The 3.8Å resolution cryo-EM structure of Zika Virus

By Devika Sirohi, Zhenguo Chen, Lei Sun, T. Klose, T. Pierson, Michael G. Rossmann, R. Kuhn. Science, 2016

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Unveiling the Zika virus The ongoing Zika virus epidemic is of grave concern because of its apparent links to congenital microcephaly and Guillain-Barré syndrome. Sirohi et al. present a near-atomic-resolution structure of mature Zika virus determined by cryo-electron microscopy. The structure is mainly similar to that of other flaviviruses such as dengue virus; however, there are differences in a region that may be involved in binding to host receptors. The structure provides a foundation for analysis of the antigenicity and pathogenesis of Zika virus. Science, this issue p. 467 The structure of mature Zika virus is similar to other flaviviruses, except in the region of a potential cell attachment site. The recent rapid spread of Zika virus and its unexpected linkage to birth defects and an autoimmune neurological syndrome have generated worldwide concern. Zika virus is a flavivirus like the dengue, yellow fever, and West Nile viruses. We present the 3.8 angstrom resolution structure of mature Zika virus, determined by cryo–electron microscopy (cryo-EM). The structure of Zika virus is similar to other known flavivirus structures, except for the ~10 amino acids that surround the Asn154 glycosylation site in each of the 180 envelope glycoproteins that make up the icosahedral shell. The carbohydrate moiety associated with this residue, which is recognizable in the cryo-EM electron density, may function as an attachment site of the virus to host cells. This region varies not only among Zika virus strains but also in other flaviviruses, which suggests that differences in this region may influence virus transmission and disease.

Subfields: Infectious Diseases, Insect Science, Public Health, Environmental and Occupational Health

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Citations in the corpus

Bispectrum Inversion with Application to Multireference Alignment (2017, methodology): “A chief motivation for this work arises from the imaging technique called single particle Cryo-Electron Microscopy (CryoEM), which allows to visualize molecules at near-atomic resolution [12], [13].”
Specificity, cross-reactivity, and function of antibodies elicited by Zika virus infection (2016, neutral): “According to the structure of the ZIKV E protein dimer (11, 12), the majority of the ZIKV and DENV conserved solvent-accessible residues are located in EDII, particularly in the fusion loop and the neighboring region (Fig.”