Constitutive production and efficient secretion of soluble full-length streptavidin by an Escherichia coli 'leaky mutant'

Journal of Biotechnology

Volumn 221, Issue , 2016, Pages 91-100

  Müller, Jakob Michael ^a   Wetzel, David ^a   Flaschel, Erwin ^a   Friehs, Karl ^a   Risse, Joe Max ^a  

^a BIELEFELD UNIVERSITY   (Germany)

Author keywords

Chain length of streptavidin; Escherichia coli; Fed batch cultivation; Periplasmic leaky mutant; Secretion; Temperature

Indexed keywords

BACTERIOLOGY; BINDING SITES; ESCHERICHIA COLI; GENE EXPRESSION; GENES; PHYSIOLOGY; PRODUCTIVITY; TEMPERATURE;

BACILLUS AMYLOLIQUEFACIENS; EXTRACELLULAR CONCENTRATION; FED-BATCH CULTIVATION; HETEROLOGOUS PRODUCTION; HIGH LEVEL EXPRESSION; PERIPLASMIC LEAKY MUTANT; SECRETION; STREPTAVIDIN;

PROTEINS;

BIOTIN; SIGNAL PEPTIDE; STREPTAVIDIN; TETRAMER; TRITON X 100; 5' UNTRANSLATED REGION; BACTERIAL PROTEIN; CULTURE MEDIUM;

ARTICLE; BACILLUS AMYLOLIQUEFACIENS; BACTERIAL GENE; BACTERIAL STRAIN; BGLA GENE; BINDING SITE; BIOREACTOR; ESCHERICHIA COLI; FED BATCH REACTOR; GENE EXPRESSION SYSTEM; GENETIC VARIABILITY; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN EXPRESSION; PROTEIN SECRETION; SUPERNATANT; 5' UNTRANSLATED REGION; BACILLUS; BATCH CELL CULTURE; BIOSYNTHESIS; CHEMISTRY; CULTURE MEDIUM; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; MOLECULAR CLONING; MUTATION; SECRETION (PROCESS);

5' UNTRANSLATED REGIONS; BACILLUS; BACTERIAL PROTEINS; BATCH CELL CULTURE TECHNIQUES; CLONING, MOLECULAR; CULTURE MEDIA; ESCHERICHIA COLI; MUTATION; PROMOTER REGIONS, GENETIC; STREPTAVIDIN;

EID: 84956635495     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2016.01.032     Document Type: Article

References (47)

