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The expression in plants of an engineered VP2 protein of Infectious Bursal Disease Virus induces formation of structurally heterogeneous particles that protect from a very virulent viral strain

TitleThe expression in plants of an engineered VP2 protein of Infectious Bursal Disease Virus induces formation of structurally heterogeneous particles that protect from a very virulent viral strain
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2021
AuthorsMarusic, Carla, Touzani C.D., Bortolami A., Donini Marcello, Zanardello C., Lico Chiara, Rage E., Fellahi S., Houadfi M.E., Terregino C., and Baschieri Selene
JournalPLoS ONE
Volume16
ISSN19326203
Keywordsanimal, animal experiment, animal tissue, Animals, antibody production, article, Blotting, bursa Fabricii, Capsid, chicken, Chickens, controlled study, electron, enzyme linked immunosorbent assay, Enzyme-Linked Immunosorbent Assay, epitope, genetics, germfree chicken, immune deficiency, infectious bursal disease, infectious bursal disease vaccine, Infectious bursal disease virus, insect cell, metabolism, Microscopy, Mortality, neutralizing antibody, Nicotiana benthamiana, nobilis gumboro, nonhuman, Pathogenicity, physiology, protein assembly, Protein Conformation, protein engineering, protein expression, protein VP2, recombinant protein, Recombinant Proteins, structural protein, sucrose density gradient centrifugation, survival rate, Tobacco, Transmission, Transmission electron microscopy, virulence, virus capsid, virus like agent, virus particle, virus strain, virus virulence, Western, Western blotting, yeast cell
Abstract

Infectious Bursal Disease Virus (IBDV), the etiological agent of Gumboro disease, causes mortality and immunosuppression in chickens and major losses to poultry industry worldwide. The IBDV major capsid protein VP2 is considered the best candidate for the production of novel subunit vaccines. This structural protein contains the major conformational epitopes responsible for the induction of IBDV neutralizing antibodies in chickens and has been demonstrated able to form supramolecular structures in yeast and insect cells. The aim of this study was to express an engineered version of the VP2 protein (His-pVP2) to verify its ability to self-assemble into virus-like particles in plants. The recombinant VP2 was transiently expressed by agroinfiltration in Nicotiana benthamiana and transmission electron microscopy of sucrose density gradient fractions revealed the presence of a mixed population of differently shaped particles ranging from spherical capsids, with a diameter between 25 and 70 nm, to tubular structures, with variable length (from 100 to 400 nm). The recombinant VP2-based particles when used for the intramuscular immunization of specific-pathogen-free chicks resulted able to induce the production of anti-IBDV specific antibodies at titers comparable to those induced by a commercial vaccine. Moreover, all the immunized birds survived to the challenge with a Moroccan very virulent IBDV strain with no major histomorphological alterations of the Bursa of Fabricius, similarly to what obtained with the commercial inactivated vaccine. © 2021 Marusic et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85101317570&doi=10.1371%2fjournal.pone.0247134&partnerID=40&md5=a26448c46bc75adb1c7c8f327b2aa130
DOI10.1371/journal.pone.0247134
Citation KeyMarusic2021