Abstract
The use of baculoviruses has become a standard approach in many labs for recombinant protein production. In addition to giving a broad and practical overview of the technology, this chapter focuses in particular on two recent developments in the field and how these can be efficiently exploited for protein production: the use of baculovirus-infected insect cells and in vivo recombination-mediated production of recombinant viruses.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Erdmann D, Zimmermann C, Fontana P et al (2010) Simultaneous protein expression and modification: an efficient approach for production of unphosphorylated and biotinylated receptor tyrosine kinases by triple infection in the baculovirus expression system. J Biomol Tech 21:9–17
Trowitzsch S, Bieniossek C, Nie Y et al (2010) New baculovirus expression tools for recombinant protein complex production. J Struct Biol 172:45–54
Trometer C, Falson P (2010) Mammalian membrane protein expression in baculovirus-infected insect cells. Methods Mol Biol 601: 105–117
Mena JA, Kamen AA (2011) Insect cell technology is a versatile and robust vaccine manufacturing platform. [Review]. Expert Rev Vaccines 10:1063–1081
Jarvis DL, Garcia A Jr (1994) Long-term stability of baculoviruses stored under various conditions. Biotechniques 16:508–513
Pijlman GP, van Schijndel JE, Vlak JM (2003) Spontaneous excision of BAC vector sequences from bacmid-derived baculovirus expression vectors upon passage in insect cells. J Gen Virol 84:2669–2678
Cohen JI, Krogmann T, Ross JP et al (2005) Varicella-zoster virus ORF4 latency-associated protein is important for establishment of latency. J Virol 79:6969–6975
Geisse S (2007) Insect cell cultivation and generation of recombinant baculovirus particles for recombinant protein production. In: Pörtner R (ed) Animal cell biotechnology: methods and protocols. Springer, Totowa, pp 489–507
Wickham TJ, Nemerow GR (1993) Optimization of growth methods and recombinant protein production in BTI-Tn-5B1-4 insect cells using the baculovirus expression system. Biotechnol Prog 9:25–30
Jorio H, Tran R, Kamen A (2006) Stability of serum-free and purified baculovirus stocks under various storage conditions. Biotechnol Prog 22:319–325
Wasilko DJ, Lee SE (2006) Titerless infected-cells preservation and scale-up. BioProcess J 5:29–32
Wasilko DJ, Lee SE, Stutzman-Engwall KJ et al (2009) The titerless infected-cells preservation and scale-up (TIPS) method for large-scale production of NO-sensitive human soluble guanylate cyclase (sGC) from insect cells infected with recombinant baculovirus. Protein Expr Purif 65:122–132
van Oers MM (2011) Opportunities and challenges for the baculovirus expression system. J Invertebr Pathol 107 Suppl:S3–S15
Hitchman RB, Locanto E, Possee RD et al (2011) Optimizing the baculovirus expression vector system. Methods 55:52–57
Possee RD, Hitchman RB, Richards KS et al (2008) Generation of baculovirus vectors for the high-throughput production of proteins in insect cells. Biotechnol Bioeng 101: 1115–1122
Zhao Y, Chapman DA, Jones IM (2003) Improving baculovirus recombination. Nucleic Acids Res 31:E6
Berrow NS, Alderton D, Sainsbury S et al (2007) A versatile ligation-independent cloning method suitable for high-throughput expression screening applications. Nucleic Acids Res 35:e45
Hitchman RB, Possee RD, King LA (2012) High-throughput baculovirus expression in insect cells. Methods Mol Biol 824:609–627
Hitchman RB, Siaterli EA, Nixon CP et al (2007) Quantitative real-time PCR for rapid and accurate titration of recombinant baculovirus particles. Biotechnol Bioeng 96:810–814
Bahia D, Cheung R, Buchs M et al (2005) Optimisation of insect cell growth in deep-well blocks: development of a high-throughput insect cell expression screen. Protein Expr Purif 39:61–70
Berrow NS, Alderton D, Sainsbury S et al (2007) A versatile ligation-independent cloning method suitable for high-throughput expression screening applications. Nucleic Acids Res 35:e45
Schlaeppi JM, Henke M, Mahnke M et al (2006) A semi-automated large-scale process for the production of recombinant tagged proteins in the Baculovirus expression system. Protein Expr Purif 50:185–195
Li TC, Scotti PD, Miyamura T et al (2007) Latent infection of a new alphanodavirus in an insect cell line. J Virol 81:10890–10896
Scherer WF, Hurlbut HS (1967) Nodamura virus from Japan: a new and unusual arbovirus resistant to diethyl ether and chloroform. Am J Epidemiol 86:271–285
Garzon S, Strykowski H, Charpentier G (1990) Implication of mitochondria in the replication of Nodamura virus in larvae of the Lepidoptera, Galleria mellonella (L.) and in suckling mice. Arch Virol 113:165–176
Appleton BA, Wu P, Maloney J et al (2007) Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding. EMBO J 26: 4902–4912
Fellouse FA, Li B, Compaan DM et al (2005) Molecular recognition by a binary code. J Mol Biol 348:1153–1162
Patel D, Lahiji A, Patel S et al (2007) Monoclonal antibody cetuximab binds to and down-regulates constitutively activated epidermal growth factor receptor vIII on the cell surface. Anticancer Res 27:3355–3366
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2014 Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Cremer, H., Bechtold, I., Mahnke, M., Assenberg, R. (2014). Efficient Processes for Protein Expression Using Recombinant Baculovirus Particles. In: Pörtner, R. (eds) Animal Cell Biotechnology. Methods in Molecular Biology, vol 1104. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-733-4_24
Download citation
DOI: https://doi.org/10.1007/978-1-62703-733-4_24
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-62703-732-7
Online ISBN: 978-1-62703-733-4
eBook Packages: Springer Protocols