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

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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Bibliographic Details
Main Authors: Constantinos Kurt Wibmer, Simone I. Richardson, Jason Yolitz, Claudia Cicala, James Arthos, Penny L. Moore, Lynn Morris
Format: Article
Language:English
Published: Nature Publishing Group 2018-10-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-06794-x
Description
Summary: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.
ISSN:2041-1723

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