B. Porche, K.; E. Lanclos, C.; Kwon, Y.-C. Challenging Post-Translational Modifications in the Cell-Free Protein Synthesis System. Synthetic Biology and Engineering 2023, 1, 1–7, doi:10.35534/sbe.2023.10011.
B. Porche, K.; E. Lanclos, C.; Kwon, Y.-C. Challenging Post-Translational Modifications in the Cell-Free Protein Synthesis System. Synthetic Biology and Engineering 2023, 1, 1–7, doi:10.35534/sbe.2023.10011.
B. Porche, K.; E. Lanclos, C.; Kwon, Y.-C. Challenging Post-Translational Modifications in the Cell-Free Protein Synthesis System. Synthetic Biology and Engineering 2023, 1, 1–7, doi:10.35534/sbe.2023.10011.
B. Porche, K.; E. Lanclos, C.; Kwon, Y.-C. Challenging Post-Translational Modifications in the Cell-Free Protein Synthesis System. Synthetic Biology and Engineering 2023, 1, 1–7, doi:10.35534/sbe.2023.10011.
Abstract
Post-translational modifications (PTMs) represent a cornerstone in the complexity of the proteome, significantly contributing to diversifying protein structure and function. PTMs can significantly influence protein function, stability, localization, and interactions with other molecules. Therefore, it is important when choosing a protein expression system to ensure the precise incorporation of PTMs during protein synthesis, which is paramount for producing biologically active proteins. Cell-free protein synthesis (CFPS) system has emerged as a powerful protein synthesis platform and research toolkit in synthetic biology. The open nature of the system allows the reaction environment to be tailored to any protein of interest to promote specific PTMs, thus allowing for the production of a protein with the desired modifications. This review presents various PTMs achieved in the CFPS systems, providing insights into the current challenges, successes, and future prospects.
Keywords
Cell-free protein synthesis; Post-translational modification; Biomanufacturing; Disulfide bonds; Glycosylation
Subject
Engineering, Bioengineering
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Commenter's Conflict of Interests:
I am employed by LenioBio GbmH and am commenting to correct an erroneous claim on our product ALiCE.
Comment:
Very nice write-up on what has been achieved with PTM engineering in CFPS to date.
However, please note that the ALiCE system does not derive from the tobacco plant but from the BY-2 cell line. It is this use of a cellular feedstock that helps enable the scalability of ALiCE lysate production from bioreactors of cells, rather than greenhouses filled with plants.
Best,
Dr. Charles Williams
Team Lead System Innovation
LenioBio GmbH
Commenter:
Commenter's Conflict of Interests: I am employed by LenioBio GbmH and am commenting to correct an erroneous claim on our product ALiCE.
However, please note that the ALiCE system does not derive from the tobacco plant but from the BY-2 cell line. It is this use of a cellular feedstock that helps enable the scalability of ALiCE lysate production from bioreactors of cells, rather than greenhouses filled with plants.
Best,
Dr. Charles Williams
Team Lead System Innovation
LenioBio GmbH