Brown W Clay, Akey David L, Konwerski Jamie R, Tarrasch Jeffrey T, Skiniotis Georgios, Kuhn Richard J, Smith Janet L
Life Sciences Institute, University of Michigan, Ann Arbor, Michigan, USA.
Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.
Nat Struct Mol Biol. 2016 Sep;23(9):865-7. doi: 10.1038/nsmb.3268. Epub 2016 Jul 25.
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.
寨卡病毒已被认为与新生儿小头畸形和吉兰-巴雷综合征的增加有关，它已在世界热带地区迅速传播。毒力蛋白NS1在基因组复制和宿主免疫系统调节中发挥作用。在此，我们报告了全长寨卡病毒NS1的晶体结构，揭示了一个用于膜结合的细长疏水表面以及一个在黄病毒之间有很大差异的极性表面。
