Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions

Antibodies blocking the V1V2 domain of HIV Envelope from binding integrin are associated with positive disease outcomes. Here, Wibmer et al. determine the structure of full length V1V2 bound to these antibodies, revealing an alternative fold of V1V2 with exposed integrin-binding sites that functions...

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Autores principales:	Constantinos Kurt Wibmer, Simone I. Richardson, Jason Yolitz, Claudia Cicala, James Arthos, Penny L. Moore, Lynn Morris
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c4e7d426f92846dd85c6cb2ac46ed15d
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spelling	oai:doaj.org-article:c4e7d426f92846dd85c6cb2ac46ed15d2021-12-02T17:31:29ZCommon helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions10.1038/s41467-018-06794-x2041-1723https://doaj.org/article/c4e7d426f92846dd85c6cb2ac46ed15d2018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06794-xhttps://doaj.org/toc/2041-1723Antibodies blocking the V1V2 domain of HIV Envelope from binding integrin are associated with positive disease outcomes. Here, Wibmer et al. determine the structure of full length V1V2 bound to these antibodies, revealing an alternative fold of V1V2 with exposed integrin-binding sites that functions on non-native Envelope.Constantinos Kurt WibmerSimone I. RichardsonJason YolitzClaudia CicalaJames ArthosPenny L. MooreLynn MorrisNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Constantinos Kurt Wibmer Simone I. Richardson Jason Yolitz Claudia Cicala James Arthos Penny L. Moore Lynn Morris Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions
description	Antibodies blocking the V1V2 domain of HIV Envelope from binding integrin are associated with positive disease outcomes. Here, Wibmer et al. determine the structure of full length V1V2 bound to these antibodies, revealing an alternative fold of V1V2 with exposed integrin-binding sites that functions on non-native Envelope.
format	article
author	Constantinos Kurt Wibmer Simone I. Richardson Jason Yolitz Claudia Cicala James Arthos Penny L. Moore Lynn Morris
author_facet	Constantinos Kurt Wibmer Simone I. Richardson Jason Yolitz Claudia Cicala James Arthos Penny L. Moore Lynn Morris
author_sort	Constantinos Kurt Wibmer
title	Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions
title_short	Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions
title_full	Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions
title_fullStr	Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions
title_full_unstemmed	Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions
title_sort	common helical v1v2 conformations of hiv-1 envelope expose the α4β7 binding site on intact virions
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/c4e7d426f92846dd85c6cb2ac46ed15d
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Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions

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