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Journal of Virology, November 2006, p. 11165-11177, Vol. 80, No. 22
0022-538X/06/$08.00+0     doi:10.1128/JVI.01107-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Herpes Simplex Virus Capsids Are Transported in Neuronal Axons without an Envelope Containing the Viral Glycoproteins{triangledown} ,{dagger}

Aleksandra Snyder, Todd W. Wisner, and David C. Johnson*

Department of Molecular Microbiology & Immunology, Oregon Health & Sciences University, Portland, Oregon 97239

Received 30 May 2006/ Accepted 31 August 2006

Electron micrographic studies of neuronal axons have produced contradictory conclusions on how alphaherpesviruses are transported from neuron cell bodies to axon termini. Some reports have described unenveloped capsids transported on axonal microtubules with separate transport of viral glycoproteins within membrane vesicles. Others have observed enveloped virions in proximal and distal axons. We characterized transport of herpes simplex virus (HSV) in human and rat neurons by staining permeabilized neurons with capsid- and glycoprotein-specific antibodies. Deconvolution microscopy was used to view 200-nm sections of axons. HSV glycoproteins were very rarely associated with capsids (3 to 5%) and vice versa. Instances of glycoprotein/capsid overlap frequently involved nonconcentric puncta and regions of axons with dense viral protein concentrations. Similarly, HSV capsids expressing a VP26-green fluorescent protein fusion protein (VP26/GFP) did not stain with antiglycoprotein antibodies. Live-cell imaging experiments with VP26/GFP-labeled capsids demonstrated that capsids moved in a saltatory fashion, and very few stalled for more than 1 to 2 min. To determine if capsids could be transported down axons without glycoproteins, neurons were treated with brefeldin A (BFA). However, BFA blocked both capsid and glycoprotein transport. Glycoproteins were transported into and down axons normally when neurons were infected with an HSV mutant that produces immature capsids that are retained in the nucleus. We concluded that HSV capsids are transported in axons without an envelope containing viral glycoproteins, with glycoproteins transported separately and assembling with capsids at axon termini.

* Corresponding author. Mailing address: L-220, Dept. of Mol. Microbiology & Immunology, Oregon Health & Science University, 3181 SW Sam Jackson Park Rd., Portland, OR 97239. Phone: (503) 494-0834. Fax: (503) 494-6862. E-mail: johnsoda{at}ohsu.edu.

{triangledown} Published ahead of print on 13 September 2006.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, November 2006, p. 11165-11177, Vol. 80, No. 22
0022-538X/06/$08.00+0     doi:10.1128/JVI.01107-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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