@article{LaineAlbeckavandeLindeetal.2015,
  author    = {Laine, Romain F. and Albecka, Anna and van de Linde, Sebastian and Rees, Eric J. and Crump, Colin M. and Kaminski, Clemens F.},
  title     = {Structural analysis of herpes simplex virus by optical super-resolution imaging},
  series = {Nature Communications},
  volume    = {6},
  journal   = {Nature Communications},
  number    = {5980},
  doi       = {10.1038/ncomms6980},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-144623},
  year      = {2015},
  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.},
  language  = {en}
}