Publication date: Available online 26 June 2018
Author(s): Madhumati Sevvana, Feng Long, Andrew S. Miller, Thomas Klose, Geeta Buda, Lei Sun, Richard J. Kuhn, Michael G. Rossmann
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.
Teaser The atomic structure of mature Zika virus at a resolution of 3.1 Å and its comparison with other mosquito-borne flavivirus structures revealed important structural components of the infection mechanism. These results also identified probable drug binding pockets and provide a structural basis for vaccine design.