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Development of plant-produced protein body vaccine candidates for bluetongue virus
Monday, 2017/06/05 | 07:28:33

Albertha R. van Zyl, Ann E. Meyers and Edward P. Rybicki

BMC Biotechnology 2017, 17:47, Published: 30 May 2017, DOI: 10.1186/s12896-017-0370-5

Abstract

Background

Bluetongue is a disease of domestic and wild ruminants caused by bluetongue virus serotypes (BTV), which have caused serious outbreaks worldwide. Commercially available vaccines are live-attenuated or inactivated virus strains: these are effective, but there is the risk of reversion to virulence or reassortment with circulating strains for live virus, and residual live virus for the inactivated vaccines. The live-attenuated virus vaccines are not able to distinguish naturally infected animals from vaccinated animals (DIVA compliant). Recombinant vaccines are preferable to minimize the risks associated with these vaccines, and would also enable the development of candidate vaccines that are DIVA-compliant.

Results

In this study, two novel protein body (PB) plant-produced vaccines were developed, Zera®-VP2ep and Zera®-VP2. Zera®-VP2ep contained B-cell epitope sequences of multiple BTV serotypes and Zera®-VP2 contained the full-length BTV-8 VP2 codon-optimised sequence. In addition to fulfilling the DIVA requirement, Zera®-VP2ep was aimed at being multivalent with the ability to stimulate an immune response to several BTV serotypes. Both these candidate vaccines were successfully made in N. benthamiana via transient Agrobacterium-mediated expression, and in situ TEM analysis showed that the expressed proteins accumulated within the cytoplasm of plant cells in dense membrane-defined PBs. The peptide sequences included in Zera®-VP2ep contained epitopes that bound antibodies produced against native VP2. Preliminary murine immunogenicity studies showed that the PB vaccine candidates elicited anti-VP2 immune responses in mice without the use of adjuvant.

Conclusions

These proof of concept results demonstrate that Zera®-VP2ep and Zera®-VP2 have potential as BTV vaccines and their development should be further investigated.

 

See: https://bmcbiotechnol.biomedcentral.com/articles/10.1186/s12896-017-0370-5

Figure 1: Construction of VP2ep. a Selected regions of the multiple alignment of 8 selected BTV VP2 serotype amino acid sequences are shown. The predicted epitope regions corresponding to most of the serotypes are shown below the alignment in bold and boxed in blue and green. The homologous region is boxed in purple. b The putative amino acid and nucleotide sequences of VP2ep

 

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