3 years ago

Functional Analysis of Glycosylation of Zika Virus Envelope Protein

Functional Analysis of Glycosylation of Zika Virus Envelope Protein
Tian Wang, Christopher M. Roundy, Elizabeth Mays, Camila R. Fontes-Garfias, Xuping Xie, Chao Shan, Jing Zou, Scott C. Weaver, Maki Wakamiya, Huanle Luo, Daniele B.A. Medeiros, Pei-Yong Shi, Shannan L. Rossi, Antonio E. Muruato


Zika virus (ZIKV) infection causes devastating congenital abnormities and Guillain-Barré syndrome. The ZIKV envelope (E) protein is responsible for viral entry and represents a major determinant for viral pathogenesis. Like other flaviviruses, the ZIKV E protein is glycosylated at amino acid N154. To study the function of E glycosylation, we generated a recombinant N154Q ZIKV that lacks the E glycosylation and analyzed the mutant virus in mammalian and mosquito hosts. In mouse models, the mutant was attenuated, as evidenced by lower viremia, decreased weight loss, and no mortality; however, knockout of E glycosylation did not significantly affect neurovirulence. Mice immunized with the mutant virus developed a robust neutralizing antibody response and were completely protected from wild-type ZIKV challenge. In mosquitoes, the mutant virus exhibited diminished oral infectivity for the Aedes aegypti vector. Collectively, the results demonstrate that E glycosylation is critical for ZIKV infection of mammalian and mosquito hosts.

Publisher URL: http://www.cell.com/cell-reports/fulltext/S2211-1247(17)31448-1

DOI: 10.1016/j.celrep.2017.10.016

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