Literature DB >> 29958768

Refinement and Analysis of the Mature Zika Virus Cryo-EM Structure at 3.1 Å Resolution.

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.
Copyright © 2018 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Zika virus; antiviral binding sites; flavivirus comparisons; receptor binding sites; structure refinement

Mesh:

Substances:

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


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