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Efficient production of foot-and-mouth disease virus empty capsids in insect cells following down regulation of 3C protease activity

Porta, C., Xu, X., Loureiro, S., Paramasivam, S., Ren, J., Al-Khalil, T., Burman, A., Jackson, T., Blesham, G. J., Curry, S., Lomonossoff, G. P., Parida, S., Paton, D., Li, Y., Wilsden, G., Ferris, N., Owens, R., Kotecha, A., Fry, E., Stuart, D. I. , Charleston, B. and Jones, I. M. (2013) Efficient production of foot-and-mouth disease virus empty capsids in insect cells following down regulation of 3C protease activity. Journal of Virological Methods, 187 (2). pp. 406-412. ISSN 0166-0934

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To link to this item DOI: 10.1016/j.jviromet.2012.11.011

Abstract/Summary

Foot-and-mouth disease virus (FMDV) is a significant economically and distributed globally pathogen of Artiodactyla. Current vaccines are chemically inactivated whole virus particles that require large-scale virus growth in strict bio-containment with the associated risks of accidental release or incomplete inactivation. Non-infectious empty capsids are structural mimics of authentic particles with no associated risk and constitute an alternate vaccine candidate. Capsids self-assemble from the processed virus structural proteins, VP0, VP3 and VP1, which are released from the structural protein precursor P1-2A by the action of the virus-encoded 3C protease. To date recombinant empty capsid assembly has been limited by poor expression levels, restricting the development of empty capsids as a viable vaccine. Here expression of the FMDV structural protein precursor P1-2A in insect cells is shown to be efficient but linkage of the cognate 3C protease to the C-terminus reduces expression significantly. Inactivation of the 3C enzyme in a P1-2A-3C cassette allows expression and intermediate levels of 3C activity resulted in efficient processing of the P1-2A precursor into the structural proteins which assembled into empty capsids. Expression was independent of the insect host cell background and leads to capsids that are recognised as authentic by a range of anti-FMDV bovine sera suggesting their feasibility as an alternate vaccine.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences > Biomedical Sciences
ID Code:29916
Publisher:Elsevier

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