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  Cryo Electron Tomography of Herpes Simplex Virus during Axonal Transport and Secondary Envelopment in Primary Neurons

Ibiricu, I., Huiskonen, J. T., Doehner, K., Bradke, F., Sodeik, B., & Gruenewald, K. (2011). Cryo Electron Tomography of Herpes Simplex Virus during Axonal Transport and Secondary Envelopment in Primary Neurons. PLOS PATHOGENS, 7(12): e1002406, pp. [1]-[11]. doi:10.1371/journal.ppat.1002406.

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Ibiricu, Iosune1, Author
Huiskonen, Juha T.1, Author
Doehner, Katinka1, Author
Bradke, Frank1, 2, Author           
Sodeik, Beate1, Author
Gruenewald, Kay1, Author
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1External Organizations, ou_persistent22              
2Max Planck Research Group: Axonal Growth and Regeneration / Bradke, MPI of Neurobiology, Max Planck Society, ou_1113553              

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Free keywords: TEGUMENT PROTEIN PUL36; ROOT GANGLION NEURONS; PSEUDORABIES VIRUS; CAPSID TRANSPORT; CRYOELECTRON TOMOGRAPHY; 3-DIMENSIONAL STRUCTURE; ANTEROGRADE TRANSPORT; NERVOUS-SYSTEM; NUCLEAR EGRESS; UL25 PROTEINInfectious Diseases; Microbiology; Parasitology; Virology;
 Abstract: During herpes simplex virus 1 (HSV1) egress in neurons, viral particles travel from the neuronal cell body along the axon towards the synapse. Whether HSV1 particles are transported as enveloped virions as proposed by the 'married' model or as non-enveloped capsids suggested by the 'separate' model is controversial. Specific viral proteins may form a recruitment platform for microtubule motors that catalyze such transport. However, their subviral location has remained elusive. Here we established a system to analyze herpesvirus egress by cryo electron tomography. At 16 h post infection, we observed intra-axonal transport of progeny HSV1 viral particles in dissociated hippocampal neurons by live-cell fluorescence microscopy. Cryo electron tomography of frozen-hydrated neurons revealed that most egressing capsids were transported independently of the viral envelope. Unexpectedly, we found not only DNA-containing capsids (cytosolic C-capsids), but also capsids lacking DNA (cytosolic A-/B-capsids) in mid-axon regions. Subvolume averaging revealed lower amounts of tegument on cytosolic A-/B-capsids than on C-capsids. Nevertheless, all capsid types underwent active axonal transport. Therefore, even few tegument proteins on the capsid vertices seemed to suffice for transport. Secondary envelopment of capsids was observed at axon terminals. On their luminal face, the enveloping vesicles were studded with typical glycoprotein-like spikes. Furthermore, we noted an accretion of tegument density at the concave cytosolic face of the vesicle membrane in close proximity to the capsids. Three-dimensional analysis revealed that these assembly sites lacked cytoskeletal elements, but that filamentous actin surrounded them and formed an assembly compartment. Our data support the 'separate model' for HSV1 egress, i.e. progeny herpes viruses being transported along axons as subassemblies and not as complete virions within transport vesicles.

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Language(s): eng - English
 Dates: 2011-12
 Publication Status: Published online
 Pages: 11
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 Table of Contents: -
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Title: PLOS PATHOGENS
Source Genre: Journal
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Publ. Info: 185 BERRY ST, STE 1300, SAN FRANCISCO, CA 94107 USA : PUBLIC LIBRARY SCIENCE
Pages: - Volume / Issue: 7 (12) Sequence Number: e1002406 Start / End Page: [1] - [11] Identifier: ISSN: 1553-7366