Easy expression of the C-terminal heavy chain domain of botulinum neurotoxin serotype A as a vaccine candidate using a bi-cistronic baculovirus system

Villaflores, Oliver B.; Hsei, Chein-Ming; Teng, Chao-Yi; Chen, Ying‐Ju; Wey, Jiunn-Jye; Tsui, Pei-Yi; Shyu, Rong-Hwa; Tung, Kuo‐Lun; Yeh, Jui‐Ming; Chiao, Der-Jiang; Wu, Tzong‐Yuan

doi:10.1016/j.jviromet.2012.11.035

Cited by 11 publications

(7 citation statements)

References 40 publications

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“…In addition to glycoprotein‐based vaccines, the BEVS platform has shown early promise for the production of toxin‐based vaccines. For example, the C‐terminal heavy chain domain of clostridial botulinum neurotoxin, a highly toxic protein that causes botulism, has been produced with BEVS and has demonstrated immunogenicity and challenge protection in mice [114, 115]. Recombinant toxin vaccines for other diseases such as Clostridium difficile could also be possible [116, 117].…”

Section: Conclusion and Future Opportunitiesmentioning

confidence: 99%

The baculovirus expression vector system: A commercial manufacturing platform for viral vaccines and gene therapy vectors

Felberbaum¹

2015

Biotechnology Journal

208

141

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The baculovirus expression vector system (BEVS) platform has become an established manufacturing platform for the production of viral vaccines and gene therapy vectors. Nine BEVS-derived products have been approved - four for human use (Cervarix(®), Provenge(®), Glybera(®) and Flublok(®)) and five for veterinary use (Porcilis(®) Pesti, BAYOVAC CSF E2(®), Circumvent(®) PCV, Ingelvac CircoFLEX(®) and Porcilis(®) PCV). The BEVS platform offers many advantages, including manufacturing speed, flexible product design, inherent safety and scalability. This combination of features and product approvals has previously attracted interest from academic researchers, and more recently from industry leaders, to utilize BEVS to develop next generation vaccines, vectors for gene therapy, and other biopharmaceutical complex proteins. In this review, we explore the BEVS platform, detailing how it works, platform features and limitations and important considerations for manufacturing and regulatory approval. To underscore the growth in opportunities for BEVS-derived products, we discuss the latest product developments in the gene therapy and influenza vaccine fields that follow in the wake of the recent product approvals of Glybera(®) and Flublok(®), respectively. We anticipate that the utility of the platform will expand even further as new BEVS-derived products attain licensure. Finally, we touch on some of the areas where new BEVS-derived products are likely to emerge.

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Section: Conclusion and Future Opportunitiesmentioning

confidence: 99%

The baculovirus expression vector system: A commercial manufacturing platform for viral vaccines and gene therapy vectors

Felberbaum¹

2015

Biotechnology Journal

208

141

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“…As an alternative, the Hc domain of BoNT/A as a subunit vaccine antigen was expressed using a bi-cistronic baculovirus-Sf21 insect cell expression system. 26 In current study, a 293E expression system was used to express the Hc of BoNT/B as soluble recombinant protein for experimental vaccine evaluation. High level of recombinant secreted BHc protein produced by the 293E expression system was immunorecognized specifically by anti-BoNT/B sera.…”

Section: Discussionmentioning

confidence: 99%

Production and evaluation of a recombinant subunit vaccine against botulinum neurotoxin serotype B using a 293E expression system

Shi²,

Liu³

et al. 2014

Human Vaccines & Immunotherapeutics

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Keywords: Botulinum neurotoxin serotype B, Hc, expression, vaccine, binding activityAlthough Escherichia coli and yeast were commonly used to express recombinant Hc of botulinum neurotoxins, as an alternative, in current study, a 293E expression system was used to express the Hc of botulinum neurotoxin serotype B (BHc) as soluble recombinant protein for experimental vaccine evaluation. Our results demonstrated that the 293E expression system could produce high level of recombinant secreted BHc protein, which was immunorecognized specifically by anti-botulinum neurotoxin serotype B (BoNT/B) sera and showed ganglioside binding activities. The serological response and efficacy of recombinant BHc formulated with aluminum hydroxide adjuvant were evaluated in mice. Immunization with Alhydrogel-formulated BHc subunit vaccine afforded the effective protection against BoNT/B challenge. A frequency-and dose-dependent effect to immunization with BHc subunit vaccine was observed and the ELISA antibody titers correlated well with neutralizing antibody titers and protection. And a solid-phase assay showed that the neutralizing antibodies from the BHc-immunized mice inhibited the binding of BHc to the ganglioside GT1b. Our results also show that the plasmid pABE293SBHc derived of the 293E expression system as DNA vaccine is capable of inducing stronger humoral response and protective efficacy against BoNT/B than the pVAX1SBHc. In summary, immunization with the 293E-expressed BHc protein generates effective immune protection against BoNT/B as E. coli or yeast-expressed BHc, so the efficient expression of botulinum Hc protein for experimental vaccine can be prepared using the 293E expression system.

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“…A number of studies have demonstrated that the 69 His tag had no effect on the activity of target protein, including enzyme (Zhou et al 2010), cytokine (Cao et al 2005), antibody (Cao et al 2006), transcription factor (Zhao et al 2010), and vaccine (Villaflores et al 2013).…”

Section: Discussionmentioning

confidence: 99%

High-level expression and characterization of bioactive human truncated variant of hepatocyte growth factor in Escherichia coli

Wang

Liu

Zhang

et al. 2014

World J Microbiol Biotechnol

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Hepatocyte growth factor (HGF) is an effective anti-fibrotic factor because of its bioactivity in inhibiting fibrosis-related proteins in the development of hepatic fibrosis. However, high-level production of bioactive mature form HGF is difficult because of its complex structure. Here, we report a non-fusion protein expression system to obtain truncated variant of N-terminal hairpin and first kringle domains of HGF (tvNK1) in Escherichia coli to determine its anti-fibrotic effects on hepatic stellate cells (HSCs). Under the selected conditions of cultivation and isopropyl-β-D-1-thiogalactopyranoside induction, the expression level of tvNK1 accounted for approximately 65 % of the total cellular protein and 50 % of fusion protein in the supernatant of whole cell lysates. The recombinant protein could be purified in one step with Ni(2+)-affinity chromatograph. Finally, about 65 mg recombinant tvNK1 was obtained from 1 l fermentation culture with no <95 % purity. In vitro, the final purified tvNK1 was shown to inhibit the proliferation of HSCs and decrease the mRNA and protein expression levels of fibrosis-related COL1A1 and α-smooth muscle actin genes.

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Easy expression of the C-terminal heavy chain domain of botulinum neurotoxin serotype A as a vaccine candidate using a bi-cistronic baculovirus system

Cited by 11 publications

References 40 publications

The baculovirus expression vector system: A commercial manufacturing platform for viral vaccines and gene therapy vectors

The baculovirus expression vector system: A commercial manufacturing platform for viral vaccines and gene therapy vectors

Production and evaluation of a recombinant subunit vaccine against botulinum neurotoxin serotype B using a 293E expression system

High-level expression and characterization of bioactive human truncated variant of hepatocyte growth factor in Escherichia coli

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