Molecular chaperone assisted expression systems: obtaining pure soluble and active recombinant proteins for structural and therapeutic purposes

Abstract

For many years recombinant protein production has been at the center of biosciences used for structural and therapeutic purposes. The production of recombinant proteins in foreign host system such as E. coli has been a biggest challenge. This has brought negative impact on the ongoing search for alternative drugs and vaccines for diseases such as schistosomiasis, African sleeping sickness and malaria. At present, no system is available to produce various recombinant proteins from different sources. Hence, the search for a universal system that can be utilized for any recombinant protein is crucial. The basic requirements for high quality protein production in a pure active and soluble form have led to the use of molecular chaperones as supplement during recombinant proteins production in E. coli. Molecular chaperones are proteins that are known to assist the newly synthesized proteins to complete their folding stages. This system has improved various proteins that are difficult to produce in E. coli host. However, some proteins have not been produced as pure, soluble or active proteins. For this reason this has led to some researchers to suggest the use of engineered host systems that do not produce endogenous molecular chaperones such as Hsp70 or Hsp40. However, these systems are not easy to work with because of their fragileness. Therefore, this work explores some progresses made as well as challenges faced in coming up with the desired system that can meet all the requirements to obtain the desired protein product.