Structure of the dengue virus glycoprotein non-structural protein 1 by electron microscopy and single-particle analysis
Structure of the dengue virus glycoprotein non-structural protein 1 by electron microscopy and single-particle analysis
复制标题
DOI：
10.1099/vir.0.039321-0
复制
发表时间：
2012-04-01
影响因子：
3.8
通讯作者：
Young, Paul R.
中科院分区：
文献类型：
--
作者：
Muller, David A.;Landsberg, Michael J.;Young, Paul R.
黄病毒非结构蛋白1（NS1）是一种糖蛋白，在自然感染过程中分泌为可溶性六聚体复合物。越来越多的证据表明，这种分泌形式的NS1（sNS1）在感染期间的免疫逃避和调节中起着重要作用。迄今为止，确定NS1晶体结构的尝试一直不成功，并且对sNS1六聚体的大分子组织知之甚少。在这里，我们应用单粒子分析的杆状病毒衍生的重组登革2型病毒NS1的电子显微镜获得的图像，以确定其三维结构的分辨率为23埃。这种结构揭示了一个桶状组织的三个二聚体单元，包括六聚体，并提供了进一步的见解寡聚体sNS 1的整体组织。
The flavivirus non-structural protein 1 (NS1) is a glycoprotein that is secreted as a soluble hexameric complex during the course of natural infection. Growing evidence indicates that this secreted form of NS1 (sNS1) plays a significant role in immune evasion and modulation during infection. Attempts to determine the crystal structure of NS1 have been unsuccessful to date and relatively little is known about the macromolecular organization of the sNS1 hexamer. Here, we have applied single-particle analysis to images of baculovirus-derived recombinant dengue 2 virus NS1 obtained by electron microscopy to determine its 3D structure to a resolution of 23 angstrom. This structure reveals a barrel-like organization of the three dimeric units that comprise the hexamer and provides further insights into the overall organization of oligomeric sNS1.