Secretory production of single-chain antibody (scFv) in Brevibacillus choshinensis using novel fusion partner

Applied Microbiology and Biotechnology

Volumn 97, Issue 19, 2013, Pages 8569-8580

  Tokunaga, Masao ^a   Mizukami, Makoto ^b   Yamasaki, Koji ^a   Tokunaga, Hiroko ^a   Onishi, Hiromasa ^b   Hanagata, Hiroshi ^b   Ishibashi, Matsujiro ^a   Miyauchi, Akira ^b   Tsumoto, Kouhei ^c   Arakawa, Tsutomu ^d  

^a KAGOSHIMA UNIVERSITY   (Japan)

^b Higeta Shoyu Co Ltd   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d ALLIANCE PROTEIN LABORATORIES   (United States)

Author keywords

Brevibacillus choshinensis; Fusion protein; Halophilic lactamase; High solubility; Net negative charge; Single chain antibody (scFv)

Indexed keywords

CLONE CELLS; CYTOLOGY; ENZYMES; ESCHERICHIA COLI; LIGHT SCATTERING; PURIFICATION;

BREVIBACILLUS CHOSHINENSIS; FUSION PROTEINS; HIGH SOLUBILITY; LACTAMASES; NEGATIVE CHARGE; SINGLE-CHAIN ANTIBODIES;

ANTIBODIES;

BETA LACTAMASE; DNA; FLUORESCEIN; HALOPHILIC BETA LACTAMASE; HYBRID PROTEIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; THROMBIN; UNCLASSIFIED DRUG;

ANTIBODY; ANTIGEN; BACTERIUM; CYTOPLASM; ENZYME ACTIVITY; GENE EXPRESSION; PROTEIN; SOLUBILITY;

ANTIBODY PRODUCTION; ARTICLE; BACTERIAL STRAIN; BACTERIUM CULTURE; BREVIBACILLUS; BREVIBACILLUS CHOSHINENSIS; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; HALOPHILIC BACTERIUM; LIGHT SCATTERING; NONHUMAN; PLASMID; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SOLUBILITY; STOICHIOMETRY;

BREVIBACILLUS; BREVIBACILLUS CHOSHINENSIS; ESCHERICHIA COLI;

BETA-LACTAMASES; BREVIBACILLUS; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR WEIGHT; RECOMBINANT FUSION PROTEINS; SINGLE-CHAIN ANTIBODIES;

EID: 84885373221     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-4695-2     Document Type: Article

References (42)

