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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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
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spelling doaj-c4e7d426f92846dd85c6cb2ac46ed15d2021-05-11T10:11:57ZengNature Publishing GroupNature Communications2041-17232018-10-019111410.1038/s41467-018-06794-xCommon helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virionsConstantinos Kurt Wibmer0Simone I. Richardson1Jason Yolitz2Claudia Cicala3James Arthos4Penny L. Moore5Lynn Morris6Centre for HIV and STIs, National Institute for Communicable Diseases (NICD), of the National Health Laboratory Service (NHLS)Centre for HIV and STIs, National Institute for Communicable Diseases (NICD), of the National Health Laboratory Service (NHLS)Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of HealthLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of HealthLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of HealthCentre for HIV and STIs, National Institute for Communicable Diseases (NICD), of the National Health Laboratory Service (NHLS)Centre for HIV and STIs, National Institute for Communicable Diseases (NICD), of the National Health Laboratory Service (NHLS)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.https://doi.org/10.1038/s41467-018-06794-x
collection DOAJ
language English
format Article
sources DOAJ
author Constantinos Kurt Wibmer
Simone I. Richardson
Jason Yolitz
Claudia Cicala
James Arthos
Penny L. Moore
Lynn Morris
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-10-01
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.
url https://doi.org/10.1038/s41467-018-06794-x
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