1. Argaraña C.E., Kuntz I.D., Birken S., Axel R., Cantor C.R. Molecular cloning and nucleotide sequence of the streptavidin gene. Nucleic Acids Res. 1986, 14:1871-1882.
2. Baba T., Ara T., Hasegawa M., Takai Y., Okumura Y., Baba M., Datsenko K.A., Tomita M., Wanner B.L., Mori H. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2006, 2:1-11.
3. Baneyx F., Ayling A., Palumbo T., Thomas D., Georgiou G. Optimization of growth conditions for the production of proteolytically-sensitive proteins in the periplasmic space of Escherichia coli. Appl. Microbiol. Biotechnol. 1991, 36:14-20.
4. Baneyx F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 1999, 10:411-421.
5. Bayer E.A., Ben-Hur H., Hiller Y., Wilchek M. Postsecretory modifications of streptavidin. Biochem. J. 1989, 259:369-376.
6. Bayer E.A., Wilchek M. Application of avidin-biotin technology to affinity-based separations. J. Chromatogr. A 1990, 510:3-11.
7. Beshay U., Miksch G., Friehs K., Flaschel E. Improved β-glucanase production by a recombinant Escherichia coli strain using zinc-ion supplemented medium. Eng. Life Sci. 2007, 7:253-258.
8. Casteluber M.C.F., Damasceno L.M., da Silveira W.B., Diniz R.H.S., Passos F.J.V., Passos F.M.L. Cloning and expression of a functional core streptavidin in Pichia pastoris: strategies to increase yield. Biotechnol. Prog. 2012, 28:1419-1425.
9. Chaiet L., Wolf F.J. The properties of streptavidin, a biotin-binding protein produced by Streptomycetes. Arch. Biochem. Biophys. 1964, 106:1-5.
10. Chen X., Xu F., Peng F., Xu H., Luo W., Xu H., Xiong Y. High-yield production of streptavidin with native C-terminal in Escherichia coli. Afr. J. Biotechnol. 2014, 8250-8258.
11. Choi J.H., Lee S.Y. Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl. Microbiol. Biotechnol. 2004, 64:625-635.
12. DiRienzo J.M., Nakamura K., Inouye M. The outer membrane proteins of gram-negative bacteria: biosynthesis, assembly, and functions. Annu. Rev. Biochem. 1978, 47:481-532.
13. Gallizia A., de Lalla C., Nardone E., Santambrogio P., Brandazza A., Sidoli A., Arosio P. Production of a soluble and functional recombinant streptavidin in Escherichia coli. Protein Expr. Purif. 1998, 14:192-196.
14. Gibson D.G., Young L., Chuang R.-Y., Venter J.C., Hutchison C.A., Smith H.O. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods 2009, 6:343-345.
15. Green N.M. Avidin and streptavidin. Methods Enzymol. 1990, 184:51-67.
16. Hartnett J., Gracyalny J., Slater M.R. The single step (KRX) competent cells: efficient cloning and high protein yields. Promega Notes 2006, 94:27-30. http://www.promega.com/pnotes/94/14410_27/14410_27.pdf.
17. Jahic M., Rotticci-Mulder J., Matrinelle M., Hult M., Enfors S.-O. Modeling of growth and energy metabolism of Pichia pastoris producing a fusion protein. Bioprocess Biosyst. Eng. 2002, 24:385-393.
18. Jensen P.R., Hammer K. The Sequence of Spacers between the Consensus Sequences Modulates the Strength of Prokaryotic Promoters. Appl. Environ. Microbiol. 1998, 64:82-87.
19. Kada G., Falk H., Gruber H.J. Accurate measurement of avidin and streptavidin in crude biofluids with a new, optimized biotin-fluorescein conjugate. BBA-Gen. Subjects 1999, 1427:33-43.
20. Kada G., Kaiser K., Falk H., Gruber H.J. Rapid estimation of avidin and streptavidin by fluorescence quenching or fluorescence polarization. BBA - Gen Subjects 1999, 1427:44-48.
21. Khosla C., Bailey J.E. Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli. Implications for protein function. J. Mol. Biol. 1989, 5:79-89.
22. Kolomiets E.I., Zdor N.A. A product of the strain Streptomyces avidinii VKM Ac1047: synthesis, purification and use in immunoassay technology. Russ. Biotechnol. 1998, 2:1-8. ISSN 1068-3682.
23. Lamla T., Erdmann V.A. The Nano-tag, a streptavidin-binding peptide for the purification and detection of recombinant proteins. Protein Expr. Purif. 2004, 33:39-47.
24. Liang S.-T., Bipatnath M., Xu Y.-C., Chen S.-L., Dennis P., Ehrenberg M., Bremer H. Activities of constitutive promoters in Escherichia coli. J. Mol. Biol. 1999, 292:19-37.
25. Miksch G., Neitzel R., Fiedler E., Friehs K., Flaschel E. Extracellular production of a hybrid β-glucanase from Bacillus by Escherichia coli under different cultivation conditions in shaking cultures and bioreactors. Appl. Microbiol. Biotechnol. 1997, 47:120-126.
