Abstract：
:The rapid spread of Zika virus (ZIKV), which causes microcephaly and Guillain-Barré syndrome, signals an urgency to identify therapeutics. Recent efforts to rescreen dengue virus human antibodies for ZIKV cross-neutralization activity showed antibody C10 as one of the most potent. To investigate the ability of the antibody to block fusion, we determined the cryoEM structures of the C10-ZIKV complex at pH levels mimicking the extracellular (pH8.0), early (pH6.5) and late endosomal (pH5.0) environments. The 4.0 Å resolution pH8.0 complex structure shows that the antibody binds to E proteins residues at the intra-dimer interface, and the virus quaternary structure-dependent inter-dimer and inter-raft interfaces. At pH6.5, antibody C10 locks all virus surface E proteins, and at pH5.0, it locks the E protein raft structure, suggesting that it prevents the structural rearrangement of the E proteins during the fusion event-a vital step for infection. This suggests antibody C10 could be a good therapeutic candidate.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Zhang S,Kostyuchenko VA,Ng TS,Lim XN,Ooi JSG,Lambert S,Tan TY,Widman DG,Shi J,Baric RS,Lok SMdoi
10.1038/ncomms13679subject
Has Abstractpub_date
2016-11-24 00:00:00pages
13679issn
2041-1723pii
ncomms13679journal_volume
7pub_type
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