Functional Analysis of Glycosylation of Zika Virus Envelope Protein

Publication date: 31 October 2017
Source:Cell Reports, Volume 21, Issue 5
Author(s): Camila R. Fontes-Garfias, Chao Shan, Huanle Luo, Antonio E. Muruato, Daniele B.A. Medeiros, Elizabeth Mays, Xuping Xie, Jing Zou, Christopher M. Roundy, Maki Wakamiya, Shannan L. Rossi, Tian Wang, Scott C. Weaver, Pei-Yong Shi
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.

Graphical abstract

Teaser

Zika virus (ZIKV) causes devastating congenital abnormities and Guillain-Barré syndrome. Fontes-Garfias et al. showed that the glycosylation of ZIKV envelope protein plays an important role in infecting mosquito vectors and pathogenesis in mouse.


http://ift.tt/2gU7jrS