.
    • (2013) Microb Cell Fact , vol.12 , pp. 21
    • Collins, T.1    Azevedo-Silva, J.2    Costa, A.3    Branca, F.4    Machado, R.5    Casal, M.6
  • 43
    • 84868324306 scopus 로고    scopus 로고
    • IPTG limitation avoids metabolic burden and acetic acid accumulation in induced fed-batch cultures of Escherichia coli M15 under glucose limiting conditions
    • Lecina M, Sarro E, Casablancas A, Godia F, Cairo JJ. IPTG limitation avoids metabolic burden and acetic acid accumulation in induced fed-batch cultures of Escherichia coli M15 under glucose limiting conditions. Biochem Eng J. 2013;70:78-83.
    • (2013) Biochem Eng J , vol.70 , pp. 78-83
    • Lecina, M.1    Sarro, E.2    Casablancas, A.3    Godia, F.4    Cairo, J.J.5
  • 44
    • 47849109569 scopus 로고    scopus 로고
    • Induction strategies in fed-batch cultures for recombinant protein in Escherichia coli: Application to rhamnulose 1-phosphate aldolase
    • Pinsach J, de Mas C, Lopez-Santin J. Induction strategies in fed-batch cultures for recombinant protein in Escherichia coli: Application to rhamnulose 1-phosphate aldolase. Biochem Eng J. 2008;41(2):181-7.
    • (2008) Biochem Eng J , vol.41 , Issue.2 , pp. 181-187
    • Pinsach, J.1    Mas, C.2    Lopez-Santin, J.3
  • 45
    • 84875091004 scopus 로고    scopus 로고
    • Metabolic responses to recombinant bioprocesses in Escherichia coli
    • Carneiro S, Ferreira EC, Rocha I. Metabolic responses to recombinant bioprocesses in Escherichia coli. J Biotechnol. 2013;164(3):396-408.
    • (2013) J Biotechnol , vol.164 , Issue.3 , pp. 396-408
    • Carneiro, S.1    Ferreira, E.C.2    Rocha, I.3
  • 46
    • 2942755215 scopus 로고    scopus 로고
    • Stress induced by recombinant protein production in Escherichia coli
    • Hoffmann F, Rinas U. Stress induced by recombinant protein production in Escherichia coli. Adv Biochem Eng Biotechnol. 2004;89:73-92.
    • (2004) Adv Biochem Eng Biotechnol , vol.89 , pp. 73-92
    • Hoffmann, F.1    Rinas, U.2
  • 47
    • 0037677435 scopus 로고    scopus 로고
    • Metabolic load of recombinant protein production: Inhibition of cellular capacities for glucose uptake and respiration after induction of a heterologous gene in Escherichia coli
    • Neubauer P, Lin HY, Mathiszik B. Metabolic load of recombinant protein production: Inhibition of cellular capacities for glucose uptake and respiration after induction of a heterologous gene in Escherichia coli. Biotechnol Bioeng. 2003;83(1):53-64.
    • (2003) Biotechnol Bioeng , vol.83 , Issue.1 , pp. 53-64
    • Neubauer, P.1    Lin, H.Y.2    Mathiszik, B.3
  • 48
    • 0025079828 scopus 로고
    • Optimal induction of protein-synthesis in recombinant bacterial cultures
    • Bentley WE, Kompala DS. Optimal induction of protein-synthesis in recombinant bacterial cultures. Ann N Y Acad Sci. 1990;589:121-38.
    • (1990) Ann N Y Acad Sci , vol.589 , pp. 121-138
    • Bentley, W.E.1    Kompala, D.S.2
  • 49
    • 79959435716 scopus 로고    scopus 로고
    • Assembly of bacterial inner membrane proteins
    • Dalbey RE, Wang P, Kuhn A. Assembly of bacterial inner membrane proteins. Annu Rev Biochem. 2011;80:161-87.
    • (2011) Annu Rev Biochem , vol.80 , pp. 161-187
    • Dalbey, R.E.1    Wang, P.2    Kuhn, A.3
  • 51
    • 0036175254 scopus 로고    scopus 로고
    • Conserved aspartic acids are essential for the enzymic activity of the WecA protein initiating the biosynthesis of O-specific lipopolysaccharide and enterobacterial common antigen in Escherichia coli
    • Amer AO, Valvano MA. Conserved aspartic acids are essential for the enzymic activity of the WecA protein initiating the biosynthesis of O-specific lipopolysaccharide and enterobacterial common antigen in Escherichia coli. Microbiology. 2002;148(Pt 2):571-82.
    • (2002) Microbiology , vol.148 , pp. 571-582
    • Amer, A.O.1    Valvano, M.A.2
  • 52
    • 0028303288 scopus 로고
    • Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a
    • Yao Z, Valvano MA. Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a. J Bacteriol. 1994;176(13):4133-43.
    • (1994) J Bacteriol , vol.176 , Issue.13 , pp. 4133-4143
    • Yao, Z.1    Valvano, M.A.2
  • 53
    • 0023892566 scopus 로고
    • Molecular cloning and overexpression of the glucosamine synthetase gene from Escherichia coli
    • Dutka-Malen S, Mazodier P, Badet B. Molecular cloning and overexpression of the glucosamine synthetase gene from Escherichia coli. Biochimie. 1988;70(2):287-90.
