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Enterovirus 71 (EV71)-neutralizing antibodies correlate with protection and have potential as therapeutic agents. We isolate and characterize a panel of plasmablast-derived monoclonal antibodies from an infected child whose antibody response focuses on the plateau epitope near the icosahedral 3-fold axes. Eight of a total of 19 antibodies target this epitope and three of these potently neutralize the virus. Representative neutralizing antibodies 38-1-10A and 38-3-11A both confer effective protection against lethal EV71 challenge in hSCARB2-transgenic mice. The cryo-electron microscopy structures of the EV71 virion in complex with Fab fragments of these potent and protective antibodies reveal the details of a conserved epitope formed by residues in the BC and HI loops of VP2 and the BC and HI loops of VP3 spanning the region around the 3-fold axis. Remarkably, the two antibodies interact with the epitope in quite distinct ways. These plateau-binding antibodies provide templates for promising candidate therapeutics.
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10.1038/s41467-020-19013-3
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document_parses/pdf_json/f9862bccf9466f5fdef936038966a227a38fa4d6.json; document_parses/pdf_json/726ad2b52d872fa4641ff344557c4d147aad2413.json
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document_parses/pmc_json/PMC7567869.xml.json
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Structural and functional analysis of protective antibodies targeting the threefold plateau of enterovirus 71
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