Expression of Recombinant Human Interferon-γ with Antiviral Activity in the Bi-Cistronic Baculovirus-Insect/Larval System

Chen, Wen-Shuo; Villaflores, Oliver B.; Jinn, Tzyy-Rong; Chan, Ming‐Tsair; Chang, Y. C.; Wu, Tzong‐Yuan

doi:10.1271/bbb.110107

Cited by 20 publications

(6 citation statements)

References 42 publications

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“…To date, the BES has been used to manufacture several biologicals, including the interferon [14], antigen [15] and vaccine [16]. One was GlaxoSmithKline's Cervarix™ (GSK, Rixensart, Belgium), a VLP-based bivalent human papillomavirus vaccine against cervical cancer, which was approved for human use in the USA in 2009 [17].…”

Section: Bes As a Platform For Protein Expressionmentioning

confidence: 99%

Use of baculovirus expression system for generation of virus-like particles: Successes and challenges

Liu

et al. 2013

Protein Expression and Purification

106

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The baculovirus expression system (BES) has been one of the versatile platforms for the production of recombinant proteins requiring multiple post-translational modifications, such as folding, oligomerization, phosphorylation, glycosylation, acylation, disulfide bond formation and proteolytic cleavage. Advances in recombinant DNA technology have facilitated application of the BES, and made it possible to express multiple proteins simultaneously in a single infection and to produce multimeric proteins sharing functional similarity with their natural analogs. Therefore, the BES has been used for the production of recombinant proteins and the construction of virus-like particles (VLPs), as well as for the development of subunit vaccines, including VLP-based vaccines. The VLP, which consists of one or more structural proteins but no viral genome, resembles the authentic virion but cannot replicate in cells. The high-quality recombinant protein expression and post-translational modifications obtained with the BES, along with its capacity to produce multiple proteins, imply that it is ideally suited to VLP production. In this article, we critically review the pros and cons of using the BES as a platform to produce both enveloped and non-enveloped VLPs.

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Section: Bes As a Platform For Protein Expressionmentioning

confidence: 99%

Use of baculovirus expression system for generation of virus-like particles: Successes and challenges

Liu

et al. 2013

Protein Expression and Purification

106

View full text Add to dashboard Cite

show abstract

“…6. A previous study also demonstrated that an insect-produced IFN-γ analyzed using a baculovirus expression vector system showed several bands representing the different levels of N-glycosylation 33 . This heterogeneous N-glycosylation was due to underglycosylation, and it has also been observed when IFN-γ was expressed in leukocytes 34 , CHO cells 35 − 38 , and plants 39 .…”

Section: Discussionmentioning

confidence: 84%

Insights into the quality of recombinant proteins produced by two different Bombyx mori expression systems

Kajiura

Tatematsu

Nomura

et al. 2022

Preprint

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The silkworm, Bombyx mori, is an attractive host for recombinant protein production due to its high expression efficiency, quality, and quantity. Two expression systems have been widely used for recombinant protein production in B. mori: baculovirus/silkworm expression system and transgenic silkworm expression system. Both expression systems enable high protein production, but the qualities of the resulting recombinant proteins have not been well evaluated. In this study, we expressed bovine interferon g (IFN-g) using the two systems and examined the quality of the resulting proteins in terms of N-glycosylation and protein cleavage. Both expression systems successfully produced IFN-g as an N-glycoprotein. Although the production in the baculovirus/silkworm expression system was much more efficient than that in the transgenic silkworm expression system, unexpected variants of IFN-g were also produced in the former system due to the different N-glycosylation and C-terminal truncations. These results indicate that while high protein production could be achieved in the baculovirus/silkworm expression system, unintentional protein modification might occur, and therefore protein expression in the transgenic silkworm expression system is preferable from the point-of-view of N-glycosylation of the recombinant protein and evasion of unexpected attack by a protease in B. mori.

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“…6 . A previous study also demonstrated that an insect-produced IFN-γ analyzed using a baculovirus expression vector system showed several bands representing the different levels of N -glycosylation 33 . This heterogeneous N -glycosylation was due to underglycosylation, and it has also been observed when IFN-γ was expressed in leukocytes 34 , CHO cells 35 – 38 , and plants 39 .…”

Section: Discussionmentioning

confidence: 84%

Insights into the quality of recombinant proteins produced by two different Bombyx mori expression systems

Kajiura

Tatematsu

Nomura

et al. 2022

Sci Rep

View full text Add to dashboard Cite

The silkworm, Bombyx mori, is an attractive host for recombinant protein production due to its high expression efficiency, quality, and quantity. Two expression systems have been widely used for recombinant protein production in B. mori: baculovirus/silkworm expression system and transgenic silkworm expression system. Both expression systems enable high protein production, but the qualities of the resulting recombinant proteins have not been well evaluated. In this study, we expressed bovine interferon γ (IFN-γ) using the two systems and examined the quality of the resulting proteins in terms of N-glycosylation and protein cleavage. Both expression systems successfully produced IFN-γ as an N-glycoprotein. Although the production in the baculovirus/silkworm expression system was much more efficient than that in the transgenic silkworm expression system, unexpected variants of IFN-γ were also produced in the former system due to the different N-glycosylation and C-terminal truncations. These results indicate that while high protein production could be achieved in the baculovirus/silkworm expression system, unintentional protein modification might occur, and therefore protein expression in the transgenic silkworm expression system is preferable from the point-of-view of N-glycosylation of the recombinant protein and evasion of unexpected attack by a protease in B. mori.

show abstract

Expression of Recombinant Human Interferon-γ with Antiviral Activity in the Bi-Cistronic Baculovirus-Insect/Larval System

Cited by 20 publications

References 42 publications

Use of baculovirus expression system for generation of virus-like particles: Successes and challenges

Use of baculovirus expression system for generation of virus-like particles: Successes and challenges

Insights into the quality of recombinant proteins produced by two different Bombyx mori expression systems

Insights into the quality of recombinant proteins produced by two different Bombyx mori expression systems

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