Structural analysis of herpes simplex virus by optical super-resolution imaging.
Structural analysis of herpes simplex virus by optical super-resolution imaging.
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DOI:
10.1038/ncomms6980
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发表时间:
2015-01-22
影响因子:
16.6
通讯作者:
Kaminski, Clemens F.
中科院分区:
文献类型:
--
作者:
Laine, Romain F.;Albecka, Anna;van de Linde, Sebastian;Rees, Eric J.;Crump, Colin M.;Kaminski, Clemens F.
Herpes simplex virus type-1 (HSV-1) is one of the most widespread pathogens among humans. Although the structure of HSV-1 has been extensively investigated, the precise organization of tegument and envelope proteins remains elusive. Here we use super-resolution imaging by direct stochastic optical reconstruction microscopy (dSTORM) in combination with a model-based analysis of single-molecule localization data, to determine the position of protein layers within virus particles. We resolve different protein layers within individual HSV-1 particles using multi-colour dSTORM imaging and discriminate envelope-anchored glycoproteins from tegument proteins, both in purified virions and in virions present in infected cells. Precise characterization of HSV-1 structure was achieved by particle averaging of purified viruses and model-based analysis of the radial distribution of the tegument proteins VP16, VP1/2 and pUL37, and envelope protein gD. From this data, we propose a model of the protein organization inside the tegument. The online version of this article (doi:10.1038/ncomms6980) contains supplementary material, which is available to authorized users. Herpes simplex virus type-1 (HSV-1) is a widespread human pathogen, the structure of which is not yet fully characterized. Here, the authors apply dSTORM super-resolution microscopy in combination with advanced data analysis tools to locate the position of four key protein layers in HSV-1 with unprecedented precision. The online version of this article (doi:10.1038/ncomms6980) contains supplementary material, which is available to authorized users.
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