Baculoviruses

Nowell KW, Pettit DA, Cabral WA, et al High-level expression of the human CB2 cannabinoid receptor using a baculovirus system. Biochem Pharmacol 55 1893— 1905, 1998... 

A number of allergens from both honey bee and vespid venoms have been cloned and expressed by either Escherichia coli or baculovirus-infected insect cells (table 1) phospholipase Aj [20], hyaluronidase [21], acid phosphatase [13] and Api m6 [14] from honey bee venom, as well as antigen 5 [22], phospholipase A and hyaluronidase [23] from vespid venom, and dipeptidylpeptidases from both bee and Vespula venoms [15, 16]. Their reactivity with human-specific IgE antibodies to the respective allergens has been documented [11-16, 22, 23] and their specificity is superior... 

Xin KQ, Hamajima K, Hattori S, Cao XR, Kawamoto S, Okuda K (1999) Evidence of HIV type 1 glycoprotein 120 binding to recombinant N-methyl-D-aspartate receptor subunits expressed in a baculovirus system. AIDS Res Hum Retroviruses 15(16) 1461-1467... 

Andersen, J.N., "Temperature Effect on Recombinant Protein Production Using a Baculovirus/Insect Cell Expression System", Diploma Thesis, University of Calgary and Technical University of Denmark, 1995. 

Narum, D. L., Welling, G. W., and Thomas, A. W., Ion-exchange-immuno-affinity purification of a recombinant baculovirus Plasmodium falciparum apical membrane antigen, PF83/AMA-1, /. Chromatogr. A, 657, 357, 1993. 

Bryant Yes, although we didn t use purified IDGF, but recombinant IDGF produced from a baculovirus expression system. These are clone 8 cells from an imaginal disc we haven t tried growing the whole imaginal disc. 

Insect cell systems represent multiple advantages compared with mammalian cell cultures (1) they are easier to handle (Table 2.1) (2) cultivation media are usually cheaper (3) they need only minimum safety precautions, as baculovirus is harmless for humans (4) they provide most higher eukaryotic posttranslational modifications and heterologous eukaryotic proteins are usually obtained in their native conformation (5) the baculovirus system is easily scalable to the bioreactor scale. However, because of the viral nature of the system, continuous fermentation for transient expression is not possible - the cells finally die. 

Zhang, F., Saarinen, M.A., Itle, L.J. et al. (2002) The effect of dissolved oxygen (DO) concentration on the glycosylation of recombinant protein produced by the insect cell-baculovirus expression system. Biotechnology and Bioengineering, 11 (2), 219-224. 

Philipps, B., Forstner, M. and Mayr, L.M. (2005) A baculovirus expression vector system for simultaneous protein expression in insect and mammalian cells. Biotechnology Progress, 21 (3), 708-711. 

Kost, T.A., Condreay, J.P. and Jarvis, D.L. (2005) Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Nature Biotechnology, 23 (5), 567-575. 

Zeng, C.Q., Wentz, M.J., Cohen, J. et al. (1996) Characterization and replicase activity of double-layered and single-layered rotavirus-like particles expressed from baculovirus recombinants. Journal of Virology, 70 (5), 2736-2742. 

Kang, C.Y. (1997) Expression of human immunodeficiency virus genes using baculovirus expression system. Molecular Biotechnology, 8 (2), 173-187. 

Ghosh, S., Parvez, M.K., Banerjee, K. et al. (2002) Baculovirus as mammalian cell expression vector for gene therapy an emerging strategy. Molecular Therapy The Journal of the American Society of Gene Therapy, 6(1), 5-11. 

Assenga, S.P, You, M., Shy, C.H. et al. (2006) The use of a recombinant baculovirus expressing a chitinase from the hard tick Haemaphysalis longicornis and its potential application as a bioacaricide for tick control. Parasitology Research, 98 (2), 111-118. 

Kondo, A. and Maeda, S. (1991) Host range expansion by recombination of the baculoviruses Bombyx mori nuclear polyhedrosis virus and Autographa californica nuclear polyhedrosis virus. Journal of Virology, 65 (7), 3625-3632. 

Wu, X., Cao, C.,Xu, Y. andLu, X. (2004) Construction of a host range-expanded hybrid baculovirus of BmNPV and AcNPV, and knockout of cysteinase gene for more efficient expression. Science in China. Series C, Life Sciences, 47 (5), 406-415. 

Jarvis, D.L. (2003) Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production. Virology, 310 (1), 1-7. 

Berger, I., Fitzgerald, D.J. and Richmond, T.J. (2004) Baculovirus expression system for heterologous multiprotein complexes. Nature Biotechnology, 22 (12), 1583-1587. 

Co-expression of the human a- and p-subunits in the yeast Pichea pastoralis produces only trace amounts of active tetramer, with the majority being present in an unassembled form. Co-expression with human type III collagens, however, increases this assembly level tenfold. This indicates that collagen synthesis and the formation of an active prolyl 4-hydroxylase complex are mutually dependent processes (Vuorela et al, 1997). A similar observation has been noted for baculovirus encoded enzymes in insect cells (Lamberg et al, 1996). These findings support the hypothesis that this unusual control mechanism may be a common feature of collagen synthesis in all cell types. 

Lamberg, A., Helaakoski, T., Myllyharju, J., Peltonen, S., Notbohm, H., Pihlajaniemi, T. and Kivirikko, K.I. (1996) Characterization of human type III collagen expressed in a baculovirus system - production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit.Journal of Biological Chemistry 271, 11988-11995. 

Veijola, J., Koivunen, P., Annunen, P., Pihlajaniemi, T. and Kivirikko, K. (1994) Cloning, baculovirus expression, and characterization of the alpha-subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans - this alpha-subunit forms an active alpha-beta dimer with the human protein disulfide-isomerase beta-subunit. Journal of Biological Chemistry 269, 26746-26753. 

A wide range of proteins have been produced at laboratory scale in recombinant insect cell culture systems. The approach generally entails the infection of cultured insect cells with an engineered baculovirus (viral family that naturally infect insects) carrying the gene coding for the desired protein placed under the influence of a powerful viral promoter. Amongst the systems most commonly employed are ... 

Baculovirus/insect cell-based systems are cited as having a number of advantages, including ... 

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