Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells

Abstract Dengue and Zika are two of the most important human viral pathogens worldwide. In both cases, the envelope glycoprotein E is the main target of the antibody response. Recently, new complex quaternary epitopes were identified which are the consequence of the arrangement of the antiparallel E...

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Autores principales:	J. L. Slon Campos, S. Marchese, J. Rana, M. Mossenta, M. Poggianella, M. Bestagno, O. R. Burrone
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b62962fcee53410a94398caacdecb0aa
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spelling	oai:doaj.org-article:b62962fcee53410a94398caacdecb0aa2021-12-02T11:53:13ZTemperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells10.1038/s41598-017-01097-52045-2322https://doaj.org/article/b62962fcee53410a94398caacdecb0aa2017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01097-5https://doaj.org/toc/2045-2322Abstract Dengue and Zika are two of the most important human viral pathogens worldwide. In both cases, the envelope glycoprotein E is the main target of the antibody response. Recently, new complex quaternary epitopes were identified which are the consequence of the arrangement of the antiparallel E dimers on the viral surface. Such epitopes can be exploited to develop more efficient cross-neutralizing vaccines. Here we describe a successful covalent stabilization of E dimers from Dengue and Zika viruses in mammalian cells. Folding and dimerization of secretory E was found to be strongly dependent on temperature but independent of PrM co-expression. In addition, we found that, due to the close relationship between flaviviruses, Dengue and Zika viruses E proteins can form heterodimers and assemble into mosaic viral particles. Finally, we present new virus-free analytical platforms to study and screen antibody responses against Dengue and Zika, which allow for differentiation of epitopes restricted to specific domains, dimers and higher order arrangements of E.J. L. Slon CamposS. MarcheseJ. RanaM. MossentaM. PoggianellaM. BestagnoO. R. BurroneNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q J. L. Slon Campos S. Marchese J. Rana M. Mossenta M. Poggianella M. Bestagno O. R. Burrone Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells
description	Abstract Dengue and Zika are two of the most important human viral pathogens worldwide. In both cases, the envelope glycoprotein E is the main target of the antibody response. Recently, new complex quaternary epitopes were identified which are the consequence of the arrangement of the antiparallel E dimers on the viral surface. Such epitopes can be exploited to develop more efficient cross-neutralizing vaccines. Here we describe a successful covalent stabilization of E dimers from Dengue and Zika viruses in mammalian cells. Folding and dimerization of secretory E was found to be strongly dependent on temperature but independent of PrM co-expression. In addition, we found that, due to the close relationship between flaviviruses, Dengue and Zika viruses E proteins can form heterodimers and assemble into mosaic viral particles. Finally, we present new virus-free analytical platforms to study and screen antibody responses against Dengue and Zika, which allow for differentiation of epitopes restricted to specific domains, dimers and higher order arrangements of E.
format	article
author	J. L. Slon Campos S. Marchese J. Rana M. Mossenta M. Poggianella M. Bestagno O. R. Burrone
author_facet	J. L. Slon Campos S. Marchese J. Rana M. Mossenta M. Poggianella M. Bestagno O. R. Burrone
author_sort	J. L. Slon Campos
title	Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells
title_short	Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells
title_full	Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells
title_fullStr	Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells
title_full_unstemmed	Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells
title_sort	temperature-dependent folding allows stable dimerization of secretory and virus-associated e proteins of dengue and zika viruses in mammalian cells
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/b62962fcee53410a94398caacdecb0aa
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Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells

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