Structural analysis of herpes simplex virus by optical super-resolution imaging
Romain F. Laine,
Anna Albecka,
Sebastian van de Linde,
Eric J. Rees,
Colin M. Crump () and
Clemens F. Kaminski ()
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Romain F. Laine: Laser Analytics Group, Cambridge University
Anna Albecka: Cambridge University
Sebastian van de Linde: Julius-Maximilians-University, Am Hubland
Eric J. Rees: Laser Analytics Group, Cambridge University
Colin M. Crump: Cambridge University
Clemens F. Kaminski: Laser Analytics Group, Cambridge University
Nature Communications, 2015, vol. 6, issue 1, 1-10
Abstract:
Abstract 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.
Date: 2015
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms6980
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DOI: 10.1038/ncomms6980
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