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

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Intercellular gamma-herpesvirus dissemination involves co-ordinated intracellular membrane protein transport

Janet S May1, Brigitte D de Lima, Susanna Colaco

  • 1Division of Virology, Department of Pathology, University of Cambridge, Cambridge, UK.

Traffic (Copenhagen, Denmark)
|August 17, 2005
PubMed

Insights

Murine gamma-herpesvirus-68 (MHV-68) ORF58 protein is essential for transporting the gp48 glycoprotein (encoded by ORF27) to the cell surface. This interaction facilitates viral spread and cell binding.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Murine gamma-herpesvirus-68 (MHV-68) ORF27 encodes gp48, a type 2 transmembrane glycoprotein.
  • Gp48 is crucial for intercellular viral spread but typically remains intracellular after transfection.
  • The precise mechanism for gp48 cell surface expression and its role in viral spread are not fully understood.

Purpose of the Study:

  • To investigate the role of MHV-68 ORF58 in the cell surface transport of gp48 (ORF27).
  • To elucidate the molecular interactions between ORF58 and ORF27.
  • To determine the function of the ORF58/ORF27 complex in viral cell binding and spread.

Main Methods:

  • Utilized MHV-68 mutants deficient in ORF58.
  • Employed transfection of ORF27 and ORF58 individually and in combination.
  • Investigated protein localization using immunofluorescence microscopy (ER and trans-Golgi network localization).
  • Analyzed protein complex formation and cell binding assays.

Main Results:

  • ORF58 is necessary and sufficient for gp48 transport to the cell surface.
  • ORF58-deficient MHV-68 retained ORF27 in the endoplasmic reticulum (ER).
  • Co-transfection of ORF27 and ORF58 resulted in complex formation and cell surface localization.
  • ORF58, not ORF27, mediated cell binding through an extracellular loop.
  • ORF27 likely protects the ORF58 binding loop via glycosylation.

Conclusions:

  • ORF58 acts as a chaperone for ORF27, enabling its cell surface expression.
  • The ORF58/ORF27 complex is essential for MHV-68 intercellular spread.
  • ORF58 mediates cell binding, while ORF27 provides antibody protection.
  • Interdependent transport ensures the functional complex is present for viral propagation.

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