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Zika virus NS1 structure reveals diversity of electrostatic surfaces among flaviviruses.

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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Song H,Qi J,Haywood J,Shi Y,Gao GF

doi

10.1038/nsmb.3213

subject

Has Abstract

pub_date

2016-05-01 00:00:00

pages

456-8

issue

5

eissn

1545-9993

issn

1545-9985

pii

nsmb.3213

journal_volume

23

pub_type

杂志文章

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