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Related Experiment Videos

Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment.

A P Huovila1, A M Eder, S D Fuller

  • 1Biological Structures and Biocomputing Programme, European Molecular Biology Laboratory, Heidelberg, Germany.

The Journal of Cell Biology
|September 1, 1992
PubMed
Summary

Hepatitis B surface antigen (HBsAg) assembly occurs in a unique pre-Golgi compartment, not the ER. This compartment lacks protein disulphide isomerase (PDI), allowing for the formation of disulfide-linked HBsAg oligomers before secretion.

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Area of Science:

  • Virology
  • Cell Biology
  • Protein Biochemistry

Background:

  • Hepatitis B surface antigen (HBsAg) forms secreted lipoprotein particles, heavily crosslinked by disulfide bonds.
  • HBsAg assembly is thought to occur in the ER, where protein disulphide isomerase (PDI) typically resolves such crosslinks.

Purpose of the Study:

  • To investigate the intracellular trafficking and assembly site of HBsAg.
  • To understand the role of the ER and post-ER compartments in HBsAg oligomerization and disulfide crosslinking.

Main Methods:

  • Double immunofluorescence studies using antibodies against ER resident proteins.
  • Localization studies using rab2 as an intermediate compartment marker.
  • Kinetic analysis of HBsAg dimer and oligomer formation.

Related Experiment Videos

  • Brefeldin A treatment to assess the role of the Golgi pathway.

    • Main Results:

    • HBsAg is rapidly sorted to a post-ER, pre-Golgi compartment that excludes PDI.
    • Disulfide-linked HBsAg dimers form early, followed by crosslinking into higher oligomers.
    • Oligomerization occurs in this PDI-deficient compartment, as evidenced by Brefeldin A treatment blocking further oligomer formation.

    Conclusions:

    • HBsAg assembly involves a two-step process: rapid dimerization in the ER, followed by transport to a PDI-excluding pre-Golgi compartment for final oligomerization.
    • This compartmentalization is crucial for achieving the specific disulfide crosslinking observed in secreted HBsAg particles.