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Extended surface for membrane association in Zika virus NS1 structure.


ABSTRACT: The Zika virus, which has been implicated in an increase in neonatal microcephaly and Guillain-Barré syndrome, has spread rapidly through tropical regions of the world. The virulence protein NS1 functions in genome replication and host immune-system modulation. Here, we report the crystal structure of full-length Zika virus NS1, revealing an elongated hydrophobic surface for membrane association and a polar surface that varies substantially among flaviviruses.

SUBMITTER: Brown WC 

PROVIDER: S-EPMC5951387 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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Extended surface for membrane association in Zika virus NS1 structure.

Brown W Clay WC   Akey David L DL   Konwerski Jamie R JR   Tarrasch Jeffrey T JT   Skiniotis Georgios G   Kuhn Richard J RJ   Smith Janet L JL  

Nature structural & molecular biology 20160725 9


The Zika virus, which has been implicated in an increase in neonatal microcephaly and Guillain-Barré syndrome, has spread rapidly through tropical regions of the world. The virulence protein NS1 functions in genome replication and host immune-system modulation. Here, we report the crystal structure of full-length Zika virus NS1, revealing an elongated hydrophobic surface for membrane association and a polar surface that varies substantially among flaviviruses. ...[more]

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