1. Andersen DC, Reilly DE (2004) Production technologies for monoclonal antibodies and their fragments. Curr Opin Biotechnol 15:456-462
2. Andersson M, Wittgren B, Wahlund KG (2003) Accuracy in multiangle light scattering measurements for molar mass and radius estimations. Model calculations and experiments. Anal Chem 75:4279-4291
3. Arakawa T, Tokunaga H, Yamaguchi R, Tokunaga M (2010) High solubility supports efficient refolding of thermally unfolded beta-lactamase. Int J Biol Macromol 47:706-709
4. Beck A, Wurch T, Bailly C, Corvaia N (2010) Strategies and challenges for the next generation of therapeutic antibodies. Nat Rev Immunol 10:345-352
5. Beckman RA, Weiner LM, Davis HM (2007) Antibody constructs in cancer therapy: protein engineering strategies to improve exposure in solid tumors. Cancer 109:170-179
6. Chon JH, Zarbis-Papastoitsis G (2011) Advances in the production and downstream processing of antibodies. N Biotechnol 28:458-463
7. DasSarma S, Berquist BR, Coker JA, DasSarma P, Muller JA (2006) Post-genomics of the model haloarchaeon Halobacterium sp. NRC-1. Saline Systems 2:3
8. Demarest SJ, Glaser SM (2008) Antibody therapeutics, antibody engineering, and the merits of protein stability. Curr Opin Drug Discov Devel 11:675-687
9. Ejima D, Yumioka R, Arakawa T, Tsumoto K (2005) Arginine as an effective additive in gel permeation chromatography. J Chromatogr A 1094:49-55
10. Elcock AH, McCammon JA (1998) Electrostatic contributions to the stability of halophilic proteins. J Mol Biol 280:731-748
11. Fujii T, Ohkuri T, Onodera R, Ueda T (2007) Stable supply of large amounts of human Fab from the inclusion bodies in E. coli. J Biochem 141:699-707
12. Fursova KK, Laman AG, Melnik BS, Semisotnov GV, Kopylov PK, Kiseleva NV, Nesmeyanov VA, Brovko FA (2009) Refolding of scFv mini-antibodies using size-exclusion chromatography via arginine solution layer. J Chromatogr B Analyt Technol Biomed Life Sci 877:2045-2051
13. Humphreys DP, Glover DJ (2001) Therapeutic antibody production technologies: molecules, applications, expression and purification. Curr Opin Drug Discov Devel 4:172-185
14. Kontermann RE (2010) Alternative antibody formats. Curr Opin Mol Ther 12:176-183
15. Kudou M, Ejima D, Sato H, Yumioka R, Arakawa T, Tsumoto K (2011) Refolding single-chain antibody (scFv) using lauroyl-L-glutamate as a solubilization detergent and arginine as a refolding additive. Protein Expr Purif 77:68-74
16. Kurucz I, Titus JA, Jost CR, Segal DM (1995) Correct disulfide pairing and efficient refolding of detergent-solubilized single-chain Fv proteins from bacterial inclusion bodies. Mol Immunol 32:1443-1452
17. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
18. Lilie H, Schwarz E, Rudolph R (1998) Advances in refolding of proteins produced in E. coli. Curr Opin Biotechnol 9:497-501
19. Mevarech M, Frolow F, Gloss LM (2000) Halophilic enzymes: proteins with a grain of salt. Biophys Chem 86:155-164
20. Midelfort KS, Hernandez HH, Lippow SM, Tidor B, Drennan CL, Wittrup KD (2004) Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody. J Mol Biol 343:685-701
21. Mizukami M, Hanagata H, Miyauchi A (2010) Brevibacillus expression system: host-vector system for efficient production of secretory proteins. Curr Pharm Biotechnol 11:251-258
22. Ottiger M, Thiel MA, Feige U, Lichtlen P, Urech DM (2009) Efficient intraocular penetration of topical anti-TNF-alpha single-chain antibody (ESBA105) to anterior and posterior segment without penetration enhancer. Invest Ophthalmol Vis Sci 50:779-786
23. Shukla AA, Thommes J (2010) Recent advances in large-scale production of monoclonal antibodies and related proteins. Trends Biotechnol 28:253-261
24. Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC (1985) Measurement of protein using bicinchoninic acid. Anal Biochem 150:76-85
25. Stockwin LH, Holmes S (2003) The role of therapeutic antibodies in drug discovery. Biochem Soc Trans 31:433-436
26. Takagi H, Kadowaki K, Udaka S (1989) Screening and characterization of protein-hyperproducing bacteria without detectable exoprotease activity. Agric Biol Chem 53:691-699
27. Tokunaga H, Ishibashi M, Arakawa T, Tokunaga M (2004) Highly efficient renaturation of beta-lactamase isolated from moderately halophilic bacteria. FEBS Lett 558:7-12
28. Tokunaga H, Arakawa T, Fukada H, Tokunaga M (2006a) Opposing effects of NaCl on reversibility and thermal stability of halophilic beta-lactamase from a moderate halophile, Chromohalobacter sp. 560. Biophys Chem 119:316-320
29. Tokunaga H, Oda Y, Yonezawa Y, Arakawa T, Tokunaga M (2006b) Contribution of halophilic nucleoside diphosphate kinase sequence to the heat stability of chimeric molecule. Protein Pept Lett 13:525-530
30. Tokunaga H, Arakawa T, Tokunaga M (2008) Engineering of halophilic enzymes: two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases. Protein Sci 17:1603-1610
31. Tokunaga H, Arakawa T, Tokunaga M (2010a) Novel soluble expression technologies derived from unique properties of halophilic proteins. Appl Microbiol Biotechnol 88:1223-1231
32. Tokunaga H, Saito S, Sakai K, Yamaguchi R, Katsuyama I, Arakawa T, Onozaki K, Tokunaga M (2010b) Halophilic beta-lactamase as a new solubility- and folding-enhancing tag protein: production of native human interleukin 1alpha and human neutrophil alpha-defensin. Appl Microbiol Biotechnol 86:649-658
33. Tsumoto K, Nakaoki Y, Ueda Y, Ogasahara K, Yutani K, Watanabe K, Kumagai I (1994) Effect of the order of antibody variable regions on the expression of the single-chain HyHEL10 Fv fragment in E. coli and the thermodynamic analysis of its antigen-binding properties. Biochem Biophys Res Commun 201:546-551
34. Tsumoto K, Shinoki K, Kondo H, Uchikawa M, Juji T, Kumagai I (1998) Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent - application to a human single-chain Fv fragment. J Immunol Methods 219:119-129
35. Tsumoto K, Ejima D, Kumagai I, Arakawa T (2003) Practical considerations in refolding proteins from inclusion bodies. Protein Expr Purif 28:1-8
36. Ventosa A, Nieto JJ, Oren A (1998) Biology of moderately halophilic aerobic bacteria. Microbiol Mol Biol Rev 62:504-544
37. Wörn A, Plückthun A (2001) Stability engineering of antibody single-chain Fv fragments. J Mol Biol 305:989-1010
38. Yamada T (2011) Therapeutic monoclonal antibodies. Keio J Med 60:37-46
39. Yamaguchi R, Tokunaga H, Ishibashi M, Arakawa T, Tokunaga M (2011) Salt-dependent thermo-reversible alpha-amylase: cloning and characterization of halophilic alpha-amylase from moderately halophilic bacterium, Kocuria varians. Appl Microbiol Biotechnol 89:673-684
40. Yamaguchi R, Inoue Y, Tokunaga H, Ishibashi M, Arakawa T, Sumitani J, Kawaguchi T, Tokunaga M (2012) Halophilic characterization of starch-binding domain from Kocuria varians alpha-amylase. Int J Biol Macromol 50:95-102
41. Yashiro K, Lowenthal JW, O'Neil TE, Ebisu S, Takagi H (2001) High-level protein production of recombinant chicken interferon-γ by Brevibacillus choshinensis. Protein Expr Purif 23:113-120
42. Yonezawa Y, Izutsu K, Tokunaga H, Maeda H, Arakawa T, Tokunaga M (2007) Dimeric structure of nucleoside diphosphate kinase from moderately halophilic bacterium: contrast to the tetrameric Pseudomonas counterpart. FEMS Microbiol Lett 268:52-58