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6NB7

SARS-CoV complex with human neutralizing S230 antibody Fab fragment (state 2)

Summary for 6NB7
Entry DOI10.2210/pdb6nb7/pdb
Related6NB3 6NB4 6NB5 6NB6 6NB8
EMDB information0401 0402 0403 0404
DescriptorSpike glycoprotein, S230 heavy chain, S230 light chain, ... (9 entities in total)
Functional Keywordscoronavirus spike glycoprotein, mers-cov, sars-cov, human neutralizing antibodies, structural genomics, seattle structural genomics center for infectious disease, ssgcid, virus
Biological sourceSARS coronavirus (SARS-CoV)
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Total number of polymer chains9
Total formula weight526244.38
Authors
Primary citationWalls, A.C.,Xiong, X.,Park, Y.J.,Tortorici, M.A.,Snijder, J.,Quispe, J.,Cameroni, E.,Gopal, R.,Dai, M.,Lanzavecchia, A.,Zambon, M.,Rey, F.A.,Corti, D.,Veesler, D.
Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.
Cell, 176:1026-1039.e15, 2019
Cited by
PubMed 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 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.
PubMed: 30712865
DOI: 10.1016/j.cell.2018.12.028
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.5 Å)
Structure validation

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