Abstract
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.
Original language | English |
---|---|
Pages (from-to) | 456-458 |
Number of pages | 3 |
Journal | Nature Structural and Molecular Biology |
Volume | 23 |
Issue number | 5 |
DOIs | |
Publication status | Published - 1 May 2016 |