Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms13679
Title: Neutralization mechanism of a highly potent antibody against Zika virus
Authors: Zhang, S 
Kostyuchenko, V.A 
Ng, T.-S 
Lim, X.-N 
Ooi, J.S.G 
Lambert, S 
Tan, T.Y 
Widman, D.G
Shi, J 
Baric, R.S
Lok, S.-M 
Keywords: epitope
neutralizing antibody
virus envelope protein
neutralizing antibody
virus antibody
antibody
gene expression
neutralization
protein
virus
antigen binding
Article
controlled study
cryoelectron microscopy
endosome
extracellular space
nonhuman
pH
protein structure
virus neutralization
virus particle
Zika virus
cross reaction
Dengue virus
immunology
ultrastructure
Zika virus
Zika virus
Antibodies, Neutralizing
Antibodies, Viral
Cross Reactions
Cryoelectron Microscopy
Dengue Virus
Hydrogen-Ion Concentration
Viral Envelope Proteins
Zika Virus
Issue Date: 2016
Publisher: Nature Publishing Group
Citation: Zhang, S, Kostyuchenko, V.A, Ng, T.-S, Lim, X.-N, Ooi, J.S.G, Lambert, S, Tan, T.Y, Widman, D.G, Shi, J, Baric, R.S, Lok, S.-M (2016). Neutralization mechanism of a highly potent antibody against Zika virus. Nature Communications 7 : 13679. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms13679
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. © The Author(s) 2016.
Source Title: Nature Communications
URI: https://scholarbank.nus.edu.sg/handle/10635/174914
ISSN: 20411723
DOI: 10.1038/ncomms13679
Appears in Collections:Elements
Staff Publications

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1038_ncomms13679.pdf2.17 MBAdobe PDF

OPEN

NoneView/Download

SCOPUSTM   
Citations

58
checked on Apr 7, 2021

Page view(s)

52
checked on Apr 9, 2021

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.