|Entry||Database: PDB / ID: 6nb3|
|Title||MERS-CoV complex with human neutralizing LCA60 antibody Fab fragment (state 1)|
|Keywords||VIRUS / coronavirus spike glycoprotein / MERS-CoV / SARS-CoV / human neutralizing antibodies / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID|
|Function / homology||Coronavirus S2 glycoprotein / Spike receptor binding domain / Coronovirus spike glycoprotein, heptad repeat 2 domain / Spike receptor binding domain superfamily / Coronavirus S2 glycoprotein / Spike receptor binding domain / membrane fusion / receptor-mediated virion attachment to host cell / viral envelope / integral component of membrane / Spike glycoprotein|
Function and homology information
|Specimen source||Middle East respiratory syndrome-related coronavirus|
Homo sapiens (human)
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 3.5 Å resolution|
|Authors||Walls, A.C. / Xiong, X. / Park, Y.J. / Tortorici, M.A. / Snijder, S. / Quispe, J. / Cameroni, E. / Gopal, R. / Mian, D. / Lanzavecchia, A. / Zambon, M. / Rey, F.A. / Corti, D. / Veesler, D. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)|
|Citation||Journal: Cell / Year: 2019|
Title: Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.
Authors: Alexandra C Walls / Xiaoli Xiong / Young-Jun Park / M Alejandra Tortorici / Joost Snijder / Joel Quispe / Elisabetta Cameroni / Robin Gopal / Mian Dai / Antonio Lanzavecchia / Maria Zambon / Félix A Rey / Davide Corti / David Veesler
Abstract: Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways ...Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism.
SummaryFull reportAbout validation report
|Date||Deposition: Dec 6, 2018 / Release: Feb 6, 2019|
|Structure viewer||Molecule: |
Downloads & links
A: Spike glycoprotein
L: LCA60 light chain
H: LCA60 heavy chain
D: LCA60 heavy chain
E: LCA60 light chain
B: Spike glycoprotein
C: Spike glycoprotein
-Protein/peptide , 3 types, 7 molecules A
B C L E H D
Mass: 149172.062 Da / Num. of mol.: 3
Source: (gene. exp.) Middle East respiratory syndrome-related coronavirus
Production host: Homo sapiens (human) / References: UniProt: A0A140AYW5
Mass: 11259.390 Da / Num. of mol.: 2 / Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)
Mass: 13920.568 Da / Num. of mol.: 2 / Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)
-Non-polymers , 3 types, 160 molecules
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: single particle reconstruction|
|Component||Name: MERS-CoV complex with human neutralizing LCA60 antibody Fab fragment (state 1)|
Type: COMPLEX / Entity ID: 1,
|Molecular weight||Value: 572 MDa / Experimental value: YES||Source (natural)||Organism: Middle East respiratory syndrome coronavirus||Source (recombinant)||Organism: Homo sapiens (human)||Buffer solution||pH: 8||Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES||Specimen support||Details: unspecified||Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 45 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C3|
|3D reconstruction||Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 54071 / Symmetry type: POINT|
|Atomic model building||Ref protocol: OTHER / Ref space: REAL|
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