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Basic Characteristics of Mutations
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Mutation Site
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N154Q |
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Mutation Site Sentence
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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. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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E |
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Standardized Encoding Gene
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envelope
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Genotype/Subtype
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- |
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Viral Reference
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KU955593.1
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Functional Impact and Mechanisms
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Disease
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Cell line
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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29091758
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Title
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Functional Analysis of Glycosylation of Zika Virus Envelope Protein
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Author
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Fontes-Garfias CR,Shan C,Luo H,Muruato AE,Medeiros DBA,Mays E,Xie X,Zou J,Roundy CM,Wakamiya M,Rossi SL,Wang T,Weaver SC,Shi PY
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Journal
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Cell reports
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Journal Info
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2017 Oct 31;21(5):1180-1190
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Abstract
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Zika virus (ZIKV) infection causes devastating congenital abnormities and Guillain-Barre 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.
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Sequence Data
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-
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