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.
Saved in:
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: | EN |
Published: |
Nature Portfolio
2020
|
Subjects: | |
Online Access: | https://doaj.org/article/66b0bc924f5e41b8ab9751e365c7c967 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Selection of immunoglobulin elbow region mutations impacts interdomain conformational flexibility in HIV-1 broadly neutralizing antibodies
by: Rory Henderson, et al.
Published: (2019) -
Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation
by: Vojtech Vyklicky, et al.
Published: (2021) -
Difficult-to-neutralize global HIV-1 isolates are neutralized by antibodies targeting open envelope conformations
by: Qifeng Han, et al.
Published: (2019) -
Structural mechanism of trimeric HIV-1 envelope glycoprotein activation.
by: Erin E H Tran, et al.
Published: (2012) -
HIV envelope V3 region mimic embodies key features of a broadly neutralizing antibody lineage epitope
by: Daniela Fera, et al.
Published: (2018)