Engineering toward a bacterial “endoplasmic reticulum” for the rapid expression of immunoglobulin proteins

References

• van Anken E, Romijn EP, Maggioni C, Mezghrani A, Sitia R, Braakman I, Heck AJR. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity 2003; 18:243 - 53; http://dx.doi.org/10.1016/S1074-7613(03)00024-4; PMID: 12594951
   PubMed Web of Science ®Google Scholar
• Feige MJ, Hendershot LM, Buchner J. How antibodies fold. Trends Biochem Sci 2010; 35:189 - 98; http://dx.doi.org/10.1016/j.tibs.2009.11.005; PMID: 20022755
   PubMed Web of Science ®Google Scholar
• Sevier CS, Kaiser CA. Formation and transfer of disulphide bonds in living cells. Nat Rev Mol Cell Biol 2002; 3:836 - 47; http://dx.doi.org/10.1038/nrm954; PMID: 12415301
   PubMed Web of Science ®Google Scholar
• Feige MJ, Groscurth S, Marcinowski M, Shimizu Y, Kessler H, Hendershot LM, Buchner J. An unfolded CH1 domain controls the assembly and secretion of IgG antibodies. Mol Cell 2009; 34:569 - 79; http://dx.doi.org/10.1016/j.molcel.2009.04.028; PMID: 19524537
   PubMed Web of Science ®Google Scholar
• Mayer M, Kies U, Kammermeier R, Buchner J. BiP and PDI cooperate in the oxidative folding of antibodies in vitro. J Biol Chem 2000; 275:29421 - 5; http://dx.doi.org/10.1074/jbc.M002655200; PMID: 10893409
   PubMed Web of Science ®Google Scholar
• Wiest DL, Burkhardt JK, Hester S, Hortsch M, Meyer DI, Argon Y. Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately. J Cell Biol 1990; 110:1501 - 11; http://dx.doi.org/10.1083/jcb.110.5.1501; PMID: 2335560
   PubMed Web of Science ®Google Scholar
• Yin G, Garces ED, Yang J, Zhang J, Tran C, Steiner AR, Roos C, Bajad S, Hudak S, Penta K, et al. Aglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system. MAbs 2012; 4:4; http://dx.doi.org/10.4161/mabs.4.2.19202; PMID: 22377750
   PubMed Web of Science ®Google Scholar
• Zawada JF, Yin G, Steiner AR, Yang J, Naresh A, Roy SM, Gold DS, Heinsohn HG, Murray CJ. Microscale to manufacturing scale-up of cell-free cytokine production--a new approach for shortening protein production development timelines. Biotechnol Bioeng 2011; 108:1570 - 8; http://dx.doi.org/10.1002/bit.23103; PMID: 21337337
   PubMed Web of Science ®Google Scholar
• Research) C (bcc. BCC Research: Global market for therapeutic monoclonal antibodies to grow to $58 billion in 2016 [Internet]. BCC Res.2012 [cited 2013 Nov 1]; Available from: http://bccresearch.blogspot.com/2012/03/global-market-for-therapeutic.html
   Google Scholar
• Frey S, Haslbeck M, Hainzl O, Buchner J. Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system. Biol Chem 2008; 389:37 - 45; http://dx.doi.org/10.1515/BC.2008.007; PMID: 18095868
   PubMed Web of Science ®Google Scholar
• Makino T, Skretas G, Kang T-H, Georgiou G. Comprehensive engineering of Escherichia coli for enhanced expression of IgG antibodies. Metab Eng 2011; 13:241 - 51; http://dx.doi.org/10.1016/j.ymben.2010.11.002; PMID: 21130896
   PubMed Web of Science ®Google Scholar
• Sitaraman K, Esposito D, Klarmann G, Le Grice SF, Hartley JL, Chatterjee DK. A novel cell-free protein synthesis system. J Biotechnol 2004; 110:257 - 63; http://dx.doi.org/10.1016/j.jbiotec.2004.02.014; PMID: 15163516
   PubMed Web of Science ®Google Scholar
• Levy R, Weiss R, Chen G, Iverson BL, Georgiou G. Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones. Protein Expr Purif 2001; 23:338 - 47; http://dx.doi.org/10.1006/prep.2001.1520; PMID: 11676610
   PubMed Web of Science ®Google Scholar
• Bothmann H, Pluckthun A. The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines. J Biol Chem 2000; 275:17100 - 5; http://dx.doi.org/10.1074/jbc.M910233199; PMID: 10748200
   PubMed Web of Science ®Google Scholar
• Yin G, Swartz JR. Enhancing multiple disulfide bonded protein folding in a cell-free system. Biotechnol Bioeng 2004; 86:188 - 95; http://dx.doi.org/10.1002/bit.10827; PMID: 15052638
   PubMed Web of Science ®Google Scholar
• Shimizu Y, Hendershot LM. Organization of the functions and components of the endoplasmic reticulum. Adv Exp Med Biol 2007; 594:37 - 46; http://dx.doi.org/10.1007/978-0-387-39975-1_4; PMID: 17205673
   PubMed Web of Science ®Google Scholar
• Blum P, Ory J, Bauernfeind J, Krska J. Physiological consequences of DnaK and DnaJ overproduction in Escherichia coli. J Bacteriol 1992; 174:7436 - 44; PMID: 1429465
   PubMed Web of Science ®Google Scholar
• Zimmerman SB, Trach SO. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J Mol Biol 1991; 222:599 - 620; http://dx.doi.org/10.1016/0022-2836(91)90499-V; PMID: 1748995
   PubMed Web of Science ®Google Scholar
• Jakob RP, Zoldák G, Aumüller T, Schmid FX. Chaperone domains convert prolyl isomerases into generic catalysts of protein folding. Proc Natl Acad Sci U S A 2009; 106:20282 - 7; http://dx.doi.org/10.1073/pnas.0909544106; PMID: 19920179
   PubMed Web of Science ®Google Scholar
• Ow DS-W, Lim DY-X, Nissom PM, Camattari A, Wong VV-T. Co-expression of Skp and FkpA chaperones improves cell viability and alters the global expression of stress response genes during scFvD1.3 production. Microb Cell Fact 2010; 9:22; http://dx.doi.org/10.1186/1475-2859-9-22; PMID: 20388215
   PubMed Web of Science ®Google Scholar
• Ramm K, Plückthun A. High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA. J Mol Biol 2001; 310:485 - 98; http://dx.doi.org/10.1006/jmbi.2001.4747; PMID: 11428902
   PubMed Web of Science ®Google Scholar
• Levy R, Ahluwalia K, Bohmann DJ, Giang HM, Schwimmer LJ, Issafras H, Reddy NB, Chan C, Horwitz AH, Takeuchi T. Enhancement of antibody fragment secretion into the Escherichia coli periplasm by co-expression with the peptidyl prolyl isomerase, FkpA, in the cytoplasm. J Immunol Methods 2013; 394:10 - 21; http://dx.doi.org/10.1016/j.jim.2013.04.010; PMID: 23624043
   PubMed Web of Science ®Google Scholar
• Nagradova NK. Foldases: Enzymes Catalyzing Protein Folding. Nova Publishers; 2008.
   Google Scholar
• Thouvenot B, Charpentier B, Branlant C. The strong efficiency of the Escherichia coli gapA P1 promoter depends on a complex combination of functional determinants. Biochem J 2004; 383:371 - 82; http://dx.doi.org/10.1042/BJ20040792; PMID: 15250823
   PubMed Web of Science ®Google Scholar