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Updated: Mar 23, 2026
Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
Published on: July 20, 2022
The 3.8 Å resolution cryo-EM structure of Zika virus
Devika Sirohi1, Zhenguo Chen1, Lei Sun1
1Markey Center for Structural Biology and Purdue Institute for Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN 47907, USA.
Abstract:
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 Asn(154) 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.
Insights
The Zika virus structure reveals variations in envelope glycoproteins, potentially explaining its transmission and disease impact. This flavivirus research offers insights into viral attachment and host cell interactions.
Area of Science:
- Virology
- Structural Biology
- Infectious Diseases
Background:
- Zika virus has rapidly spread globally, causing concern due to its association with birth defects and neurological syndromes.
- Zika virus belongs to the Flaviviridae family, which includes other significant human pathogens like dengue, yellow fever, and West Nile viruses.
Purpose of the Study:
- To determine the high-resolution structure of the mature Zika virus.
- To identify structural differences compared to other flaviviruses that might explain Zika's unique pathogenic properties.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was employed to resolve the Zika virus structure at 3.8 angstrom resolution.
- Analysis focused on the envelope glycoproteins and their surrounding regions, particularly the N-linked glycosylation site.
Main Results:
- The overall structure of Zika virus is similar to other flaviviruses.
- A key difference was observed in the ~10 amino acids surrounding the Asn(154) glycosylation site on the envelope glycoproteins.
- Electron density corresponding to a carbohydrate moiety at this site was identified, suggesting a potential role in host cell attachment.
Conclusions:
- The identified structural variations, especially around the glycosylation site, may influence Zika virus's transmission efficiency and disease spectrum.
- These findings provide a structural basis for understanding flavivirus diversity and host-pathogen interactions.
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