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, Clemens F. Kaminski

Research output: Contribution to journalArticlepeer-review

69 Citations (Scopus)
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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.

Original languageEnglish
Article number5980
Number of pages10
JournalNature Communications
Publication statusPublished - 22 Jan 2015


  • Herpes simplex virus type-1
  • HSV-1
  • dSTORM
  • protein layers
  • envelope-anchored glycoproteins
  • tegument proteins


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