SavedAdd your journal

Journals / Hacettepe Journal of Biology and Chemistry / 2026 / Volume: 46 Issue: 2

A Bacterial Machinery for Surface Displayed Enzymes

Urartu Özgür Şafak Şeker(BİLKENT UNAM - INSTITUTE OF MATERIAL SCIENCES AND ENGINEERING, RESEARCH CENTER)
Pages
—
Publication Date
2018-06-03
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

In this study a cellular machinery is proposed to be used as a controlled enzyme delivery system. 

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Biomaterial based protein delivery systems have been utilized for many applications in biomedicine.
📊
Key Findings & Data:In this regard a Escherichia coli autotransporter protein, Ag43 was engineered to display on its cell membrane.
💡
Conclusion & Impact:In this study a cellular machinery is proposed to be used as a controlled enzyme delivery system. 
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Whole cell biocatalysis · autotransporter · synthetic biology

Abstract

Biomaterial based protein delivery systems have been utilized for many applications in biomedicine. Despite their great success, there is a need to develop innovative living, decision making systems for protein delivery. In this context, here, a cellular system is proposed for protein release and delivery. Such systems can be used not for biomedical purposes but also for other biochemical applications. In this regard a Escherichia coli autotransporter protein, Ag43 was engineered to display on its cell membrane. Using this system alkaline phosphatase protein is displayed on the cell surface as a fusion of Ag43-ALP which is also carrying a specific TEV protease excision site. It was shown that the active from of the enzyme was released upon its interaction with TEV protease from the cell surface. In this study a cellular machinery is proposed to be used as a controlled enzyme delivery system. 

🔖

Cite This Article

Şeker, U. Ö. Ş. (2018). A Bacterial Machinery for Surface Displayed Enzymes. Hacettepe Journal of Biology and Chemistry, Volume: 46 Issue: 2. https://ajindex.com/articles/1270674

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (25)

