The effects of phage defense on recombinant protein expression

点击翻译按钮获取中文摘要

To generate large quantities of proteins used for biotechnology applications, it is usually necessary to express the protein as a "recombinant" product in an organism distinct from the original source (e.g. producing a human protein in a bacterial cell). This is necessary because it is generally difficult to obtain adequate quantities of protein from native sources. When practical, bacterial systems are ideal because bacteria grow rapidly, bacterial growth medium is inexpensive, bacterial physiology is relatively well understood, and several strains of genetically modified bacteria have been developed that can produce high-quality, intact recombinant proteins. Despite the development of techniques for protein production in bacterial systems, it is still difficult to obtain high-yields of certain proteins for unknown reasons. This is particularly true when attempting the production of proteins from higher organisms such as humans, due to the small but significant differences in human gene structure compared to bacteria. In 2000 the sales of the 30 leading recombinant proteins exceeded $13 billion, $5.6 billion of which were produced in E. coli. Advances that make it easier to express or increase yield of recombinant proteins would be of considerable interest to a large number of important industries.