Herpes simplex virus capsid localization to ESCRT-VPS4 Complexes in the presence and absence of the large tegument protein UL36p

Himanshu Kharkwal, Caitlin G. Smith, Duncan W. Wilson

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

UL36p (VP1/2) is the largest protein encoded by herpes simplex virus 1 (HSV-1) and resides in the innermost layer of tegument, the complex protein layer between the capsid and envelope. UL36p performs multiple functions in the HSV life cycle, including a critical but unknown role in capsid cytoplasmic envelopment. We tested whether UL36p is essential for envelopment because it is required to engage capsids with the cellular ESCRT/Vps4 apparatus. A green fluorescent protein (GFP)-fused form of the dominant negative ATPase Vps4-EQ was used to irreversibly tag ESCRT envelopment sites during infection by UL36p-expressing and UL36-null HSV strains. Using fluorescence microscopy and scanning electron microscopy, we quantitated capsid/Vps4-EQ colocalization and examined the ultrastructure of the corresponding viral assembly intermediates. We found that loss of UL36p resulted in a two-thirds reduction in the efficiency of capsid/Vps4-EQ association but that the remaining UL36p-null capsids were still able to engage the ESCRT envelopment apparatus. It appears that although UL36p helps to couple HSV capsids to the ESCRT pathway, this is likely not the sole reason for its absolute requirement for envelopment.

Original languageEnglish (US)
Pages (from-to)7257-7267
Number of pages11
JournalJournal of Virology
Volume90
Issue number16
DOIs
StatePublished - 2016

ASJC Scopus subject areas

  • Immunology
  • Medicine(all)
  • Virology

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