Production of therapeutic proteins with baculovirus expression system in insect cell

Abstract

Recombinant DNA technology has a major advantage in that it is capable of producing specific therapeutic proteins on demand in a heterologous expression system. The extent of this notion can be understood when one considers how crucial such proteins are, and how problematic the economical and safe production of such proteins are. Therapeutic recombinant protein production is a fundamental aspect of 21st century biotechnology industries. The improved therapeutic recombinant protein expression systems that use prokaryotic and eukaryotic cells have enabled the development of a multi-billion dollar industry. Among the variety of available heterologous expression systems, the baculovirus-based insect cell expression system has been utilized frequently for the high-level production of therapeutic recombinant proteins. Thus, the baculovirus expression system has been recognized as one of the most powerful expression technologies for production, by virtue of the achievable amount and purity, and the ease of the eukaryotic production process. The majority of therapeutic proteins are glycoproteins originating from humans. The insect-based expression system harbors glycosylation processing pathways, which constitute an advantage over other prokaryotic systems that lack glycosylation. However, there are several drawbacks which must be circumvented in order to establish an efficient system for the production of recombinant proteins. This review presents a brief overview of the perspective, particularly the glycosylation aspect, of the production of therapeutic recombinant proteins via a baculovirus-based insect cell expression system.