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Nat Struct Mol Biol. 2016 May;23(5):456-8. doi: 10.1038/nsmb.3213. Epub 2016 Apr 18.

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

Song H1,2, Qi J1, Haywood J1, Shi Y1,2,3,4,5, Gao GF1,2,3,4,5,6.

Author information

1
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
2
Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing, China.
3
Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen, China.
4
Center for Influenza Research and Early-warning (CASCIRE), Chinese Academy of Sciences, Beijing, China.
5
Savaid Medical School, University of Chinese Academy of Sciences, Beijing, China.
6
National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing, China.

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.

PMID:
27088990
DOI:
10.1038/nsmb.3213
[Indexed for MEDLINE]

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