26. Miksch G., Bettenworth F., Friehs K., Flaschel E. The sequence upstream of the -10 consensus sequence modulates the strength and induction time of stationary-phase promoters in Escherichia coli. Appl. Microbiol. Biotechnol. 2005, 69:312-320.
27. Miksch G., Ryu S., Risse J.M., Flaschel E. Factors that influence the extracellular expression of streptavidin in Escherichia coli using a bacteriocin release protein. Appl. Microbiol. Biotechnol. 2008, 81:319-326.
28. Muzykantov V.R., Christo Christofidou-Solomidou M., Balyasnikova I., Harshaw D.W., Schultz L., Fisher A.B., Albelda S.M. Streptavidin facilitates internalization and pulmonary targeting of an anti-endothelial cell antibody (platelet-endothelial cell adhesion molecule 1): a strategy for vascular immunotargeting of drugs. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:2379-2384.
29. Müller J.M., Risse J.M., Jussen D., Flaschel E. Development of fed-batch strategies for the production of streptavidin by Streptomyces avidinii based on power input and oxygen supply studies. J. Biotechnol. 2013, 163:325-332.
30. Müller J.M., Risse J.M., Friehs K., Flaschel E. Model-based development of an assay for the rapid detection of biotin-blocked binding sites of streptavidin. Eng. Life Sci. 2015, 15:627-639.
31. Ni Y., Reye J., Chen R.R. lpp deletion as a permeabilization method. Biotechnol. Bioeng. 2007, 97:1347-1356.
32. Nogueira E.S., Schleier T., Dürrenberger M., Ballmer-Hofer K., Ward T.R., Jaussi R. High-level secretion of recombinant full-length streptavidin in Pichia pastoris and its application to enantioselective catalysis. Protein Expr. Purif. 2014, 93:54-62.
33. Rösli C., Rybak J.-N., Neri D., Elia G. Quantitative recovery of biotinylated proteins from streptavidin-based affinity chromatography resins. Methods Mol. Biol. 2008, 418:89-100.
34. Pähler A., Hendrickson W.A., Kolks M.A., Argaraña C.E., Cantor C.R. Characterization and crystallization of core streptavidin. J. Biol. Chem. 1987, 262:13933-13937.
35. Pugsley A.P. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 1993, 57:50-108.
36. Sambrook J. Molecular Cloning: A Laboratory Manual 1989, Cold Spring Harbor Laboratory Press, New York.
37. Sano T., Cantor C.R. Expression of a cloned streptavidin gene in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 1990, 87:142-146.
38. Sano T., Pandori M.W., Chen X., Smith C.L., Cantor C.R. Recombinant core streptavidins. J. Biol. Chem. 1995, 270:28204-28209.
39. Selvamani R.S.V., Telaar M., Friehs K., Flaschel E. Antibiotic-free segregational plasmid stabilization in Escherichia coli owing to the knockout of triosephosphate isomerase (tpiA). Microb. Cell Fact. 2014, 13:58.
40. Shin H.D., Chen R.R. Extracellular protein production from an Escherichia coli lpp deletion mutant. Biotechnol. Bioeng. 2008, 101:1288-1296.
41. Skerra A., Schmidt T.G.M. Applications of a peptide ligand for streptavidin: the strep-tag. Biomol. Eng. 1999, 16:79-86.
42. Wang W.W.-S., Das D., Suresh M.R. Biotin carboxyl carrier protein co-purifies as a contaminant in core-streptavid in preparations. Mol. Biotechnol. 2005, 31:29-40..
43. Wu S.-C., Wong S.-L. Engineering of a Bacillus subtilis strain with adjustable levels of intracellular biotin for secretory production of functional streptavidin. Appl. Environ. Micobiol. 2002, 68:1102-1108.
44. Wu S.-C., Qureshi M.H., Wong S.-L. Secretory production and purification of functional full-length streptavidin from Bacillus subtilis. Protein Expr. Purif. 2002, 24:348-356.
45. Wu S.-C., Wong S.-L. Intracellular production of a soluble and functional monomeric streptavidin in Escherichia coli and its application for affinity purification of biotinylated proteins. Protein Expr. Purif. 2006, 46:268-273.
46. Yang J., Moyana T., MacKenzie S., Xia Q., Xiang J. One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-alpha) from Escherichia coli caused by the synergistic effects of glycine and triton X-100. Appl. Environ. Microbiol. 1998, 64:2869-2874.
47. Zwart S.R., Lewis B.J. Optimization of detection and quantification of proteins on membranes in very high and very low abundance using avidin and streptavidin. Methods Mol. Biol. 2008, 418:25-34.