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- EMDB-25025: Cryo-EM map for HIV-1 Env bound with two 4E10 Fabs -

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Basic information

Entry
Database: EMDB / ID: EMD-25025
TitleCryo-EM map for HIV-1 Env bound with two 4E10 Fabs
Map dataCryo-EM map for HIV-1 Env bound with two 4E10 Fabs
Sample
  • Complex: HIV-1 gp145 bound with three 4E10 Fabs
Biological speciesHIV whole-genome vector AA1305#18 (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 8.24 Å
AuthorsYang S / Walz T
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: Nat Commun / Year: 2022
Title: Dynamic HIV-1 spike motion creates vulnerability for its membrane-bound tripod to antibody attack.
Authors: Shuang Yang / Giorgos Hiotis / Yi Wang / Junjian Chen / Jia-Huai Wang / Mikyung Kim / Ellis L Reinherz / Thomas Walz /
Abstract: Vaccines targeting HIV-1's gp160 spike protein are stymied by high viral mutation rates and structural chicanery. gp160's membrane-proximal external region (MPER) is the target of naturally arising ...Vaccines targeting HIV-1's gp160 spike protein are stymied by high viral mutation rates and structural chicanery. gp160's membrane-proximal external region (MPER) is the target of naturally arising broadly neutralizing antibodies (bnAbs), yet MPER-based vaccines fail to generate bnAbs. Here, nanodisc-embedded spike protein was investigated by cryo-electron microscopy and molecular-dynamics simulations, revealing spontaneous ectodomain tilting that creates vulnerability for HIV-1. While each MPER protomer radiates centrally towards the three-fold axis contributing to a membrane-associated tripod structure that is occluded in the upright spike, tilting provides access to the opposing MPER. Structures of spike proteins with bound 4E10 bnAb Fabs reveal that the antibody binds exposed MPER, thereby altering MPER dynamics, modifying average ectodomain tilt, and imposing strain on the viral membrane and the spike's transmembrane segments, resulting in the abrogation of membrane fusion and informing future vaccine development.
History
DepositionSep 27, 2021-
Header (metadata) releaseNov 9, 2022-
Map releaseNov 9, 2022-
UpdateFeb 22, 2023-
Current statusFeb 22, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_25025.png

Downloads & links

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Map

FileDownload / File: emd_25025.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-EM map for HIV-1 Env bound with two 4E10 Fabs
Voxel sizeX=Y=Z: 1.03 Å
Density
Contour LevelBy AUTHOR: 0.003
Minimum - Maximum-0.0055883983 - 0.024128001
Average (Standard dev.)0.0006910505 (±0.0018019439)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 263.68 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : HIV-1 gp145 bound with three 4E10 Fabs

EntireName: HIV-1 gp145 bound with three 4E10 Fabs
Components
  • Complex: HIV-1 gp145 bound with three 4E10 Fabs

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Supramolecule #1: HIV-1 gp145 bound with three 4E10 Fabs

SupramoleculeName: HIV-1 gp145 bound with three 4E10 Fabs / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: HIV whole-genome vector AA1305#18 (others) / Strain: BG505

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Support film - Material: GRAPHENE OXIDE / Support film - topology: CONTINUOUS
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 80.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 8.24 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 21454

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