  1. D.D. Boehr, R.N. D’Amico, N. Rebecca, K.F. O’Rourke, F. Kathleen, Engineered control of enzyme structural dynamics and function, Prot. Sci., 27 (2018) 825-838.
  2. C. Silva, M. Martins, S. Jing, J.J. Fu, J. Fu, A. CavacoPaulo, Practical insights on enzyme stabilization, Crit. Rev. Biotechnol., 38 (2018) 335-350.
  3. J.H. Schrittwieser, S. Velikogne, M. Hall, Artificial biocatalytic linear cascades for preparation of organic molecules, Chem. Rev., 118 (2018) 270-348. Figure 5. ALP release from the surface of the cells displaying the enzyme upon addition of the TEV protease. The increase in the enzyme activity is statistically significant (t-test, p < 0.05). U.Ö.Ş. Şeker / Hacettepe J. Biol. & Chem., 2018, 46 (2), 307-313 313
  4. F. Kazenwadel; M. Franzreb, B.E. Rapp, Synthetic enzyme supercomplexes: co-immobilization of enzyme cascades, Anal. Methods, 7 (2015) 4030- 4037.
  5. M. Jeschek, S. Panke, T.R., Artificial metalloenzymes on the verge of new-to-nature metabolism, Trends Biotech. 36 (2018) 60-72.
  6. T. Nicolay, J. Vanderleyden, S. Spaepen, Autotransporter-based cell surface display in gramnegative bacteria, Critical Reviews in Microbiology, 41 (2015) 109-123.
  7. H. Nakatani, K. Hori, Cell surface protein engineering for high-performance whole-cell catalysts, Frontiers of Chemical Science and Engineering, 1 (2017) 46-57.
  8. Decorating microbes: surface display of proteins on Escherichia coli, E. van Bloois, R.T. Winter, H. Kolmar, M.W. Fraaije, Trends in Biotechnology, 29 (2011) 79- 86.
  9. N. Dautin, H. D. Bernstein, Protein secretion in gramnegative bacteria via the autotransporter pathway. Annu. Rev. Microbiol., 61 (2007) 89–112.
  10. W. Haagmans, M. van der Woude M., Phase variation of Ag43 in Escherichia coli: Dam-dependent methylation abrogates OxyR binding and OxyRmediated repression of transcription, Mol. Microbiol., 35 (2000) 877–887.
  11. D.E. Waldron, P. Owen, C.J. Dorman, Competitive interaction of the OxyR DNA-binding protein and the Dam methylase at the antigen 43 gene regulatory region in Escherichia coli, Mol. Microbiol., 44 (2002) 509–520.
  12. A. Wallecha, V. Munster, J. Correnti, T. Chan, M. van der Woude, Dam- and OxyR-dependent phase variation of agn43: essential elements and evidence for a new role of DNA methylation, J. Bacteriol., 184 (2002) 3338–3347.
  13. G.C. Ulett, J. Valle, C. Beloin, O. Sherlock, J.M. Ghigo, M. A. Schembri1, Functional analysis of antigen 43 in uropathogenic Escherichia coli reveals a role in longterm persistence in the urinary tract, Infect. Immun., 75 (2007) 3233-3244.
  14. H. Hasman, T. Chakraborty, P. J. Klemm, Antigen43-mediated autoaggregation of Escherichia coli is blocked by fimbriation, J. Bacteriol., 181(1999) 4834- 4841.
  15. K. Kjaergaard, M.A. Schembri, H. Hasman, P.J. Klemm, Antigen 43 from Escherichia coli induces inter- and intraspecies cell aggregation and changes in colony morphology of Pseudomonas fluorescens, J. Bacteriol., 182 (2000) 4789-4796.
  16. O. Sherlock, U. Dobrindt, J.B. Jensen, R.V. Munk, P. Klemm, Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein, J. Bacteriol., 188 (2006) 1789-1807.
  17. K. Kjaergaard, H. Hasman, M.A. Schembri, P. Klemm, Antigen 43-mediated autotransporter display, a versatile bacterial cell surface presentation system, J. Bacteriol., 184 (2002) 4197-4204.
  18. F.Y. Huang, C.C. Wang; Y.H. Huang, H.G. Zhao, J.L. Guo, S.L. Zhou, H. Wang, Y.Y. Lin, G.H. Tan, Antigen 43/Fc epsilon 3 chimeric protein expressed by a novel bacterial surface expression system as an effective asthma vaccine, Immunology, 143 (2014) 230-240.
  19. I. Munoz-Gutierrez, C. Moss-Acosta, B. Trujillo-Martinez, G. Gosset, A. Martinez, Ag43-mediated display of a thermostable beta-glucosidase in Escherichia coli and its use for simultaneous saccharification and fermentation at high temperatures, Microb. Cell Fact., 13 (2014) 106-.
  20. D.G. Gibson, L. Young, R.Y. Chuang, J.C. Venter, C.A. Hutchison, H.O. Smith, Enzymatic assembly of DNA molecules up to several hundred kilobases, Nat. Methods, 6 (2009) 343-345.
  21. C.W. Lee, S.H. Jang, H. Chung, Improving the stability of cold-adapted enzymes by immobilization, Catalysts, 7 (2017) 112.
  22. Y. Liu, D.S. Kim, M. Jewett, C. Michael, Repurposing ribosomes for synthetic biology, Curr. Opin. Chem. Biol., 40 (2017) 87-94.
  23. R. Lutz, H. Bujard, Independent and tight regulation of transcriptional units in Escherichia coli via the LacR/O, the TetR/O and AraC/I-1-I-2 regulatory elements, Nucleic Acids Res., 25 (1997) 1203-1210.
  24. C. Magni, F. Sessa, J. Capraro, M. Duranti, E. Maffioli, A. Scarafoni, Structural and functional insights into the basic globulin 7S of soybean seeds by using trypsin as a molecular probe, Biochem. Biophys. Res. Commun., 496 (2018) 89-94.
  25. I. Munoz-Gutierrez, C. Moss-Acosta, B. Trujillo-Martinez, G. Gosset, A. Martinez, Ag43-mediated display of a thermostable beta-glucosidase in Escherichia coli and its use for simultaneous saccharification and fermentation at high temperatures, Microb. Cell Fact., 13 (2014) 106-.