Structural analysis of herpes simplex virus by optical super-resolution imaging

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 r...

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Bibliographic Details
Published in:Nature communications 2015-01, Vol.6 (1), p.5980-5980, Article 5980
Main Authors: Laine, Romain F, Albecka, Anna, van de Linde, Sebastian, Rees, Eric J, Crump, Colin M, Kaminski, Clemens F
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal - chemistry
Cell Line
Cryoelectron Microscopy
Female
Glycoproteins
Herpes viruses
Herpesvirus 1, Human
Humans
Image Processing, Computer-Assisted
Investigations
Keratinocytes - virology
Localization
Mice
Mice, Inbred BALB C
Microscopy
Microscopy - methods
Microscopy, Fluorescence
Optical Imaging - methods
Proteins
Recombinant Proteins - chemistry
Simplexvirus - ultrastructure
Viral Envelope Proteins - chemistry
Viral Proteins - chemistry
Viral Structural Proteins - chemistry
Virion - metabolism
Virology
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Summary: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.
ISSN:2041-1723
2041-1723
DOI:10.1038/ncomms6980