Abstract
Cell infection by picornaviruses leads to membrane permeabilization. Recent evidence suggests the involvement of the non-structural protein 2B in this process. We have recently reported the detection of 2B porin-like activity in isolated membrane-protein systems that lack other cell components. According to data derived from these model membranes, four self-aggregated 2B monomers (i.e. tetramers) would be sufficient to permeabilize a single lipid vesicle, allowing the free diffusion of solutes under ca. 1000 Da. Our findings also support a role for lipids in protein oligomerization and subsequent pore opening. The lipid dependence of these processes points to negatively charged cytofacial surfaces as 2B cell membrane targets.
Original language | English |
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Pages (from-to) | 68-73 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 552 |
Issue number | 1 |
DOIs | |
State | Published - 18 Sep 2003 |
Keywords
- Membrane permeabilization
- Poliovirus 2B
- Pore model
- Viroporin