2011
DOI: 10.1007/978-94-007-1257-7_3
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Production of Antibody in Insect Cells

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Cited by 12 publications
(12 citation statements)
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“…[8][9][10] In this system, following infection with a recombinant nucleopolyhedrovirus (NPV) carrying the foreign gene of interest, lepidopteran insect cells produce extremely large quantities of biologically active proteins with complex folding and posttranslational processing and modifications performed in higher eukaryotes during the very late phase of infection. [11][12][13] Compared with mammalian cells, insect cells are easy to culture, and the growth rates of both cells are comparable. Insect cells can be maintained at around 27 °C without CO 2 supplementation in the Five cells than with the baculovirus-insect cell system (approximately 3 μg/ml).…”
Section: Production Of Japanese Encephalitis Virus-like Particles In mentioning
confidence: 99%
See 1 more Smart Citation
“…[8][9][10] In this system, following infection with a recombinant nucleopolyhedrovirus (NPV) carrying the foreign gene of interest, lepidopteran insect cells produce extremely large quantities of biologically active proteins with complex folding and posttranslational processing and modifications performed in higher eukaryotes during the very late phase of infection. [11][12][13] Compared with mammalian cells, insect cells are easy to culture, and the growth rates of both cells are comparable. Insect cells can be maintained at around 27 °C without CO 2 supplementation in the Five cells than with the baculovirus-insect cell system (approximately 3 μg/ml).…”
Section: Production Of Japanese Encephalitis Virus-like Particles In mentioning
confidence: 99%
“…9 Stably transformed insect cells allow the constitutive production of recombinant proteins and can be employed as attractive alternative platforms to the baculovirus-insect cell system. 13,[16][17][18][19][20] They are particularly useful for the production of secreted complex proteins, because the protein synthesis and processing machinery of the host insect cell is not compromised by baculoviral infection. Recently, we investigated the production of JE VLPs in stably transformed lepidopteran insect cells.…”
mentioning
confidence: 99%
“…Recently, baculoviruses such as the Autographa californica nucleopolyhedrovirus (AcNPV) have been successfully used for the display of foreign proteins on the surface of viral particles by fusing the protein to the major baculoviral envelope glycoprotein, gp64 (Boublik et al 1995;Grabherr et al 2001;Mäkelä and Oker-Blom 2006;Yamaji 2011). After the infection of insect cells with such a recombinant baculovirus, the gp64-fusion proteins are expressed and transported to the cell membrane, where they are picked up by progeny viruses during the budding process, thereby displaying the gp64-fusion protein on the surface of baculovirus particles.…”
Section: Introductionmentioning
confidence: 99%
“…Insect cells are ideal host cells that efficiently and safely produce recombinant proteins with complex folding and post-translational processing and modifications found in higher eukaryotes (Kost et al 2005;Luckow 1995;Yamaji 2011). The baculovirus-insect cell system has been used extensively for the production of various mammalian virus proteins including a wide range of VLPs (Cox 2012;Kost et al 2005;Metz and Pijlman 2011;van Oers 2006;Vicente et al 2011).…”
Section: Introductionmentioning
confidence: 99%
“…Successful expressions have been demonstrated: Japanese encephalitis (JE) VLPs in a stably transformed Drosophila cell line (Zhang et al 2007); JE VLPs in Trichoplusia ni BTI-TN-5B1-4 (High Five) cells (Yamaji et al 2009(Yamaji et al , 2010; HIV-1 Pr55gag-based VLPs in High Five cells (Tagliamonte et al 2010); Rous sarcoma virus protein-based VLPs in High Five cells (Deo et al 2011); and, double-layered rotavirus-like particles in Drosophila melanogaster S2 cells (Lee et al 2011). When lepidopteran insect cells, such as Sf9 and High Five cells, are used as host cells for stable expression, the choice of a promoter to drive the heterologous gene expression is crucial as the use of weak promoters results in low recombinant protein yields (Yamaji 2011). Recently, a high-level expression vector containing the Bombyx mori cytoplasmic actin promoter, from which foreign gene expression is stimulated with the B. mori NPV (BmNPV) IE-1 transactivator and the BmNPV HR3 enhancer, has been developed for lepidopteran insect cells (Farrell et al 1998Keith et al 1999).…”
Section: Introductionmentioning
confidence: 99%