About this Research Topic
Escherichia coli is the pioneering host for recombinant protein production. Its relatively easy genetic manipulation, rapid growth in inexpensive culture media, and high protein titers are the main advantages of using E.coli as a heterologous expression system. However, some features of E.coli, such as the absence of post translational modifications (such as glycosylation which causes folding problems leading to biologically inactive proteins), presence of lipopolysaccharide (LPS) (an endotoxin that must be removed from biopharmaceutical products), and plasmid instability (which can cause reduction of protein yield), has resulted in its lower use in industrial biopharmaceutical production relative to other hosts. Moreover, fusion tags that increase solubility and facilitate purification also have drawbacks for recombinant human proteins and should be remove without leaving additional amino acid residues to avoid undesirable immune responses and rapid in vivo elimination.
The present Research Topic aims to highlight new tools and techniques that have been developed to overcome the limitations of E.coli for successful industrial recombinant protein production, and how these tools and techniques can contribute to reducing the cost of biopharmaceutical products. The Research Topic aims to cover the proposed solutions to solving plasmid instability, bioprospecting of new vectors without antibiotic resistance genes, techniques used to improve protein folding and solubility, new E.coli hosts to deal with LPS content and/or toxicity, new protein purification process to remove LPS, novel refolding methods, integration of production and purification processes, and new fusion tags and novel tools for tag removal. The collection will also cover technical-economic analyses of recombinant protein production in E.coli.
This Research Topic welcomes submissions related (but not limited) to the following areas:
• Novel Escherichia coli host strains
• New vectors for heterologous gene expression
• Fusion tags and tag removal procedures
• LPS removal methods
• Advances in production and purification methods
The present Research Topic aims to highlight new tools and techniques that have been developed to overcome the limitations of E.coli for successful industrial recombinant protein production, and how these tools and techniques can contribute to reducing the cost of biopharmaceutical products. The Research Topic aims to cover the proposed solutions to solving plasmid instability, bioprospecting of new vectors without antibiotic resistance genes, techniques used to improve protein folding and solubility, new E.coli hosts to deal with LPS content and/or toxicity, new protein purification process to remove LPS, novel refolding methods, integration of production and purification processes, and new fusion tags and novel tools for tag removal. The collection will also cover technical-economic analyses of recombinant protein production in E.coli.
This Research Topic welcomes submissions related (but not limited) to the following areas:
• Novel Escherichia coli host strains
• New vectors for heterologous gene expression
• Fusion tags and tag removal procedures
• LPS removal methods
• Advances in production and purification methods
Keywords: Escherichia coli, recombinant protein, production process, purification process, biopharmaceutical proteins
Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.
