| Literature DB >> 29958768 |
Madhumati Sevvana1, Feng Long1, Andrew S Miller1, Thomas Klose1, Geeta Buda1, Lei Sun1, Richard J Kuhn1, Michael G Rossmann2.
Abstract
Among the several arthropod-borne human flaviviral diseases, the recent outbreak of Zika virus (ZIKV) has caused devastating birth defects and neurological disorders, challenging the world with another major public health concern. We report here the refined structure of the mature ZIKV at a resolution of 3.1 Å as determined by cryo-electron microscopic single-particle reconstruction. The improvement in the resolution, compared with previous enveloped virus structures, was the result of optimized virus preparation methods and data processing techniques. The glycoprotein interactions and surface properties of ZIKV were compared with other mosquito-borne flavivirus structures. The largest structural differences and sequence variations occur at the glycosylation loop associated with receptor binding. Probable drug binding pockets were identified on the viral surface. These results also provide a structural basis for the design of vaccines against ZIKV.Entities:
Keywords: Zika virus; antiviral binding sites; flavivirus comparisons; receptor binding sites; structure refinement
Mesh:
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Year: 2018 PMID: 29958768 PMCID: PMC6125166 DOI: 10.1016/j.str.2018.05.006
Source DB: PubMed Journal: Structure ISSN: 0969-2126 Impact factor: 5.006