| Literature DB >> 27158114 |
Lianpan Dai1, Jian Song2, Xishan Lu3, Yong-Qiang Deng4, Abednego Moki Musyoki2, Huijun Cheng1, Yanfang Zhang3, Yuan Yuan2, Hao Song2, Joel Haywood2, Haixia Xiao3, Jinghua Yan5, Yi Shi6, Cheng-Feng Qin7, Jianxun Qi8, George F Gao9.
Abstract
Zika virus (ZIKV), a mosquito-borne flavivirus, is a current global public health concern. The flavivirus envelope (E) glycoprotein is responsible for virus entry and represents a major target of neutralizing antibodies for other flaviviruses. Here, we report the structures of ZIKV E protein at 2.0 Å and in complex with a flavivirus broadly neutralizing murine antibody 2A10G6 at 3.0 Å. ZIKV-E resembles all the known flavivirus E structures but contains a unique, positively charged patch adjacent to the fusion loop region of the juxtaposed monomer, which may influence host attachment. The ZIKV-E-2A10G6 complex structure reveals antibody recognition of a highly conserved fusion loop. 2A10G6 binds to ZIKV-E with high affinity in vitro and neutralizes currently circulating ZIKV strains in vitro and in mice. The E protein fusion loop epitope represents a potential candidate for therapeutic antibodies against ZIKV.Entities:
Mesh：
Substances：
Year: 2016 PMID： 27158114 DOI： 10.1016/j.chom.2016.04.013
Source DB: PubMed Journal: Cell Host Microbe ISSN： 1931-3128 Impact factor: 21.023