UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules

Sara K. Shanda, Duncan W. Wilson

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

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, KΔUL36GFP, 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 KΔUL36GFP 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.

Original languageEnglish (US)
Pages (from-to)7388-7394
Number of pages7
JournalJournal of virology
Volume82
Issue number15
DOIs
StatePublished - Aug 2008

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Fingerprint Dive into the research topics of 'UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules'. Together they form a unique fingerprint.

Cite this