6Z3P
Structure of EV71 in complex with a protective antibody 38-3-11A Fab
Summary for 6Z3P
Entry DOI | 10.2210/pdb6z3p/pdb |
EMDB information | 11061 |
Descriptor | VP1, VP2, VP3, ... (7 entities in total) |
Functional Keywords | ev71, antibody 38-3-11a, antibody 38-1-10a, ev71-fab complex, virus |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 6 |
Total formula weight | 145250.55 |
Authors | Zhou, D.,Fry, E.E.,Ren, J.,Stuart, D.I. (deposition date: 2020-05-21, release date: 2020-09-02, Last modification date: 2024-10-23) |
Primary citation | Huang, K.A.,Zhou, D.,Fry, E.E.,Kotecha, A.,Huang, P.N.,Yang, S.L.,Tsao, K.C.,Huang, Y.C.,Lin, T.Y.,Ren, J.,Stuart, D.I. Structural and functional analysis of protective antibodies targeting the threefold plateau of enterovirus 71. Nat Commun, 11:5253-5253, 2020 Cited by PubMed 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. PubMed: 33067459DOI: 10.1038/s41467-020-19013-3 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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