The association of Zika virus (ZIKV) infections with microcephaly has resulted in an ongoing public-health emergency. Here we report the crystal structure of a C-terminal fragment of ZIKV nonstructural protein 1 (NS1), a major host-interaction molecule that functions in flaviviral replication, pathogenesis and immune evasion. Comparison with West Nile and dengue virus NS1 structures reveals conserved features but diverse electrostatic characteristics at host-interaction interfaces, thus possibly implying different modes of flavivirus pathogenesis.

April 19, 2016

Zika virus NS1 structure reveals diversity of electrostatic surfaces among flaviviruses : Nature Structural & Molecular Biology : Nature Publishing Group


Nature Structural & Molecular Biology 23, 456–458  doi:10.1038/nsmb.3213

The crystal structure of the C-terminal region of Zika virus nonstructural protein 1 (NS1) reveals a fold similar to those of other flaviviruses (dengue and West Nile viruses) but different surface electrostatic features.

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