Full inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.

Whole inactivated vaccines (WIVs) possess greater immunogenicity than split or subunit vaccines, and recent studies have demonstrated that WIVs with preserved fusogenic activity are more protective than non-fusogenic WIVs. In this work, we describe the inactivation of human influenza virus X-31 by h...

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Autores principales:	Carlos H Dumard, Shana P C Barroso, Guilherme A P de Oliveira, Carlos A M Carvalho, Andre M O Gomes, José Nelson S S Couceiro, Davis F Ferreira, Dirlei Nico, Andrea C Oliveira, Jerson L Silva, Patrícia S Santos
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/69e65d813b2749b885bd2a31fe2d950f
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spelling	oai:doaj.org-article:69e65d813b2749b885bd2a31fe2d950f2021-11-18T08:44:52ZFull inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.1932-620310.1371/journal.pone.0080785https://doaj.org/article/69e65d813b2749b885bd2a31fe2d950f2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24282553/?tool=EBIhttps://doaj.org/toc/1932-6203Whole inactivated vaccines (WIVs) possess greater immunogenicity than split or subunit vaccines, and recent studies have demonstrated that WIVs with preserved fusogenic activity are more protective than non-fusogenic WIVs. In this work, we describe the inactivation of human influenza virus X-31 by high hydrostatic pressure (HHP) and analyze the effects on the structure by spectroscopic measurements, light scattering, and electron microscopy. We also investigated the effects of HHP on the glycoprotein activity and fusogenic activity of the viral particles. The electron microscopy data showed pore formation on the viral envelope, but the general morphology was preserved, and small variations were seen in the particle structure. The activity of hemagglutinin (HA) during the process of binding and fusion was affected in a time-dependent manner, but neuraminidase (NA) activity was not affected. Infectious activity ceased after 3 hours of pressurization, and mice were protected from infection after being vaccinated. Our results revealed full viral inactivation with overall preservation of viral structure and maintenance of fusogenic activity, thereby conferring protection against infection. A strong response consisting of serum immunoglobulin IgG1, IgG2a, and serum and mucosal IgA was also detected after vaccination. Thus, our data strongly suggest that applying hydrostatic pressure may be an effective method for developing new vaccines against influenza A as well as other viruses.Carlos H DumardShana P C BarrosoGuilherme A P de OliveiraCarlos A M CarvalhoAndre M O GomesJosé Nelson S S CouceiroDavis F FerreiraDirlei NicoAndrea C OliveiraJerson L SilvaPatrícia S SantosPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 11, p e80785 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Carlos H Dumard Shana P C Barroso Guilherme A P de Oliveira Carlos A M Carvalho Andre M O Gomes José Nelson S S Couceiro Davis F Ferreira Dirlei Nico Andrea C Oliveira Jerson L Silva Patrícia S Santos Full inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.
description	Whole inactivated vaccines (WIVs) possess greater immunogenicity than split or subunit vaccines, and recent studies have demonstrated that WIVs with preserved fusogenic activity are more protective than non-fusogenic WIVs. In this work, we describe the inactivation of human influenza virus X-31 by high hydrostatic pressure (HHP) and analyze the effects on the structure by spectroscopic measurements, light scattering, and electron microscopy. We also investigated the effects of HHP on the glycoprotein activity and fusogenic activity of the viral particles. The electron microscopy data showed pore formation on the viral envelope, but the general morphology was preserved, and small variations were seen in the particle structure. The activity of hemagglutinin (HA) during the process of binding and fusion was affected in a time-dependent manner, but neuraminidase (NA) activity was not affected. Infectious activity ceased after 3 hours of pressurization, and mice were protected from infection after being vaccinated. Our results revealed full viral inactivation with overall preservation of viral structure and maintenance of fusogenic activity, thereby conferring protection against infection. A strong response consisting of serum immunoglobulin IgG1, IgG2a, and serum and mucosal IgA was also detected after vaccination. Thus, our data strongly suggest that applying hydrostatic pressure may be an effective method for developing new vaccines against influenza A as well as other viruses.
format	article
author	Carlos H Dumard Shana P C Barroso Guilherme A P de Oliveira Carlos A M Carvalho Andre M O Gomes José Nelson S S Couceiro Davis F Ferreira Dirlei Nico Andrea C Oliveira Jerson L Silva Patrícia S Santos
author_facet	Carlos H Dumard Shana P C Barroso Guilherme A P de Oliveira Carlos A M Carvalho Andre M O Gomes José Nelson S S Couceiro Davis F Ferreira Dirlei Nico Andrea C Oliveira Jerson L Silva Patrícia S Santos
author_sort	Carlos H Dumard
title	Full inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.
title_short	Full inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.
title_full	Full inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.
title_fullStr	Full inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.
title_full_unstemmed	Full inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.
title_sort	full inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/69e65d813b2749b885bd2a31fe2d950f
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Full inactivation of human influenza virus by high hydrostatic pressure preserves virus structure and membrane fusion while conferring protection to mice against infection.

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