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Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
Walls, A
Xiong, X
Park, Y
Tortorici, M
Snijder, J
Quispe, J
Cameroni, E
Gopal, R
Dai, M
Lanzavecchia, A
Zambon, M
Rey, F
Corti, D
Veesler, D
Acceso Abierto
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 intohost 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.
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