The 3.8 Å resolution cryo-EM structure of Zika virus

TLDR

The rapid spread of Zika virus and its unexpected links to birth defects and autoimmune neurological syndrome have raised global concern, and the virus belongs to the flavivirus family alongside dengue, yellow fever, and West Nile viruses. We determined a 3.8‑Å cryo‑EM structure of mature Zika virus that is similar to other flaviviruses except for a ~10‑residue region around the Asn154 glycosylation site, whose carbohydrate moiety may serve as a host‑cell attachment site and whose variation among strains and flaviviruses could affect transmission and disease.

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.