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Journal of Virology, November 2008, p. 10613-10624, Vol. 82, No. 21
0022-538X/08/$08.00+0     doi:10.1128/JVI.01241-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Herpes Simplex Virus gE/gI and US9 Proteins Promote Transport of both Capsids and Virion Glycoproteins in Neuronal Axons

Aleksandra Snyder,¹ Katarina Polcicova,² and David C. Johnson^1*

Department of Molecular Microbiology and Immunology, Oregon Health and Sciences University, Portland, Oregon 97239,¹ Institute of Virology, Slovak Academy of Sciences, Bratislava, Slovak Republic²

Received 14 June 2008/ Accepted 19 August 2008

Following reactivation from latency, alphaherpesviruses replicate in sensory neurons and assemble capsids that are transported in the anterograde direction toward axon termini for spread to epithelial tissues. Two models currently describe this transport. The Separate model suggests that capsids are transported in axons independently from viral envelope glycoproteins. The Married model holds that fully assembled enveloped virions are transported in axons. The herpes simplex virus (HSV) membrane glycoprotein heterodimer gE/gI and the US9 protein are important for virus anterograde spread in the nervous systems of animal models. It was not clear whether gE/gI and US9 contribute to the axonal transport of HSV capsids, the transport of membrane proteins, or both. Here, we report that the efficient axonal transport of HSV requires both gE/gI and US9. The transport of both capsids and glycoproteins was dramatically reduced, especially in more distal regions of axons, with gE^–, gI^–, and US9-null mutants. An HSV mutant lacking just the gE cytoplasmic (CT) domain displayed an intermediate reduction in capsid and glycoprotein transport. We concluded that HSV gE/gI and US9 promote the separate transport of both capsids and glycoproteins. gE/gI was transported in association with other HSV glycoproteins, gB and gD, but not with capsids. In contrast, US9 colocalized with capsids and not with membrane glycoproteins. Our observations suggest that gE/gI and US9 function in the neuron cell body to promote the loading of capsids and glycoprotein-containing vesicles onto microtubule motors that ferry HSV structural components toward axon tips.

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* Corresponding author. Mailing address: L-220, Department of Microbiology and Immunology, Oregon Health and 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

Published ahead of print on 27 August 2008.

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Journal of Virology, November 2008, p. 10613-10624, Vol. 82, No. 21
0022-538X/08/$08.00+0     doi:10.1128/JVI.01241-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

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