|Entry||Database: EMDB / ID: 8884|
|Title||RCT reconstruction of HCMV Pentamer with receptor and 3G16 Fab fragment.|
|Map data||RCT reconstruction of CMV Pentamer bound to Receptor and 3G16 Fab fragment.|
|Sample||HCMV Pentamer with receptor and 3G16 Fab fragment bound.:|
|Source||Human cytomegalovirus (Human cytomegalovirus)|
|Method||single particle reconstruction / 25 Å resolution|
|Authors||Ciferri C / Arthur CP / Dosey AM|
|Citation||Journal: Cell / Year: 2018|
Title: An Unbiased Screen for Human Cytomegalovirus Identifies Neuropilin-2 as a Central Viral Receptor.
Authors: Nadia Martinez-Martin / Jessica Marcandalli / Christine S Huang / Christopher P Arthur / Michela Perotti / Mathilde Foglierini / Hoangdung Ho / Annie M Dosey / Stephanie Shriver / Jian Payandeh / Alexander Leitner / Antonio Lanzavecchia / Laurent Perez / Claudio Ciferri
Abstract: Characterizing cell surface receptors mediating viral infection is critical for understanding viral tropism and developing antiviral therapies. Nevertheless, due to challenges associated with ...Characterizing cell surface receptors mediating viral infection is critical for understanding viral tropism and developing antiviral therapies. Nevertheless, due to challenges associated with detecting protein interactions on the cell surface, the host receptors of many human pathogens remain unknown. Here, we build a library consisting of most single transmembrane human receptors and implement a workflow for unbiased and high-sensitivity detection of receptor-ligand interactions. We apply this technology to elucidate the long-sought receptor of human cytomegalovirus (HCMV), the leading viral cause of congenital birth defects. We identify neuropilin-2 (Nrp2) as the receptor for HCMV-pentamer infection in epithelial/endothelial cells and uncover additional HCMV interactors. Using a combination of biochemistry, cell-based assays, and electron microscopy, we characterize the pentamer-Nrp2 interaction and determine the architecture of the pentamer-Nrp2 complex. This work represents an important approach to the study of host-pathogen interactions and provides a framework for understanding HCMV infection, neutralization, and the development of novel anti-HCMV therapies.
|Date||Deposition: Aug 9, 2017 / Header (metadata) release: Oct 25, 2017 / Map release: Nov 28, 2018 / Last update: Nov 28, 2018|
|Structure viewer||EM map: |
Downloads & links
|File||emd_8884.map.gz (map file in CCP4 format, 5325 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 5.4 Å|
CCP4 map header:
-Entire HCMV Pentamer with receptor and 3G16 Fab fragment bound.
|Entire||Name: HCMV Pentamer with receptor and 3G16 Fab fragment bound.|
Number of components: 1
-Component #1: protein, HCMV Pentamer with receptor and 3G16 Fab fragment bound.
|Protein||Name: HCMV Pentamer with receptor and 3G16 Fab fragment bound.|
Recombinant expression: No
|Source||Species: Human cytomegalovirus (Human cytomegalovirus)|
|Source (engineered)||Expression System: Homo sapiens (human) / Cell of expression system: Hek293|
|Specimen||Specimen state: particle|
|Sample solution||pH: 7.5|
|Vitrification||Cryogen name: NONE|
-Electron microscopy imaging
Model: Tecnai Spirit / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI SPIRIT|
|Electron gun||Electron source: LAB6 / Accelerating voltage: 120 kV / Electron dose: 3 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN ULTRASCAN 1000 (2k x 2k)|
|Processing||Method: single particle reconstruction / Number of projections: 570|
|3D reconstruction||Resolution: 25 Å / Resolution method: OTHER|
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