|Entry||Database: EMDB / ID: EMD-5794|
|Title||A common solution to group 2 influenza virus neutralization|
|Sample||Influenza (A/Bangkok/1/1979, H3N2) hemagglutinin bound to neutralizing antibody CR8043|
|Keywords||Antibody recognition / Hemagglutinin|
|Biological species||Homo sapiens (human) / Influenza A virus|
|Method||single particle reconstruction / negative staining / Resolution: 23 Å|
|Authors||Friesen RHE / Leeb PS / Stoop EJM / Hoffman RMB / Ekiert DC / Bhabha G / Yu W / Juraszek J / Koudstaal W / Jongeneelen M / Korse HJWM / Ophorst C / Brinkman-van der Linden ECM / Throsby M / Kwakkenbos MJ / Bakkerd AQ / Beaumont Y / Spits H / Kwaks T / Vogels R / Ward AB / Goudsmit J / Wilson IA|
|Citation||Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2014|
Title: A common solution to group 2 influenza virus neutralization.
Authors: Robert H E Friesen / Peter S Lee / Esther J M Stoop / Ryan M B Hoffman / Damian C Ekiert / Gira Bhabha / Wenli Yu / Jarek Juraszek / Wouter Koudstaal / Mandy Jongeneelen / Hans J W M Korse / Carla Ophorst / Els C M Brinkman-van der Linden / Mark Throsby / Mark J Kwakkenbos / Arjen Q Bakker / Tim Beaumont / Hergen Spits / Ted Kwaks / Ronald Vogels / Andrew B Ward / Jaap Goudsmit / Ian A Wilson /
Abstract: The discovery and characterization of broadly neutralizing antibodies (bnAbs) against influenza viruses have raised hopes for the development of monoclonal antibody (mAb)-based immunotherapy and the ...The discovery and characterization of broadly neutralizing antibodies (bnAbs) against influenza viruses have raised hopes for the development of monoclonal antibody (mAb)-based immunotherapy and the design of universal influenza vaccines. Only one human bnAb (CR8020) specifically recognizing group 2 influenza A viruses has been previously characterized that binds to a highly conserved epitope at the base of the hemagglutinin (HA) stem and has neutralizing activity against H3, H7, and H10 viruses. Here, we report a second group 2 bnAb, CR8043, which was derived from a different germ-line gene encoding a highly divergent amino acid sequence. CR8043 has in vitro neutralizing activity against H3 and H10 viruses and protects mice against challenge with a lethal dose of H3N2 and H7N7 viruses. The crystal structure and EM reconstructions of the CR8043-H3 HA complex revealed that CR8043 binds to a site similar to the CR8020 epitope but uses an alternative angle of approach and a distinct set of interactions. The identification of another antibody against the group 2 stem epitope suggests that this conserved site of vulnerability has great potential for design of therapeutics and vaccines.
|Date||Deposition: Nov 14, 2013 / Header (metadata) release: Dec 11, 2013 / Map release: Dec 11, 2013 / Update: Feb 17, 2016|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_5794.map.gz / Format: CCP4 / Size: 26.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 2.05 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Influenza (A/Bangkok/1/1979, H3N2) hemagglutinin bound to neutral...
|Entire||Name: Influenza (A/Bangkok/1/1979, H3N2) hemagglutinin bound to neutralizing antibody CR8043|
Number of components: 2 / Oligomeric State: One HA trimer bound to three Fabs
|Mass||Theoretical: 288 kDa|
-Component #1: protein, CR8043 Fab
|Protein||Name: CR8043 Fab / Oligomeric Details: Monomer / Number of Copies: 3 / Recombinant expression: Yes|
|Mass||Theoretical: 44 kDa|
|Source||Species: Homo sapiens (human)|
|Source (engineered)||Expression System: unidentified baculovirus|
-Component #2: protein, Influenza A/Bangkok/1/1979 (H3N2) hemagglutinin
|Protein||Name: Influenza A/Bangkok/1/1979 (H3N2) hemagglutinin / Oligomeric Details: trimer / Recombinant expression: Yes / Number of Copies: 1|
|Mass||Theoretical: 157 kDa|
|Source||Species: Influenza A virus / Strain: A/Hong Kong/1/1968|
|Source (engineered)||Expression System: unidentified baculovirus|
|Specimen||Specimen state: Particle / Method: negative staining|
|Sample solution||Specimen conc.: 0.01 mg/mL / Buffer solution: TBS / pH: 7.4|
|Support film||400 mesh copper with nitrocellulose and thin layer of carbon|
|Staining||Samples were applied to freshly glow-discharged grids and stained with 2% uranyl formate (20s seconds).|
|Vitrification||Cryogen name: NONE|
-Electron microscopy imaging
|Imaging||Microscope: FEI TECNAI 12 / Date: Mar 26, 2013|
|Electron gun||Electron source: LAB6 / Accelerating voltage: 120 kV / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 52000 X (calibrated)|
Astigmatism: Objective lens astigmatism corrected at 100,000 times magnification.
Imaging mode: BRIGHT FIELD / Defocus: 1000 nm
|Specimen Holder||Model: SIDE ENTRY, EUCENTRIC / Tilt Angle: 0 - 55 ° / Temperature: 293|
|Camera||Detector: TVIPS TEMCAM-F416 (4k x 4k)|
|Image acquisition||Number of digital images: 206|
|Processing||Method: single particle reconstruction / Applied symmetry: C3 (3 fold cyclic) / Number of projections: 7009 |
Details: Projection matching seeded with a low-pass filtered hemagglutinin
|3D reconstruction||Algorithm: Projection matching / Software: Appion, Spider, Xmipp, Eman1, Sparx / Resolution: 23 Å / Resolution method: FSC 0.5, semi-independent|
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