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Related Experiment Videos

Secreted hepatitis B surface antigen polypeptides are derived from a transmembrane precursor.

K Simon1, V R Lingappa, D Ganem

  • 1Department of Microbiology, University of California Medical Center, San Francisco 94143.

The Journal of Cell Biology
|December 1, 1988
PubMed
Summary

Hepatitis B surface antigen (HBsAg) is secreted from cells as a lipoprotein particle. This process involves its initial synthesis as a membrane protein, followed by conversion and secretion without viral protein involvement.

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Area of Science:

  • Virology
  • Cell Biology
  • Biochemistry

Background:

  • Hepatitis B surface antigen (HBsAg) is the primary coat protein of the Hepatitis B virus.
  • HBsAg is secreted from infected cells as lipoprotein particles, independent of signal sequence removal.

Purpose of the Study:

  • To investigate the synthesis and transport pathway of HBsAg in cultured cells.
  • To elucidate the mechanism of HBsAg secretion.

Main Methods:

  • Utilized cultured cells engineered to express the cloned HBsAg gene.
  • Monitored the synthesis and intracellular transport of HBsAg.

Main Results:

  • HBsAg is initially synthesized as an integral membrane protein.
  • This transmembrane form undergoes conversion to a secreted lipoprotein complex within the endoplasmic reticulum.

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  • The secretion process occurs without cleavage of polypeptide segments or involvement of other viral proteins.

    • Conclusions:

    • HBsAg export is an unusual process involving conversion from a membrane-bound to a secreted form.
    • This pathway shares similarities with enveloped virus budding but does not require viral proteins.