@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}
}
@article{MakbulKraftGriessmannetal.2021,
  author    = {Makbul, Cihan and Kraft, Christian and Grießmann, Matthias and Rasmussen, Tim and Katzenberger, Kilian and Lappe, Melina and Pfarr, Paul and Stoffer, Cato and St{\"o}hr, Mara and Wandinger, Anna-Maria and B{\"o}ttcher, Bettina},
  title     = {Binding of a pocket factor to Hepatitis B virus capsids changes the rotamer conformation of Phenylalanine 97},
  series = {Viruses},
  volume    = {13},
  journal   = {Viruses},
  number    = {11},
  issn      = {1999-4915},
  doi       = {10.3390/v13112115},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-248565},
  year      = {2021},
  abstract  = {(1) Background: During maturation of the Hepatitis B virus, a viral polymerase inside the capsid transcribes a pre-genomic RNA into a partly double stranded DNA-genome. This is followed by envelopment with surface proteins inserted into a membrane. Envelopment is hypothetically regulated by a structural signal that reports the maturation state of the genome. NMR data suggest that such a signal can be mimicked by the binding of the detergent Triton X 100 to hydrophobic pockets in the capsid spikes. (2) Methods: We have used electron cryo-microscopy and image processing to elucidate the structural changes that are concomitant with the binding of Triton X 100. (3) Results: Our maps show that Triton X 100 binds with its hydrophobic head group inside the pocket. The hydrophilic tail delineates the outside of the spike and is coordinated via Lys-96. The binding of Triton X 100 changes the rotamer conformation of Phe-97 in helix 4, which enables a π-stacking interaction with Trp-62 in helix 3. Similar changes occur in mutants with low secretion phenotypes (P5T and L60V) and in a mutant with a pre-mature secretion phenotype (F97L). (4) Conclusion: Binding of Triton X 100 is unlikely to mimic structural maturation because mutants with different secretion phenotypes show similar structural responses.},
  language  = {en}
}