|Entry||Database: EMDB / ID: EMD-5413|
|Title||CryoEM map of the mature astrovirus (HAstV-1)|
|Sample||mature human astrovirus HAstV-1:|
|Biological species||Human astrovirus|
|Method||single particle reconstruction / cryo EM / Resolution: 25 Å|
|Authors||Dryden KA / Tihova M / Nowotny N / Matsui SM / Mendez E / Yeager M|
|Citation||Journal: J Mol Biol / Year: 2012|
Title: Immature and mature human astrovirus: structure, conformational changes, and similarities to hepatitis E virus.
Authors: Kelly A Dryden / Mariana Tihova / Norbert Nowotny / Suzanne M Matsui / Ernesto Mendez / Mark Yeager /
Abstract: Human astroviruses (HAstVs) are a major cause of gastroenteritis. HAstV assembles from the structural protein VP90 and undergoes a cascade of proteolytic cleavages. Cleavage to VP70 is required for ...Human astroviruses (HAstVs) are a major cause of gastroenteritis. HAstV assembles from the structural protein VP90 and undergoes a cascade of proteolytic cleavages. Cleavage to VP70 is required for release of immature particles from cells, and subsequent cleavage by trypsin confers infectivity. We used electron cryomicroscopy and icosahedral image analysis to determine the first experimentally derived, three-dimensional structures of an immature VP70 virion and a fully proteolyzed, infectious virion. Both particles display T=3 icosahedral symmetry and nearly identical solid capsid shells with diameters of ~350Å. Globular spikes emanate from the capsid surface, yielding an overall diameter of ~440Å. While the immature particles display 90 dimeric spikes, the mature capsid only displays 30 spikes, located on the icosahedral 2-fold axes. Loss of the 60 peripentonal spikes likely plays an important role in viral infectivity. In addition, immature HAstV bears a striking resemblance to the structure of hepatitis E virus (HEV)-like particles, as previously predicted from structural similarity of the crystal structure of the astrovirus spike domain with the HEV P-domain [Dong, J., Dong, L., Méndez, E. & Tao, Y. (2011). Crystal structure of the human astrovirus capsid spike. Proc. Natl. Acad. Sci. USA108, 12681-12686]. Similarities between their capsid shells and dimeric spikes and between the sequences of their capsid proteins suggest that these viral families are phylogenetically related and may share common assembly and activation mechanisms.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_5413.map.gz / Format: CCP4 / Size: 58.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 2 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire mature human astrovirus HAstV-1
|Entire||Name: mature human astrovirus HAstV-1 / Number of components: 1|
-Component #1: virus, Human astrovirus
|Virus||Name: Human astrovirus / Class: VIRION / Empty: No / Enveloped: No / Isolate: STRAIN|
|Species||Species: Human astrovirus|
|Source (natural)||Host Species: Homo sapiens (human) / Host category: VERTEBRATES|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||Buffer solution: 50mM Tris-HCl, pH 8, 100mM NaCl, 10mM MgCl2, 10mM CaCl2|
|Support film||holey carbon, glow discharged with amylamine|
|Vitrification||Instrument: HOMEMADE PLUNGER / Cryogen name: ETHANE / Method: watch drop spread on filter paper before plunging|
-Electron microscopy imaging
|Imaging||Microscope: FEI/PHILIPS CM120T / Date: Sep 22, 1997|
|Electron gun||Electron source: LAB6 / Accelerating voltage: 120 kV / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 35000 X (nominal) / Imaging mode: BRIGHT FIELD / Defocus: 1450 - 1850 nm|
|Specimen Holder||Model: GATAN LIQUID NITROGEN|
|Camera||Detector: KODAK SO-163 FILM|
|Image acquisition||Number of digital images: 6 / Scanner: ZEISS SCAI / Sampling size: 7 µm|
|Processing||Method: single particle reconstruction|
Details: Particles were selected with X3D, and processed with Auto3dem.
Number of projections: 397 / Applied symmetry: I (icosahedral)
|3D reconstruction||Algorithm: polar Fourier transform / Software: Auto3dem / Resolution: 25 Å / Resolution method: FSC 0.5|
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