Structural and functional analysis of protective antibodies targeting the threefold plateau of enterovirus 71

Kuan-Ying A. Huang (), Daming Zhou, Elizabeth E. Fry, Abhay Kotecha, Peng-Nien Huang, Shu-Li Yang, Kuo-Chien Tsao, Yhu-Chering Huang, Tzou-Yien Lin, Jingshan Ren and David I. Stuart ()
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Kuan-Ying A. Huang: Chang Gung Memorial Hospital
Daming Zhou: University of Oxford
Elizabeth E. Fry: University of Oxford
Abhay Kotecha: University of Oxford
Peng-Nien Huang: Chang Gung University
Shu-Li Yang: Chang Gung University
Kuo-Chien Tsao: Chang Gung University
Yhu-Chering Huang: Chang Gung Memorial Hospital
Tzou-Yien Lin: Chang Gung Memorial Hospital
Jingshan Ren: University of Oxford
David I. Stuart: University of Oxford

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: Abstract 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.

Date: 2020
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DOI: 10.1038/s41467-020-19013-3

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