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Related Experiment Videos

Membrane protein lateral interactions control Semliki Forest virus budding

M Ekström1, P Liljeström, H Garoff

  • 1Department of Molecular Biology, Karolinska Institute, Huddinge, Sweden.

The EMBO Journal
|March 1, 1994
PubMed
Summary

Semliki Forest virus (SFV) membrane proteins p62 and E1 form trimers essential for virus budding. Genetic analysis reveals these trimers bind nucleocapsid, driving efficient virus particle formation.

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Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Semliki Forest virus (SFV) synthesizes p62 and E1 membrane proteins.
  • These proteins form heterodimers in the endoplasmic reticulum and are transported to the plasma membrane.
  • Mature SFV particles display trimeric spikes of p62E1 heterodimers forming a T=4 lattice.

Purpose of the Study:

  • To investigate the role of p62E1 heterodimer trimerization in Semliki Forest virus budding.
  • To understand the mechanism by which nucleocapsid (NC) binding influences virus particle formation.

Main Methods:

  • Co-expression of budding-competent and NC binding-deficient SFV heterodimers.
  • Genetic manipulation to create defects in nucleocapsid binding.
  • Analysis of virus budding efficiency and particle formation.

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Main Results:

  • NC binding-deficient heterodimers inhibit budding of competent heterodimers in a concentration-dependent manner.
  • Competent heterodimers can rescue incompetent ones, facilitating their incorporation into virus particles.
  • Trimerization of p62E1 heterodimers at the plasma membrane is crucial for efficient virus budding.

Conclusions:

  • Heterodimer complexation into trimers at the plasma membrane is essential for Semliki Forest virus budding.
  • Trimeric structures likely provide a multivalent binding site for the nucleocapsid, driving efficient virus budding.