    • (1988) Biochimie , vol.70 , Issue.2 , pp. 287-290
    • Dutka-Malen, S.1    Mazodier, P.2    Badet, B.3
  • 54
    • 0030032719 scopus 로고    scopus 로고
    • Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli
    • Mengin-Lecreulx D, van Heijenoort J. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. J Biol Chem. 1996;271(1):32-9.
    • (1996) J Biol Chem , vol.271 , Issue.1 , pp. 32-39
    • Mengin-Lecreulx, D.1    Heijenoort, J.2
  • 55
    • 0027938707 scopus 로고
    • Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis
    • Mengin-Lecreulx D, van Heijenoort J. Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J Bacteriol. 1994;176(18):5788-95.
    • (1994) J Bacteriol , vol.176 , Issue.18 , pp. 5788-5795
    • Mengin-Lecreulx, D.1    Heijenoort, J.2
  • 56
    • 0037013983 scopus 로고    scopus 로고
    • Glucosamine-6-phosphate synthase-the multi-facets enzyme
    • Milewski S. Glucosamine-6-phosphate synthase-the multi-facets enzyme. Biochim Biophys Acta. 2002;1597(2):173-92.
    • (2002) Biochim Biophys Acta , vol.1597 , Issue.2 , pp. 173-192
    • Milewski, S.1
  • 57
    • 0023848581 scopus 로고
    • Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase
    • Rogers MJ, Ohgi T, Plumbridge J, Soll D. Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase. Gene. 1988;62(2):197-207.
    • (1988) Gene , vol.62 , Issue.2 , pp. 197-207
    • Rogers, M.J.1    Ohgi, T.2    Plumbridge, J.3    Soll, D.4
  • 58
    • 0036233290 scopus 로고    scopus 로고
    • UDP-GlcNAc concentration is an important factor in the biosynthesis of beta1,6-branched oligosaccharides: regulation based on the kinetic properties of N-acetylglucosaminyltransferase V
    • Sasai K, Ikeda Y, Fujii T, Tsuda T, Taniguchi N. UDP-GlcNAc concentration is an important factor in the biosynthesis of beta1,6-branched oligosaccharides: regulation based on the kinetic properties of N-acetylglucosaminyltransferase V. Glycobiology. 2002;12(2):119-27.
    • (2002) Glycobiology , vol.12 , Issue.2 , pp. 119-127
    • Sasai, K.1    Ikeda, Y.2    Fujii, T.3    Tsuda, T.4    Taniguchi, N.5
  • 59
    • 55749110442 scopus 로고    scopus 로고
    • Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA
    • Al-Dabbagh B, Mengin-Lecreulx D, Bouhss A. Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA. J Bacteriol. 2008;190(21):7141-6.
    • (2008) J Bacteriol , vol.190 , Issue.21 , pp. 7141-7146
    • Al-Dabbagh, B.1    Mengin-Lecreulx, D.2    Bouhss, A.3
  • 61
    • 22144436954 scopus 로고    scopus 로고
    • Bacteriophage-encoded glucosyltransferase GtrII of Shigella flexneri: membrane topology and identification of critical residues
    • Lehane AM, Korres H, Verma NK. Bacteriophage-encoded glucosyltransferase GtrII of Shigella flexneri: membrane topology and identification of critical residues. Biochem J. 2005;389(Pt 1):137-43.
    • (2005) Biochem J , vol.389 , pp. 137-143
    • Lehane, A.M.1    Korres, H.2    Verma, N.K.3
  • 62
    • 38049051311 scopus 로고    scopus 로고
    • Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
    • Igura M, Maita N, Kamishikiryo J, Yamada M, Obita T, Maenaka K, et al. Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. EMBO J. 2008;27(1):234-43.
    • (2008) EMBO J , vol.27 , Issue.1 , pp. 234-243
    • Igura, M.1    Maita, N.2    Kamishikiryo, J.3    Yamada, M.4    Obita, T.5    Maenaka, K.6
  • 63
    • 0021100147 scopus 로고
    • Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides
    • Welply JK, Shenbagamurthi P, Lennarz WJ, Naider F. Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides. J Biol Chem. 1983;258(19):11856-63.
    • (1983) J Biol Chem , vol.258 , Issue.19 , pp. 11856-11863
    • Welply, J.K.1    Shenbagamurthi, P.2    Lennarz, W.J.3    Naider, F.4
  • 64
    • 0025826932 scopus 로고
    • High cell density cultivation of Escherichia coli at controlled specific growth rate
    • Riesenberg D, Schulz V, Knorre WA, Pohl HD, Korz D, Sanders EA, et al. High cell density cultivation of Escherichia coli at controlled specific growth rate. J Biotechnol. 1991;20(1):17-27.
    • (1991) J Biotechnol , vol.20 , Issue.1 , pp. 17-27
    • Riesenberg, D.1    Schulz, V.2    Knorre, W.A.3    Pohl, H.D.4    Korz, D.5    Sanders, E.A.6
  • 65
    • 0030600480 scopus 로고    scopus 로고
    • A set of compatible tac promoter expression vectors
    • Dykxhoorn DM, St Pierre R, Linn T. A set of compatible tac promoter expression vectors. Gene. 1996;177(1-2):133-6.
    • (1996) Gene , vol.177 , Issue.1-2 , pp. 133-136
    • Dykxhoorn, D.M.1    St Pierre, R.2    Linn, T.3
  • 66
    • 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


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