The interaction of the HSV-1 tegument proteins pUL36 and pUL37 is essential for secondary envelopment during viral egress

Barbara J Kelly, Rudolf Bauerfeind, Anne Binz, Beate Sodeik, Andrea S Laimbacher, Cornel Fraefel, Russell J Diefenbach

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The herpes simplex virus type 1 (HSV-1) tegument proteins pUL36 (VP1/2) and pUL37 are essential for viral egress. We previously defined a minimal domain in HSV-1 pUL36, residues 548-572, as important for binding pUL37. Here, we investigated the role of this region in binding to pUL37 and facilitating viral replication. We deleted residues 548-572 in frame in a virus containing a mRFP tag at the N-terminus of the capsid protein VP26 and an eGFP tag at the C-terminus of pUL37 (HSV-1pUL36∆548-572). This mutant virus was unable to generate plaques in Vero cells, indicating that deletion of this region of pUL36 blocks viral replication. Imaging of HSV-1pUL36∆548-572-infected Vero cells, in comparison to parental and resucant, revealed a block in secondary envelopment of cytoplasmic capsids. In addition, immunoblot analysis suggested that failure to bind pUL37 affected the stability of pUL36. This study provides further insight into the role of this essential interaction.

Original languageEnglish
Pages (from-to)67-77
Number of pages11
JournalVirology
Volume454–455
DOIs
Publication statusPublished - Apr 2014
Externally publishedYes

Keywords

  • Animals
  • Cercopithecus aethiops
  • DNA Mutational Analysis
  • Herpesvirus 1, Human
  • Vero Cells
  • Viral Plaque Assay
  • Viral Proteins
  • Viral Structural Proteins
  • Virus Release
  • Journal Article
  • Research Support, Non-U.S. Gov't
  • Tegument
  • Virus assembly
  • PUL37
  • PUL36
  • Herpes simplex virus

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