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Introduction

Infectious diseases directly account for nearly 25% of deaths worldwide, and are predominant causes of morbidity and mortality in the developing world (Franci et al, 2005). Many developing world diseases do not yet have vaccine; both cost and ease of administration are challenges that must be tackled to address this undue burden.

The idea of targeted therapy, whereby drug or protein molecules are delivered to speciļ¬c cells, is a compelling approach to treating disease. 

Human proteins produced through genetic engineering rather than isolated from tissue samples have become an important category within therapeutic medicines.

From a clinical perspective, therapeutic proteins provide essential therapies in various life threatening disease including diabetes (insulin), end-stage renal disease (erythropoietin),viral hepatitis [interferon (IFN)], cancer-treatment related neutropenia (G-CSF), clotting disorders (Factor VII, VIII, IX), and inborn errors of metabolism (lysosomal enzymes).

Since the approval of insulin in 1982, more than 120 recombinant drug substances have been approved and become available as extremely valuable therapeutic options. 

For a long period of time, basically all recombinant proteins that were approved as drugs were produced in just four cell systems: E. coli, S. cerevisiae,CHO and BHK cells.

None of these expression systems has general advantages in all situations and for all applications, and the choice for an expression system has to be made on a case-by-case basis, sometimes with rather unexpected outcomes. 

From one safety point of view, it would theoretically be best to choose an expression platform that is phylogenetically most distant from humans since human pathogens cannot contaminate such systems.