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Mechanisms of membrane permeabilization by picornavirus 2B viroporin
Author(s) -
Nieva José L.,
Agirre Aitziber,
Nir Shlomo,
Carrasco Luis
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00852-4
Subject(s) - membrane , picornavirus , chemistry , protein–lipid interaction , biophysics , membrane protein , lipid bilayer , porin , cell membrane , cell , vesicle , microbiology and biotechnology , biochemistry , biology , bacterial outer membrane , integral membrane protein , rna , escherichia coli , gene
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.