3J2X: Electron Cryo-microscopy Of Chikungunya Vlp In Complex With Neutralizing Antibody Fab M242

Citation:
Abstract
A 5.3 A resolution, cryo-electron microscopy (cryoEM) map of Chikungunya virus-like particles (VLPs) has been interpreted using the previously published crystal structure of the Chikungunya E1-E2 glycoprotein heterodimer. The heterodimer structure was divided into domains to obtain a good fit to the cryoEM density. Differences in the T = 4 quasi-equivalent heterodimer components show their adaptation to different environments. The spikes on the icosahedral 3-fold axes and those in general positions are significantly different, possibly representing different phases during initial generation of fusogenic E1 trimers. CryoEM maps of neutralizing Fab fragments complexed with VLPs have been interpreted using the crystal structures of the Fab fragments and the VLP structure. Based on these analyses the CHK-152 antibody was shown to stabilize the viral surface, hindering the exposure of the fusion-loop, likely neutralizing infection by blocking fusion. The CHK-9, m10 and m242 antibodies surround the receptor-attachment site, probably inhibiting infection by blocking cell attachment. DOI:http://dx.doi.org/10.7554/eLife.00435.001.
PDB ID: 3J2XDownload
MMDB ID: 109304
PDB Deposition Date: 2013/1/28
Updated in MMDB: 2013/04
Experimental Method:
electron microscopy
Resolution: 15.6  Å
Source Organism:
Similar Structures:
Biological Unit for 3J2X: 480-meric
Molecular Components in 3J2X
Label Count Molecule
Proteins (480 molecules)
240
M242 Light Chain
Molecule annotation
240
M242 Heavy Chain
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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