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Mechanisms of membrane permeabilization by picornavirus 2B viroporin

José L Nieva1, Aitziber Agirre, Shlomo Nir

  • 1Unidad de Biofísica (CSIC-UPV/EHU) and Departamento de Bioquímica, Universidad del País Vasco, Aptdo. 644, 48080 Bilbao, Spain. gbpniesj@lg.ehu.es

FEBS Letters
|September 16, 2003
PubMed

Insights

Picornavirus infection causes cell membrane permeabilization, with the 2B protein forming pores. Four 2B monomers create a tetramer sufficient to permeabilize lipid vesicles, highlighting lipid interactions in this viral process.

Area of Science:

  • Virology
  • Molecular Biology
  • Biophysics

Background:

  • Picornaviruses induce cell membrane permeabilization during infection.
  • The non-structural protein 2B is implicated in this membrane damage.

Purpose of the Study:

  • To investigate the porin-like activity of picornavirus 2B protein.
  • To elucidate the mechanism of 2B-mediated membrane permeabilization.

Main Methods:

  • Utilized isolated membrane-protein systems and model membranes.
  • Studied 2B protein behavior in the absence of other cellular components.

Main Results:

  • Detected 2B porin-like activity in model membrane systems.
  • Four 2B monomers (tetramers) were sufficient to permeabilize lipid vesicles.
  • Demonstrated lipid dependence of 2B oligomerization and pore formation.

Conclusions:

  • Picornavirus 2B protein forms functional pores in lipid membranes.
  • Lipid composition, particularly negatively charged surfaces, influences 2B pore formation.
  • This provides a molecular mechanism for viral-induced membrane permeabilization.

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