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Updated: Jul 5, 2026

Live Cell Imaging of Alphaherpes Virus Anterograde Transport and Spread
Published on: August 16, 2013
UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules
Sara K Shanda1, Duncan W Wilson
1Department of Developmental and Molecular Biology, 1300 Morris Park Ave., Bronx, NY 10461, USA.
Abstract:
Microtubule-mediated anterograde transport is essential for the transport of herpes simplex virus type 1 (HSV-1) along axons, yet little is known regarding the mechanism and the machinery required for this process. Previously, we were able to reconstitute anterograde transport of HSV-1 on microtubules in an in vitro microchamber assay. Here we report that the large tegument protein UL36p is essential for this trafficking. Using a fluorescently labeled UL36 null HSV-1 strain, KDeltaUL36GFP, we found that it is possible to isolate a membrane-associated population of this virus. Although these viral particles contained normal amounts of tegument proteins VP16, vhs, and VP22, they displayed a 3-log decrease in infectivity and showed a different morphology compared to UL36p-containing virions. Membrane-associated KDeltaUL36GFP also displayed a slightly decreased binding to microtubules in our microchamber assay and a two-thirds decrease in the frequency of motility. This decrease in binding and motility was restored when UL36p was supplied in trans by a complementing cell line. These findings suggest that UL36p is necessary for HSV-1 anterograde transport.
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