The 3.8 Å resolution cryo-EM structure of Zika virus

• Published in: Science (American Association for the Advancement of Science) Vol. 352; no. 6284; pp. 467 - 470
• Main Authors: Sirohi, Devika, Chen, Zhenguo, Sun, Lei, Klose, Thomas, Pierson, Theodore C., Rossmann, Michael G., Kuhn, Richard J.
• Format: Journal Article
• Language: English
• Published: United States American Association for the Advancement of Science 22.04.2016; The American Association for the Advancement of Science
• Subjects: Amino Acid Sequence; Analysis; Birth defects; Cryoelectron Microscopy; Electron microscopes; Glycosylation; Humans; Molecular Sequence Data; Protein Structure, Tertiary; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - ultrastructure; Viral Matrix Proteins - chemistry; Viral Matrix Proteins - ultrastructure; Zika virus; Zika Virus - chemistry; Zika Virus - ultrastructure
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.aaf5316

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.