title: Mechanisms of membrane permeabilization by picornavirus 2B viroporin.
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.
authors.affiliation: Unidad de Biofísica (CSIC-UPV/EHU) and Departamento de Bioquímica, Universidad del País Vasco, Aptdo. 644, 48080 Bilbao, Spain. gbpniesj@lg.ehu.es
authors.forename: José L
authors.initials: JL
authors.lastname: Nieva
authors.forename: Aitziber
authors.initials: A
authors.lastname: Agirre
authors.forename: Shlomo
authors.initials: S
authors.lastname: Nir
authors.forename: Luis
authors.initials: L
authors.lastname: Carrasco
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism; D002463:Cell Membrane Permeability; D007473:Ion Channels; D007700:Kinetics; D050356:Lipid Metabolism; D015233:Models, Statistical; D008969:Molecular Sequence Data; D010716:Phosphatidylinositols / Q000737:chemistry; D010849:Picornaviridae / Q000737:chemistry* / Q000378:metabolism; D018272:Porins / Q000737:chemistry* / Q000378:metabolism; D020836:Protein Structure, Quaternary; D017386:Sequence Homology, Amino Acid
chemical_list: D007473:Ion Channels; D010716:Phosphatidylinositols; D018272:Porins