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The Murid Herpesvirus-4 gL regulates an entry-associated conformation change in gH

Laurent Gillet1, Susanna Colaco, Philip G Stevenson

  • 1Division of Virology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom.

Plos One
|July 31, 2008
PubMed

Insights

Glycoprotein H (gH) and gL are essential for herpesvirus fusion. gL regulates gH and gB conformation switches, controlling viral entry and infectivity.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Herpesvirus membrane fusion is mediated by the glycoprotein H (gH)/gL heterodimer.
  • The precise mechanism of gH/gL function in viral entry remains incompletely understood.

Purpose of the Study:

  • To investigate the role of gL in regulating the conformational states of gH and gB during Murid Herpesvirus-4 infection.
  • To elucidate the functional switch of gH from cell binding to membrane fusion.

Main Methods:

  • Comparative analysis of wild-type and gL-deficient Murid Herpesvirus-4 virions.
  • Conformational analysis of gH and gB.
  • Assessment of capsid release and viral infectivity.

Main Results:

  • Murid Herpesvirus-4 gH adopts a gL-dependent conformation on the virion, switching to a gL-independent form post-endocytosis.
  • This gH conformational switch coincides with gB conformational changes and capsid release.
  • Absence of gL leads to constitutive gL-independent gH conformation, premature gB activation, and reduced infectivity.

Conclusions:

  • gL is critical for maintaining the correct conformation of gH on the virion.
  • gL acts as a key regulator for the functional transition of gH and gB, essential for efficient herpesvirus membrane fusion and infection.

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