School of Molecular and Cellular Biology, Faculty of Biological Sciences, and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, West Yorkshire, LS2 9JT, United Kingdom.
Institute of Technology, University of Tartu, Tartu, Estonia.
Sci Rep. 2017 Jul 18;7(1):5682. doi: 10.1038/s41598-017-05820-0.
Chikungunya virus (CHIKV), a mosquito-borne alphavirus, causes febrile disease, muscle and joint pain, which can become chronic in some individuals. The non-structural protein 3 (nsP3) plays essential roles during infection, but a complete understanding of its function is lacking. Here we used a microscopy-based approach to image CHIKV nsP3 inside human cells. The SNAP system consists of a self-labelling enzyme tag, which catalyses the covalent linking of exogenously supplemented synthetic ligands. Genetic insertion of this tag resulted in viable replicons and specific labelling while preserving the effect of nsP3 on stress granule responses and co-localisation with GTPase Activating Protein (SH3 domain) Binding Proteins (G3BPs). With sub-diffraction, three-dimensional, optical imaging, we visualised nsP3-positive structures with variable density and morphology, including high-density rod-like structures, large spherical granules, and small, low-density structures. Next, we confirmed the utility of the SNAP-tag for studying protein turnover by pulse-chase labelling. We also revealed an association of nsP3 with cellular lipid droplets and examined the spatial relationships between nsP3 and the non-structural protein 1 (nsP1). Together, our study provides a sensitive, specific, and versatile system for fundamental research into the individual functions of a viral non-structural protein during infection with a medically important arthropod-borne virus (arbovirus).
基孔肯雅病毒(CHIKV)是一种蚊媒甲病毒,可引起发热、肌肉和关节疼痛,在某些个体中可能会变为慢性疾病。非结构蛋白 3(nsP3)在感染过程中发挥着重要作用,但对其功能的全面了解仍存在不足。在这里,我们使用基于显微镜的方法来观察 CHIKV nsP3 在人体细胞内的情况。SNAP 系统由一种自我标记的酶标签组成,该标签可催化外源补充的合成配体的共价连接。将该标签插入基因中会导致有活力的复制子和特异性标记,同时保留 nsP3 对应激颗粒反应和与 GTP 酶激活蛋白(SH3 结构域)结合蛋白(G3BPs)共定位的影响。通过亚衍射、三维、光学成像,我们可视化了具有不同密度和形态的 nsP3 阳性结构,包括高密度棒状结构、大球形颗粒以及小而低密度的结构。接下来,我们通过脉冲追踪标记证实了 SNAP 标签在研究蛋白周转方面的实用性。我们还揭示了 nsP3 与细胞脂滴的关联,并检查了 nsP3 与非结构蛋白 1(nsP1)之间的空间关系。总之,我们的研究为研究医学上重要的节肢动物传播病毒(arbovirus)感染过程中病毒非结构蛋白的单个功能提供了一种敏感、特异和通用的系统。