Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements

Here, using cryo-EM and smFRET, Henderson et al. show how tryptophan 571 in the HIV-1 Env acts as a conformational switch during receptor-mediated viral entry and design HIV-1 Env proteins that cannot undergo conformational changes. This has important implications for HIV-1 vaccine design.

Bibliographic Details
Main Authors: Rory Henderson, Maolin Lu, Ye Zhou, Zekun Mu, Robert Parks, Qifeng Han, Allen L. Hsu, Elizabeth Carter, Scott C. Blanchard, R J Edwards, Kevin Wiehe, Kevin O. Saunders, Mario J. Borgnia, Alberto Bartesaghi, Walther Mothes, Barton F. Haynes, Priyamvada Acharya, S. Munir Alam
Format: Article
Language:English
Published: Nature Publishing Group 2020-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-14196-w
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spelling doaj-66b0bc924f5e41b8ab9751e365c7c9672021-05-11T09:06:59ZengNature Publishing GroupNature Communications2041-17232020-01-0111111410.1038/s41467-019-14196-wDisruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangementsRory Henderson0Maolin Lu1Ye Zhou2Zekun Mu3Robert Parks4Qifeng Han5Allen L. Hsu6Elizabeth Carter7Scott C. Blanchard8R J Edwards9Kevin Wiehe10Kevin O. Saunders11Mario J. Borgnia12Alberto Bartesaghi13Walther Mothes14Barton F. Haynes15Priyamvada Acharya16S. Munir Alam17Department of Medicine, Duke University School of MedicineDepartment of Microbial Pathogenesis, Yale University School of MedicineDepartment of Computer Science, Duke UniversityDepartment of Immunology, Duke University School of MedicineDuke Human Vaccine Institute, Duke University School of MedicineDepartment of Medicine, Duke University School of MedicineGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human ServicesDepartment of Medicine, Duke University School of MedicineDepartment of Physiology and Biophysics, Weill Cornell MedicineDepartment of Medicine, Duke University School of MedicineDepartment of Medicine, Duke University School of MedicineDuke Human Vaccine Institute, Duke University School of MedicineGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human ServicesDepartment of Computer Science, Duke UniversityDepartment of Microbial Pathogenesis, Yale University School of MedicineDepartment of Medicine, Duke University School of MedicineDuke Human Vaccine Institute, Duke University School of MedicineDepartment of Medicine, Duke University School of MedicineHere, using cryo-EM and smFRET, Henderson et al. show how tryptophan 571 in the HIV-1 Env acts as a conformational switch during receptor-mediated viral entry and design HIV-1 Env proteins that cannot undergo conformational changes. This has important implications for HIV-1 vaccine design.https://doi.org/10.1038/s41467-019-14196-w
collection DOAJ
language English
format Article
sources DOAJ
author Rory Henderson
Maolin Lu
Ye Zhou
Zekun Mu
Robert Parks
Qifeng Han
Allen L. Hsu
Elizabeth Carter
Scott C. Blanchard
R J Edwards
Kevin Wiehe
Kevin O. Saunders
Mario J. Borgnia
Alberto Bartesaghi
Walther Mothes
Barton F. Haynes
Priyamvada Acharya
S. Munir Alam
spellingShingle Rory Henderson
Maolin Lu
Ye Zhou
Zekun Mu
Robert Parks
Qifeng Han
Allen L. Hsu
Elizabeth Carter
Scott C. Blanchard
R J Edwards
Kevin Wiehe
Kevin O. Saunders
Mario J. Borgnia
Alberto Bartesaghi
Walther Mothes
Barton F. Haynes
Priyamvada Acharya
S. Munir Alam
Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements
Nature Communications
author_facet Rory Henderson
Maolin Lu
Ye Zhou
Zekun Mu
Robert Parks
Qifeng Han
Allen L. Hsu
Elizabeth Carter
Scott C. Blanchard
R J Edwards
Kevin Wiehe
Kevin O. Saunders
Mario J. Borgnia
Alberto Bartesaghi
Walther Mothes
Barton F. Haynes
Priyamvada Acharya
S. Munir Alam
author_sort Rory Henderson
title Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements
title_short Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements
title_full Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements
title_fullStr Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements
title_full_unstemmed Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements
title_sort disruption of the hiv-1 envelope allosteric network blocks cd4-induced rearrangements
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-01-01
description Here, using cryo-EM and smFRET, Henderson et al. show how tryptophan 571 in the HIV-1 Env acts as a conformational switch during receptor-mediated viral entry and design HIV-1 Env proteins that cannot undergo conformational changes. This has important implications for HIV-1 vaccine design.
url https://doi.org/10.1038/s41467-019-14196-w
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