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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

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 s...

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Autores principales: Marusic, Carla, Drissi Touzani, Charifa, Bortolami, Alessio, Donini, Marcello, Zanardello, Claudia, Lico, Chiara, Rage, Emile, Fellahi, Siham, El Houadfi, Mohammed, Terregino, Calogero, Baschieri, Selene
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7886152/
https://www.ncbi.nlm.nih.gov/pubmed/33592038
http://dx.doi.org/10.1371/journal.pone.0247134
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author Marusic, Carla
Drissi Touzani, Charifa
Bortolami, Alessio
Donini, Marcello
Zanardello, Claudia
Lico, Chiara
Rage, Emile
Fellahi, Siham
El Houadfi, Mohammed
Terregino, Calogero
Baschieri, Selene
author_facet Marusic, Carla
Drissi Touzani, Charifa
Bortolami, Alessio
Donini, Marcello
Zanardello, Claudia
Lico, Chiara
Rage, Emile
Fellahi, Siham
El Houadfi, Mohammed
Terregino, Calogero
Baschieri, Selene
author_sort Marusic, Carla
collection PubMed
description 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.
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spelling pubmed-78861522021-02-23 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 Marusic, Carla Drissi Touzani, Charifa Bortolami, Alessio Donini, Marcello Zanardello, Claudia Lico, Chiara Rage, Emile Fellahi, Siham El Houadfi, Mohammed Terregino, Calogero Baschieri, Selene PLoS One Research Article 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. Public Library of Science 2021-02-16 /pmc/articles/PMC7886152/ /pubmed/33592038 http://dx.doi.org/10.1371/journal.pone.0247134 Text en © 2021 Marusic et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Marusic, Carla
Drissi Touzani, Charifa
Bortolami, Alessio
Donini, Marcello
Zanardello, Claudia
Lico, Chiara
Rage, Emile
Fellahi, Siham
El Houadfi, Mohammed
Terregino, Calogero
Baschieri, Selene
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
title 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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_short 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
title_sort 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
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7886152/
https://www.ncbi.nlm.nih.gov/pubmed/33592038
http://dx.doi.org/10.1371/journal.pone.0247134
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