title: In planta production of two peptides of the Classical Swine Fever Virus (CSFV) E2 glycoprotein fused to the coat protein of potato virus X.
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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Dipartimento di Biologia vegetale e Biotecnologie Agroambientali e Zootecniche, Università degli Studi di Perugia, Borgo XX Giugno 74, 06121 Perugia, Italy. gpmarconi@gmail.com
authors.forename: Gianpiero
authors.initials: G
authors.lastname: Marconi
authors.forename: Emidio
authors.initials: E
authors.lastname: Albertini
authors.forename: Pierluigi
authors.initials: P
authors.lastname: Barone
authors.forename: Francesca
authors.initials: F
authors.lastname: De Marchis
authors.forename: Chiara
authors.initials: C
authors.lastname: Lico
authors.forename: Carla
authors.initials: C
authors.lastname: Marusic
authors.forename: Domenico
authors.initials: D
authors.lastname: Rutili
authors.forename: Fabio
authors.initials: F
authors.lastname: Veronesi
authors.forename: Andrea
authors.initials: A
authors.lastname: Porceddu
mesh_terms: D000818:Animals; D036022:Capsid Proteins / Q000235:genetics / Q000378:metabolism*; D006692:Classical Swine Fever Virus / Q000235:genetics / Q000378:metabolism*; D006023:Glycoproteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D010455:Peptides / Q000235:genetics / Q000378:metabolism; D030821:Plants, Genetically Modified / Q000378:metabolism; D017863:Potexvirus / Q000235:genetics / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000276:immunology / Q000378:metabolism; D014026:Nicotiana / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*
chemical_list: D036022:Capsid Proteins; D006023:Glycoproteins; D010455:Peptides; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins