Engineering of therapeutic proteins production in Escherichia coli.
Low cost and simplicity of cultivating bacteria make the E. coli expression system a preferable choice for production of therapeutic proteins both on a lab scale and in industry. In addition straightforward recombinant DNA technology offers engineering tools to produce protein molecules with modified features. The lack of posttranslational modification mechanisms in bacterial cells such as glycosylation, proteolytic protein maturation or limited capacity for formation of disulfide bridges may, to a certain extent, be overcome with protein engineering. Protein engineering is also often employed to improve protein stability or to modulate its biological action. More sophisticated modifications may be achieved by genetic fusions of two proteins. This article presents a variety of examples of genetic engineering of therapeutic proteins. It emphasizes the importance of designing a construct without any unnecessary amino acid residues.
School of Pharmacy and Pharmaceutical Sciences, Trinity College, University of Dublin, Dublin 2, Ireland. kamionkm@tcd.ie.
Mariusz
M
Kamionka
D004274:DNA, Recombinant / Q000378:metabolism; D015195:Drug Design; D004926:Escherichia coli / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D006031:Glycosylation; D015202:Protein Engineering; D011499:Protein Processing, Post-Translational; D055550:Protein Stability; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000627:therapeutic use
D004274:DNA, Recombinant; D011994:Recombinant Proteins