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Syncytial phenotype of C-terminally truncated herpes simplex virus type 1 gB is associated with diminished membrane

Tirumala Kumar Chowdary1, Ekaterina E Heldwein

  • 1Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111 , USA.

Journal of Virology
|March 5, 2010
PubMed

Insights

The herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) cytoplasmic domain binds lipid membranes, regulating fusion. This interaction is crucial for controlling viral membrane fusion mechanisms.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • The cytoplasmic domain of herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) is a key regulator of membrane fusion.
  • The structural and mechanistic basis of gB's fusion regulation remains largely unknown.

Purpose of the Study:

  • To investigate the interaction of the full-length and truncated HSV-1 gB cytoplasmic domains with lipid membranes.
  • To elucidate the role of membrane association in the regulation of HSV-1-mediated membrane fusion.

Main Methods:

  • Studied the association of full-length and truncated HSV-1 gB cytoplasmic domains with lipid membranes using biophysical techniques.
  • Analyzed changes in helical content upon membrane interaction.

Main Results:

  • The full-length HSV-1 gB cytoplasmic domain stably associates with lipid membranes, particularly those with anionic head groups, accompanied by a significant increase in helical content.
  • Truncated domains associated with hyperfusion showed minimal membrane interaction and slight helical increase, while the fusion-null mutant exhibited negligible membrane binding and no helical change.
  • Identified two specific regions critical for membrane interactions within the gB cytoplasmic domain.

Conclusions:

  • Stable lipid membrane binding by the HSV-1 gB cytoplasmic domain is essential for its negative regulatory role in membrane fusion.
  • Specific regions within the gB cytoplasmic domain are critical for mediating these membrane interactions.

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