Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
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DOI：
10.1038/nsb990
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发表时间：
2003-11-01
期刊：
影响因子：
--
通讯作者：
Kuhn, RJ
中科院分区：
文献类型：
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作者：
Zhang, W;Chipman, PR;Kuhn, RJ
改进的技术重建冷冻电子显微镜（cryo-EM）图像，现在已经有可能确定二级结构的包膜病毒的膜蛋白的特点。成熟登革病毒颗粒的结构通过cryo-EM和图像重建技术确定为9.5埃的分辨率，建立脂质包膜中180包膜（E）和180膜（M）蛋白的二级结构布置。E分子的α-螺旋茎区，以及M蛋白的N-末端部分的一部分，被埋在病毒膜的外小叶中。E和M蛋白的锚区各自形成反平行的E-E和M-M跨膜α-螺旋，使它们的C末端位于病毒膜的外部，与未加工的多蛋白的预测拓扑结构一致。这是仅有的几个跨膜蛋白原位分布的测定之一，表明核衣壳核心和包膜蛋白在成熟病毒中没有直接的相互作用。
Improved technology for reconstructing cryo-electron microscopy (cryo-EM) images has now made it possible to determine secondary structural features of membrane proteins in enveloped viruses. The structure of mature dengue virus particles was determined to a resolution of 9.5 Angstrom by cryo-EM and image reconstruction techniques, establishing the secondary structural disposition of the 180 envelope ( E) and 180 membrane ( M) proteins in the lipid envelope. The alpha-helical stem regions of the E molecules, as well as part of the N-terminal section of the M proteins, are buried in the outer leaflet of the viral membrane. The anchor regions of E and the M proteins each form antiparallel E-E and M-M transmembrane alpha-helices, leaving their C termini on the exterior of the viral membrane, consistent with the predicted topology of the unprocessed polyprotein. This is one of only a few determinations of the disposition of transmembrane proteins in situ and shows that the nucleocapsid core and envelope proteins do not have a direct interaction in the mature virus.