Structure-function analysis of coxsackie B3 virus protein 2B

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F J Van kuppeveld1, W J Melchers, K Kirkegaard

  • 1Department of Medical Microbiology, University of Nijmegen, The Netherlands.

Virology
|January 6, 1997
PubMed

Insights

Coxsackievirus B3 protein 2B alters mammalian cells by inhibiting protein secretion and increasing membrane permeability. Specific domains within protein 2B are crucial for these functions, suggesting additional roles beyond membrane changes.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Poliovirus protein 2B inhibits protein secretion and increases cell membrane permeability.
  • These effects are observed in mammalian cells and are linked to poliovirus infection.

Purpose of the Study:

  • To investigate if coxsackievirus B3 (CBV3) protein 2B induces similar biochemical alterations in mammalian cells.
  • To determine the functional importance of specific domains within CBV3 protein 2B for its biochemical activities.

Main Methods:

  • Expression of wild-type and mutant CBV3 protein 2B in mammalian cells.
  • Analysis of protein secretion inhibition and hygromycin B susceptibility.
  • Mutagenesis of predicted cationic amphipathic alpha-helix and hydrophobic domains within CBV3 2B.

Main Results:

  • CBV3 protein 2B expression inhibits protein secretion and increases membrane permeability, mirroring poliovirus 2B effects.
  • The cationic amphipathic alpha-helix domain is essential for both functions.
  • Mutations in a second hydrophobic domain differentially affect protein secretion inhibition versus membrane permeability.

Conclusions:

  • Inhibition of protein secretion by CBV3 2B is not solely a consequence of increased membrane permeability.
  • CBV3 protein 2B likely possesses functions beyond altering membrane permeability and inhibiting protein secretion.
  • Specific domains within CBV3 2B are critical for its distinct biochemical activities.

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