|Entry||Database: EMDB / ID: EMD-21498|
|Title||BG505 SOSIP.664 in complex with rabbit Fab 43A2|
|Sample||BG505 SOSIP.664 in complex with rabbit Fab 43A2|
|Biological species||Human immunodeficiency virus 1|
|Method||single particle reconstruction / Resolution: 25 Å|
|Authors||Cottrell CA / Shin M / Ward AB|
|Funding support|| United States, 3 items |
|Citation||Journal: Sci Adv / Year: 2020|
Title: HIV envelope trimer-elicited autologous neutralizing antibodies bind a region overlapping the N332 glycan supersite.
Authors: Bartek Nogal / Laura E McCoy / Marit J van Gils / Christopher A Cottrell / James E Voss / Raiees Andrabi / Matthias Pauthner / Chi-Hui Liang / Terrence Messmer / Rebecca Nedellec / Mia Shin ...Authors: Bartek Nogal / Laura E McCoy / Marit J van Gils / Christopher A Cottrell / James E Voss / Raiees Andrabi / Matthias Pauthner / Chi-Hui Liang / Terrence Messmer / Rebecca Nedellec / Mia Shin / Hannah L Turner / Gabriel Ozorowski / Rogier W Sanders / Dennis R Burton / Andrew B Ward /
Abstract: To date, immunization studies of rabbits with the BG505 SOSIP.664 HIV envelope glycoprotein trimers have revealed the 241/289 glycan hole as the dominant neutralizing antibody epitope. Here, we ...To date, immunization studies of rabbits with the BG505 SOSIP.664 HIV envelope glycoprotein trimers have revealed the 241/289 glycan hole as the dominant neutralizing antibody epitope. Here, we isolated monoclonal antibodies from a rabbit that did not exhibit glycan hole-dependent autologous serum neutralization. The antibodies did not compete with a previously isolated glycan hole-specific antibody but did compete with N332 glycan supersite broadly neutralizing antibodies. A 3.5-Å cryoEM structure of one of the antibodies in complex with the BG505 SOSIP.v5.2 trimer demonstrated that while the epitope recognized overlapped the N332 glycan supersite by contacting the GDIR motif at the base of V3, primary contacts were located in the variable V1 loop. These data suggest that strain-specific responses to V1 may interfere with broadly neutralizing responses to the N332 glycan supersite and vaccine immunogens may require engineering to minimize these off-target responses or steer them toward a more desirable pathway.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_21498.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.98 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire BG505 SOSIP.664 in complex with rabbit Fab 43A2
|Entire||Name: BG505 SOSIP.664 in complex with rabbit Fab 43A2 / Number of components: 1|
-Component #1: protein, BG505 SOSIP.664 in complex with rabbit Fab 43A2
|Protein||Name: BG505 SOSIP.664 in complex with rabbit Fab 43A2 / Recombinant expression: No|
|Source||Species: Human immunodeficiency virus 1|
|Source (engineered)||Expression System: Homo sapiens (human) / Cell of expression system: HEK293F|
|Specimen||Specimen state: Particle|
|Sample solution||pH: 7.4|
|Vitrification||Cryogen name: NONE|
-Electron microscopy imaging
Model: Talos Arctica / Image courtesy: FEI Company
|Imaging||Microscope: FEI TALOS ARCTICA|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 25 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: FEI CETA (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C3 (3 fold cyclic) / Number of projections: 2878|
|3D reconstruction||Software: RELION / Resolution: 25 Å / Resolution method: FSC 0.143 CUT-OFF|
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