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Updated: Aug 29, 2026

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
06:40

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy

Published on: November 4, 2018

Analysis of the requirement for glycoprotein m in herpes simplex virus type 1 morphogenesis

Helena Browne1, Susanne Bell, Tony Minson

  • 1Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom. hb100@mole.bio.cam.ac.uk

Journal of Virology
|December 25, 2003
PubMed

Insights

Herpes simplex virus type 1 mutants lacking glycoproteins M and E showed minor growth defects. This contrasts with pseudorabies virus, indicating varied glycoprotein needs for virion assembly in alphaherpesviruses.

Area of Science:

  • Virology
  • Molecular Biology
  • Genetics

Background:

  • Herpes simplex virus type 1 (HSV-1) is a significant human pathogen.
  • Glycoproteins are crucial for viral structure and function.
  • Previous studies on related viruses like pseudorabies virus (PRV) highlight the importance of specific glycoproteins.

Purpose of the Study:

  • To investigate the role of glycoprotein M (gM) and glycoprotein E (gE) in HSV-1 replication.
  • To compare the function of gM and gE in HSV-1 with their counterparts in PRV.
  • To understand the variations in glycoprotein requirements for virion assembly among alphaherpesviruses.

Main Methods:

  • Construction and characterization of an HSV-1 mutant lacking both gM and gE.
  • Assessment of in vitro growth characteristics of the mutant virus compared to wild-type HSV-1.
  • Comparative analysis with existing data on a similar PRV mutant.

Main Results:

  • The HSV-1 mutant lacking gM and gE exhibited only marginal defects in in vitro growth.
  • This phenotype is significantly different from the severe growth impairment observed in a comparable PRV mutant.
  • The findings suggest that gM and gE are less critical for HSV-1 in vitro replication than for PRV.

Conclusions:

  • Glycoprotein requirements for efficient virion assembly and replication differ between HSV-1 and PRV.
  • The study highlights the diversity within the alphaherpesvirus family regarding essential viral glycoproteins.
  • Further research is needed to elucidate the specific roles and compensatory mechanisms for gM and gE in HSV-1.

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