Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope

The immunodominant epitope of dengue virus envelope protein (E) induces poorly neutralizing antibodies, which poses a problem for vaccine development. Here, the authors engineer covalently locked E dimers exposing an epitope that has been shown to induce potent and broadly neutralizing antibodies.

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Autores principales:	Alexander Rouvinski, Wanwisa Dejnirattisai, Pablo Guardado-Calvo, Marie-Christine Vaney, Arvind Sharma, Stéphane Duquerroy, Piyada Supasa, Wiyada Wongwiwat, Ahmed Haouz, Giovanna Barba-Spaeth, Juthathip Mongkolsapaya, Félix A. Rey, Gavin R. Screaton
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c0392b2c359d48c4a3fd76ff74086826
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spelling	oai:doaj.org-article:c0392b2c359d48c4a3fd76ff740868262021-12-02T17:06:18ZCovalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope10.1038/ncomms154112041-1723https://doaj.org/article/c0392b2c359d48c4a3fd76ff740868262017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15411https://doaj.org/toc/2041-1723The immunodominant epitope of dengue virus envelope protein (E) induces poorly neutralizing antibodies, which poses a problem for vaccine development. Here, the authors engineer covalently locked E dimers exposing an epitope that has been shown to induce potent and broadly neutralizing antibodies.Alexander RouvinskiWanwisa DejnirattisaiPablo Guardado-CalvoMarie-Christine VaneyArvind SharmaStéphane DuquerroyPiyada SupasaWiyada WongwiwatAhmed HaouzGiovanna Barba-SpaethJuthathip MongkolsapayaFélix A. ReyGavin R. ScreatonNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Alexander Rouvinski Wanwisa Dejnirattisai Pablo Guardado-Calvo Marie-Christine Vaney Arvind Sharma Stéphane Duquerroy Piyada Supasa Wiyada Wongwiwat Ahmed Haouz Giovanna Barba-Spaeth Juthathip Mongkolsapaya Félix A. Rey Gavin R. Screaton Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope
description	The immunodominant epitope of dengue virus envelope protein (E) induces poorly neutralizing antibodies, which poses a problem for vaccine development. Here, the authors engineer covalently locked E dimers exposing an epitope that has been shown to induce potent and broadly neutralizing antibodies.
format	article
author	Alexander Rouvinski Wanwisa Dejnirattisai Pablo Guardado-Calvo Marie-Christine Vaney Arvind Sharma Stéphane Duquerroy Piyada Supasa Wiyada Wongwiwat Ahmed Haouz Giovanna Barba-Spaeth Juthathip Mongkolsapaya Félix A. Rey Gavin R. Screaton
author_facet	Alexander Rouvinski Wanwisa Dejnirattisai Pablo Guardado-Calvo Marie-Christine Vaney Arvind Sharma Stéphane Duquerroy Piyada Supasa Wiyada Wongwiwat Ahmed Haouz Giovanna Barba-Spaeth Juthathip Mongkolsapaya Félix A. Rey Gavin R. Screaton
author_sort	Alexander Rouvinski
title	Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope
title_short	Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope
title_full	Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope
title_fullStr	Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope
title_full_unstemmed	Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope
title_sort	covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/c0392b2c359d48c4a3fd76ff74086826
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Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope

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