|Entry||Database: EMDB / ID: EMD-8629|
|Title||Conformational states of a soluble, uncleaved HIV-1 envelope trimer|
|Sample||HIV-1 envelope glycoprotein gp140|
|Function / homology|
Function and homology information
positive regulation of plasma membrane raft polarization / positive regulation of establishment of T cell polarity / positive regulation of receptor clustering / actin filament reorganization / host cell endosome membrane / mitigation of host immune response by virus / clathrin-dependent endocytosis of virus by host cell / fusion of virus membrane with host plasma membrane / viral protein processing / fusion of virus membrane with host endosome membrane ...positive regulation of plasma membrane raft polarization / positive regulation of establishment of T cell polarity / positive regulation of receptor clustering / actin filament reorganization / host cell endosome membrane / mitigation of host immune response by virus / clathrin-dependent endocytosis of virus by host cell / fusion of virus membrane with host plasma membrane / viral protein processing / fusion of virus membrane with host endosome membrane / virion attachment to host cell / viral envelope / host cell plasma membrane / virion membrane / structural molecule activity / integral component of membrane / identical protein binding / plasma membrane
Similarity search - Function
Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Envelope glycoprotein GP120 / Gp120 core superfamily / Human immunodeficiency virus 1, envelope glycoprotein Gp120
Similarity search - Domain/homology
Envelope glycoprotein gp160
Similarity search - Component
|Biological species||Human immunodeficiency virus 1|
|Method||single particle reconstruction / cryo EM / Resolution: 21 Å|
|Authors||Liu YH / Pan JH / Cai YF / Grigorieff N / Harrison SC / Chen B|
|Funding support|| United States, 3 items |
|Citation||Journal: J Virol / Year: 2017|
Title: Conformational States of a Soluble, Uncleaved HIV-1 Envelope Trimer.
Authors: Yuhang Liu / Junhua Pan / Yongfei Cai / Nikolaus Grigorieff / Stephen C Harrison / Bing Chen /
Abstract: The HIV-1 envelope spike [Env; trimeric (gp160) cleaved to (gp120/gp41)] induces membrane fusion, leading to viral entry. It is also the viral component targeted by neutralizing antibodies. Vaccine ...The HIV-1 envelope spike [Env; trimeric (gp160) cleaved to (gp120/gp41)] induces membrane fusion, leading to viral entry. It is also the viral component targeted by neutralizing antibodies. Vaccine development requires production, in quantities suitable for clinical studies, of a recombinant form that resembles functional Env. HIV-1 gp140 trimers-the uncleaved ectodomains of (gp160)-from a few selected viral isolates adopt a compact conformation with many antigenic properties of native Env spikes. One is currently being evaluated in a clinical trial. We report here low-resolution (20 Å) electron cryomicroscopy (cryoEM) structures of this gp140 trimer, which adopts two principal conformations, one closed and the other slightly open. The former is indistinguishable at this resolution from those adopted by a stabilized, cleaved trimer (SOSIP) or by a membrane-bound Env trimer with a truncated cytoplasmic tail (EnvΔCT). The latter conformation is closer to a partially open Env trimer than to the fully open conformation induced by CD4. These results show that a stable, uncleaved HIV-1 gp140 trimer has a compact structure close to that of native Env. Development of any HIV vaccine with a protein component (for either priming or boosting) requires production of a recombinant form to mimic the trimeric, functional HIV-1 envelope spike in quantities suitable for clinical studies. Our understanding of the envelope structure has depended in part on a cleaved, soluble trimer, known as SOSIP.664, stabilized by several modifications, including an engineered disulfide. This construct, which is difficult to produce in large quantities, has yet to induce better antibody responses than those to other envelope-based immunogens, even in animal models. The uncleaved ectodomain of the envelope protein, called gp140, has also been made as a soluble form to mimic the native Env present on the virion surface. Most HIV-1 gp140 preparations are not stable, however, and have an inhomogeneous conformation. The results presented here show that gp140 preparations from suitable isolates can adopt a compact, native-like structure, supporting its use as a vaccine candidate.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_8629.map.gz / Format: CCP4 / Size: 22.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 3.96 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire HIV-1 envelope glycoprotein gp140
|Entire||Name: HIV-1 envelope glycoprotein gp140 / Number of Components: 2|
-Component #1: protein, HIV-1 envelope glycoprotein gp140
|Protein||Name: HIV-1 envelope glycoprotein gp140 / Recombinant expression: No|
|Source||Species: Human immunodeficiency virus 1 / Strain: C97ZA012|
|Source (engineered)||Expression System: Homo sapiens (human) / Cell of expression system: HEK 293T|
-Component #2: protein, HIV-1 envelope glycoprotein gp140
|Protein||Name: HIV-1 envelope glycoprotein gp140 / Recombinant expression: No|
|Source||Species: Human immunodeficiency virus 1|
|Source (engineered)||Expression System: Homo sapiens (human)|
|Specimen||Specimen State: Particle / Method: cryo EM|
|Sample solution||pH: 7.5|
|Vitrification||Cryogen Name: ETHANE|
-Electron microscopy imaging
Model: Tecnai Polara / Image courtesy: FEI Company
|Imaging||Microscope: FEI POLARA 300|
|Electron gun||Electron Source: FIELD EMISSION GUN / Accelerating Voltage: 300 kV / Electron Dose: 40 e/Å2 / Illumination Mode: FLOOD BEAM|
|Lens||Cs: 2 mm / Imaging Mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Image acquisition||Number of Digital Images: 3138 / Sampling Size: 5 µm / Details: movies were collected in super resolution mode|
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