The Ablation of Envelope Protein Glycosylation Enhances the Neurovirulence of ZIKV and Cell Apoptosis in Newborn Mice

Figure 1

Mutation, phylogenetic, and structural analyses of the ZKC2P4 and ZKC2P6 strains. (a) The aa mutation (highlighted yellow) of the ZKC2P4 and ZKC2P6 strain are aligned to the corresponding aa of other ZIKV strains. “-” indicates an aa deficiency. Red indicates the N154 glycosylation site. (b) Phylogenetic tree constructed based on the nucleic acids of the complete open reading frame by the maximum-likelihood algorithm in the MEGA v5.05 software. “●” indicates the African lineage reference strain; “○” indicates the Asian lineage reference strain; “△” indicates the strains used in this study. (c) Superposition of the artist-rendered models of E proteins in the ZKC2P4 (green) and ZKC2P6 (blue). Red circle indicates the loop region surrounding the glycosylation site, and yellow circle indicates the glycan loop. (d) Superposition of the loop region surrounding the glycosylation site (140 to 177 in ZKC2P4 and 140 to 170 in ZKC2P6) of the E protein. The stick structure represents the glycan of the ZKC2P4 strain, and the alpha-helix is indicated by the black arrow.

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