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
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Acceso en línea:https://doaj.org/article/c4e7d426f92846dd85c6cb2ac46ed15d
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Sumario: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.