|Entry||Database: EMDB / ID: 2886|
|Title||Cryo-Molecular electron tomography of PfEMP1-IT4Var60)|
|Map data||Subtomogram average of 10 PfEMP1s|
|Sample||ectodomain of PfEMP1-IT4Var60|
|Keywords||Malaria / Rosetting / PfEMP1|
|Source||Plasmodium falciparum (malaria parasite P. falciparum)|
|Method||subtomogram averaging / cryo EM / 20 Å resolution|
|Authors||Akhouri RR / Goel S / Furusho H / Skoglund U / Wahlgren M|
|Citation||Journal: Cell Rep / Year: 2016|
Title: Architecture of Human IgM in Complex with P. falciparum Erythrocyte Membrane Protein 1.
Authors: Reetesh Raj Akhouri / Suchi Goel / Hirotoshi Furusho / Ulf Skoglund / Mats Wahlgren
Abstract: Plasmodium falciparum virulence is associated with sequestration of infected erythrocytes. Microvascular binding mediated by PfEMP1 in complex with non-immune immunoglobulin M (IgM) is common among ...Plasmodium falciparum virulence is associated with sequestration of infected erythrocytes. Microvascular binding mediated by PfEMP1 in complex with non-immune immunoglobulin M (IgM) is common among parasites that cause both severe childhood malaria and pregnancy-associated malaria. Here, we present cryo-molecular electron tomography structures of human IgM, PfEMP1 and their complex. Three-dimensional reconstructions of IgM reveal that it has a dome-like core, randomly oriented Fab2s units, and the overall shape of a turtle. PfEMP1 is a C- shaped molecule with a flexible N terminus followed by an arc-shaped backbone and a bulky C terminus that interacts with IgM. Our data demonstrate that the PfEMP1 binding pockets on IgM overlap with those of C1q, and the bulkiness of PfEMP1 limits the capacity of IgM to interact with PfEMP1. We suggest that P. falciparum exploits IgM to cluster PfEMP1 into an organized matrix to augment its affinity to host cell receptors.
|Date||Deposition: Feb 8, 2015 / Header (metadata) release: Feb 25, 2015 / Map release: Jan 13, 2016 / Last update: Feb 17, 2016|
|Structure viewer||EM map: |
Downloads & links
|File||emd_2886.map.gz (map file in CCP4 format, 461 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 4.534 Å|
CCP4 map header:
-Entire ectodomain of PfEMP1-IT4Var60
|Entire||Name: ectodomain of PfEMP1-IT4Var60 / Details: the sample was monodisperse. / Number of components: 1 / Oligomeric State: Monomer|
|Mass||Theoretical: 280 kDa / Experimental: 320 kDa|
-Component #1: protein, PfEMP1
|Protein||Name: PfEMP1Plasmodium falciparum erythrocyte membrane protein 1|
Oligomeric Details: monomer / Recombinant expression: Yes / Number of Copies: 1
|Mass||Theoretical: 280 kDa / Experimental: 320 kDa|
|Source||Species: Plasmodium falciparum (malaria parasite P. falciparum)|
|Source (engineered)||Expression System: Drosophila melanogaster (fruit fly) / Vector: pMTBipV5HisA / Strain: S2 cells|
|Source (natural)||Location in cell: Infected erythrocyte membrane|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Specimen conc.: 2 mg/ml / Buffer solution: 20mM Hepes, 200mM NaCl / pH: 7.5|
|Support film||C-Flat (Copper grid with thin Carbon support)|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 78 K / Humidity: 100 % / Method: Blot for 4 seconds before plunging|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS / Date: Oct 25, 2013|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 40 e/Å2 / Illumination mode: OTHER|
|Lens||Magnification: 37000 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 0.7 - 1.5 nm / Energy filter: FEI|
|Specimen Holder||Holder: LN2 cooled / Model: FEI TITAN KRIOS AUTOGRID HOLDER / Tilt Angle: -70 - 70 deg. / Temperature: K ( 78 - 100 K)|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Image acquisition||Number of digital images: 281|
|Processing||Method: subtomogram averaging / Number of subtomograms: 10 / Applied symmetry: C1 (asymmetric)|
|3D reconstruction||Software: COMET / CTF correction: each frame / Resolution: 20 Å|
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