Author
Listed:
- 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)
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.
Suggested Citation
Romain F. Laine & Anna Albecka & Sebastian van de Linde & Eric J. Rees & Colin M. Crump & Clemens F. Kaminski, 2015.
"Structural analysis of herpes simplex virus by optical super-resolution imaging,"
Nature Communications, Nature, vol. 6(1), pages 1-10, May.
Handle:
RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms6980
DOI: 10.1038/ncomms6980
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