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Open AccessResearch article

In planta production of two peptides of the Classical Swine Fever Virus (CSFV) E2 glycoprotein fused to the coat protein of potato virus X

Gianpiero Marconi1 email, Emidio Albertini1 email, Pierluigi Barone1,2 email, Francesca De Marchis1,3 email, Chiara Lico4 email, Carla Marusic4 email, Domenico Rutili5 email, Fabio Veronesi1 email and Andrea Porceddu1,3 email

1Dipartimento di Biologia vegetale e Biotecnologie Agroambientali e Zootecniche, Università degli Studi di Perugia, Borgo XX Giugno 74, 06121 Perugia, Italy

2University of Illinois at Urbana-Champaign, College of Agricultural, Consumer and Environmental Sciences, Department of Crop Sciences, 289 Edward R. Madigan Laboratory, 1201 West Gregory Drive, Urbana, IL 61801, USA

3Istituto di Genetica Vegetale, Sezione di Perugia, Via Madonna Alta 130, 06100 Perugia, Italy

4ENEA, Centro Ricerche Casaccia, Roma, Italy

5Istituto Sperimentale Zooprofilattico dell'Umbria e delle Marche, Sezione di Perugia, Italy

author email corresponding author email

BMC Biotechnology 2006, 6:29doi:10.1186/1472-6750-6-29

Published: 22 June 2006

Abstract

Background

Classical Swine Fever (CSFV) is one of the most important viral infectious diseases affecting wild boars and domestic pigs. The etiological agent of the disease is the CSF virus, a single stranded RNA virus belonging to the family Flaviviridae.

All preventive measures in domestic pigs have been focused in interrupting the chain of infection and in avoiding the spread of CSFV within wild boars as well as interrupting transmission from wild boars to domestic pigs. The use of plant based vaccine against CSFV would be advantageous as plant organs can be distributed without the need of particular treatments such as refrigeration and therefore large areas, populated by wild animals, could be easily covered.

Results

We report the in planta production of peptides of the classical swine fever (CSF) E2 glycoprotein fused to the coat protein of potato virus X. RT-PCR studies demonstrated that the peptide encoding sequences are correctly retained in the PVX construct after three sequential passage in Nicotiana benthamiana plants. Sequence analysis of RT-PCR products confirmed that the epitope coding sequences are replicated with high fidelity during PVX infection. Partially purified virions were able to induce an immune response in rabbits.

Conclusion

Previous reports have demonstrated that E2 synthetic peptides can efficiently induce an immunoprotective response in immunogenized animals. In this work we have showed that E2 peptides can be expressed in planta by using a modified PVX vector. These results are particularly promising for designing strategies for disease containment in areas inhabited by wild boars.


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