Abstract
The baculovirus/insect cell system (BICS) is widely used in academia and industry to produce eukaryotic proteins for many applications, ranging from structure analysis to drug screening and the provision of protein biologics and therapeutics. Multi-protein complexes have emerged as vital catalysts of cellular function. In order to unlock the structure and mechanism of these essential molecular machines and decipher their function, we developed MultiBac, a BICS particularly tailored for heterologous multigene transfer and multi-protein complex production. Baculovirus is unique among common viral vectors in its capacity to accommodate very large quantities of heterologous DNA and to faithfully deliver this cargo to a host cell of choice. We exploited this beneficial feature to outfit insect cells with synthetic DNA circuitry conferring new functionality during heterologous protein expression, and developing customized MultiBac baculovirus variants in the process. By altering its tropism, recombinant baculovirions can be used for the highly efficient delivery of a customized DNA cargo in mammalian cells and tissues. Current advances in synthetic biology greatly facilitate the construction or recombinant baculoviral genomes for gene editing and genome engineering, mediated by a MultiBac baculovirus tailored to this purpose. Here, recent developments and exploits of the MultiBac system are presented and discussed.
Highlights
In 1983, Max Summers and his team reported the successful production of a heterologous protein, human IFN-β, in insect cells by using a recombinant baculovirus [1]
We validated our system and communicated the MultiBac reagents were immediately well received by the community, underscoring the existing need for heterologous and protocols we developed which were immediately well received by the community, underscoring expression systems that could enable the high quality ofthe large protein the existing need for heterologous expression systems thatproduction could enable highmulti-subunit quality production assemblies
We recently alternatives to inactivated viruses which have dominated the selection of influenza vaccinations to engineered a version of MultiBac for efficient expression of virus-like particles (VLPs) based on the influenza M1 capsid protein [78]
Summary
In 1983, Max Summers and his team reported the successful production of a heterologous protein, human IFN-β, in insect cells by using a recombinant baculovirus [1] They had modified the genome of Autographa californica multiple nuclear polyhedrosis virus (AcMNPV) and transfected insect cell cultures derived from the fall armyworm with the recombinant AcMNPV genome. By replacing the polyhedrin gene with their heterologous gene of choice, Summers and his team could exploit the machinery of the virus to drive the high-level expression of IFN-β which they could purify [2] This remarkable feat demonstrated the utility of baculovirus for heterologous protein production, and the baculovirus/insect cell system (BICS) has since been used to produce many proteins, accelerating research and development in laboratories world-wide, in academia and industry. To forestall boring the audience, we will restrict ourselves to just briefly summarizing the essentials of MultiBac, and proceed to highlight in the present review the most recent exploits and developments, by us and others, of this baculoviral system we have conceived
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