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.
%0 Journal Article
%1 laine2015structural
%A Laine, Romain F.
%A Albecka, Anna
%A van de Linde, Sebastian
%A Rees, Eric J.
%A Crump, Colin M.
%A Kaminski, Clemens F.
%D 2015
%I Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
%J Nat Commun
%K linde
%T Structural analysis of herpes simplex virus by optical super-resolution imaging
%U http://dx.doi.org/10.1038/ncomms6980
%V 6
%X 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.
@article{laine2015structural,
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.},
added-at = {2015-01-22T14:22:41.000+0100},
author = {Laine, Romain F. and Albecka, Anna and van de Linde, Sebastian and Rees, Eric J. and Crump, Colin M. and Kaminski, Clemens F.},
biburl = {https://www.bibsonomy.org/bibtex/2a24fb5fa0cd5867e2a8e6552a82e3469/reichert},
comment = {Supplementary information available for this article at http://www.nature.com/ncomms/2015/150122/ncomms6980/suppinfo/ncomms6980_S1.html},
interhash = {c85b610cb65c2f47a994a3bae56cf361},
intrahash = {a24fb5fa0cd5867e2a8e6552a82e3469},
journal = {Nat Commun},
keywords = {linde},
month = jan,
publisher = {Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.},
timestamp = {2015-01-22T14:22:41.000+0100},
title = {Structural analysis of herpes simplex virus by optical super-resolution imaging},
url = {http://dx.doi.org/10.1038/ncomms6980},
volume = 6,
year = 2015
}