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

doi:10.1016/j.virol.2014.02.003

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

Virology. 2014 Apr:454-455:67-77. doi: 10.1016/j.virol.2014.02.003. Epub 2014 Feb 22.

Authors

Barbara J Kelly¹, Rudolf Bauerfeind², Anne Binz³, Beate Sodeik³, Andrea S Laimbacher⁴, Cornel Fraefel⁴, Russell J Diefenbach⁵

Affiliations

¹ Centre for Virus Research, Westmead Millennium Institute, The University of Sydney and Westmead Hospital, Westmead, NSW 2145, Australia.
² Institute of Cell Biology, Hannover Medical School, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany.
³ Institute of Virology, Hannover Medical School, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany.
⁴ Institute of Virology, University of Zurich, 8057 Zurich, Switzerland.
⁵ Centre for Virus Research, Westmead Millennium Institute, The University of Sydney and Westmead Hospital, Westmead, NSW 2145, Australia. Electronic address: russell.diefenbach@sydney.edu.au.

PMID: 24725933
DOI: 10.1016/j.virol.2014.02.003

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.

Keywords: Herpes simplex virus; Tegument; Virus assembly; pUL36; pUL37.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Chlorocebus aethiops
DNA Mutational Analysis
Herpesvirus 1, Human / physiology*
Vero Cells
Viral Plaque Assay
Viral Proteins / metabolism*
Viral Structural Proteins / metabolism*
Virus Release*

Substances

UL36 protein, Human herpesvirus 1
UL37 protein, Human herpesvirus 1
Viral Proteins
Viral Structural Proteins