Synthesis and processing of ENV and VPU / evasion of host immune response / Alpha-defensins / Dectin-2 family / Binding and entry of HIV virion / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / actin filament organization ...Synthesis and processing of ENV and VPU / evasion of host immune response / Alpha-defensins / Dectin-2 family / Binding and entry of HIV virion / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / actin filament organization / Assembly Of The HIV Virion / Budding and maturation of HIV virion / clathrin-dependent endocytosis of virus by host cell / viral protein processing / symbiont entry into host cell / fusion of virus membrane with host plasma membrane / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / apoptotic process / host cell plasma membrane / structural molecule activity / virion membrane / membrane Similarity search - Function
Journal: Nature / Year: 2008 Title: Molecular architecture of native HIV-1 gp120 trimers. Authors: Jun Liu / Alberto Bartesaghi / Mario J Borgnia / Guillermo Sapiro / Sriram Subramaniam / Abstract: The envelope glycoproteins (Env) of human and simian immunodeficiency viruses (HIV and SIV, respectively) mediate virus binding to the cell surface receptor CD4 on target cells to initiate infection. ...The envelope glycoproteins (Env) of human and simian immunodeficiency viruses (HIV and SIV, respectively) mediate virus binding to the cell surface receptor CD4 on target cells to initiate infection. Env is a heterodimer of a transmembrane glycoprotein (gp41) and a surface glycoprotein (gp120), and forms trimers on the surface of the viral membrane. Using cryo-electron tomography combined with three-dimensional image classification and averaging, we report the three-dimensional structures of trimeric Env displayed on native HIV-1 in the unliganded state, in complex with the broadly neutralizing antibody b12 and in a ternary complex with CD4 and the 17b antibody. By fitting the known crystal structures of the monomeric gp120 core in the b12- and CD4/17b-bound conformations into the density maps derived by electron tomography, we derive molecular models for the native HIV-1 gp120 trimer in unliganded and CD4-bound states. We demonstrate that CD4 binding results in a major reorganization of the Env trimer, causing an outward rotation and displacement of each gp120 monomer. This appears to be coupled with a rearrangement of the gp41 region along the central axis of the trimer, leading to closer contact between the viral and target cell membranes. Our findings elucidate the structure and conformational changes of trimeric HIV-1 gp120 relevant to antibody neutralization and attachment to target cells.
History
Deposition
Jun 29, 2008
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Header (metadata) release
Jul 3, 2008
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Map release
May 5, 2009
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Update
Aug 2, 2011
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Current status
Aug 2, 2011
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Download / File: emd_5021.map.gz / Format: CCP4 / Size: 3.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation
b12-bound HIV-1 BaL membrane
Voxel size
X=Y=Z: 4.1 Å
Density
Contour Level
By AUTHOR: 0.0432 / Movie #1: 0.06
Minimum - Maximum
-0.671275 - 0.648455
Average (Standard dev.)
-0.000154365 (±0.0434309)
Symmetry
Space group: 1
Details
EMDB XML:
Map geometry
Axis order
X
Y
Z
Origin
0
0
0
Dimensions
100
100
100
Spacing
100
100
100
Cell
A=B=C: 410 Å α=β=γ: 90 °
CCP4 map header:
mode
Image stored as Reals
Å/pix. X/Y/Z
4.1
4.1
4.1
M x/y/z
100
100
100
origin x/y/z
0.000
0.000
0.000
length x/y/z
410.000
410.000
410.000
α/β/γ
90.000
90.000
90.000
start NX/NY/NZ
-127
-127
-127
NX/NY/NZ
255
255
255
MAP C/R/S
1
2
3
start NC/NR/NS
0
0
0
NC/NR/NS
100
100
100
D min/max/mean
-0.671
0.648
-0.000
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Supplemental data
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Sample components
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Entire : HIV-1 BaL virus
Entire
Name: HIV-1 BaL virus
Components
Sample: HIV-1 BaL virus
Virus: envelope glycoprotein (unknown)
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Supramolecule #1000: HIV-1 BaL virus
Supramolecule
Name: HIV-1 BaL virus / type: sample / ID: 1000 Details: Structures determined by cryo-electron tomography combined with 3D averaging Number unique components: 1
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