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Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum

R K Plemper1, A L Hammond, R Cattaneo

  • 1Molecular Medicine Program, Mayo Foundation, Rochester, Minnesota 55905, USA. plemper.richard@mayo.edu

The Journal of Biological Chemistry
|September 6, 2001
PubMed

Insights

Measles virus (MV) envelope glycoproteins H and F oligomerize in the endoplasmic reticulum (ER). This ER retention impacts viral replication and particle assembly, with ER-retained H severely affecting virus viability.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Measles virus (MV) is a significant human pathogen belonging to the Paramyxoviridae family.
  • The roles of envelope glycoproteins H and F in MV assembly and replication are crucial but not fully elucidated.
  • Understanding protein trafficking and oligomerization is key to viral pathogenesis.

Purpose of the Study:

  • To investigate the endoplasmic reticulum (ER) as the primary site for measles virus (MV) envelope glycoproteins H and F oligomerization.
  • To determine the impact of ER-retained H and F glycoproteins on MV replication and particle assembly.
  • To elucidate the significance of glycoprotein homo- and hetero-oligomerization in the ER for MV particle formation.

Main Methods:

  • Utilizing ER-retention motifs (RRR and KKXX) to retain MV glycoproteins H and F in the ER.
  • Employing co-transfection assays to assess the biological activity of retained glycoproteins.
  • Performing pulse-chase analysis and co-immunoprecipitation to study protein interactions.
  • Generating and analyzing recombinant MV expressing ER-retained glycoproteins.

Main Results:

  • ER-retained MV glycoproteins H and F formed homo- and hetero-oligomers within the ER.
  • Co-expression of ER-retained glycoproteins exhibited a dominant-negative effect on the biological activity of transport-competent glycoproteins.
  • Recombinant MV expressing ER-retained F showed altered cytopathic effects and reduced particle release.
  • Recombinant MV expressing ER-retained H could not be rescued, indicating a severe impact on viral viability.

Conclusions:

  • Measles virus (MV) envelope glycoproteins H and F undergo homo- and hetero-oligomerization in the ER.
  • ER oligomerization is critical for the proper trafficking and function of MV glycoproteins.
  • These ER-based oligomerization events play a significant role in the early stages of MV particle assembly and viral viability.

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