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Plasma Membrane-porating Domain in Poliovirus 2B Protein. A Short Peptide Mimics Viroporin Activity

AutorMadan, Vanesa; Sánchez-Martínez, Silvia; Vedovato, Natascia; Rispoli, Giorgio; Carrasco Llamas, Luis ; Nieva, José Luis
Palabras claveVirus–host interactions
Viroporin
Enterovirus
Pore-forming toxin
Transmembrane domain
Fecha de publicación26-sep-2007
EditorElsevier
CitaciónJournal of Molecular Biology Vol. 374, Issue 4, 7 December 2007, Pages 951-964
ResumenPicornavirus 2B, a non-structural protein required for effective viral replication, has been implicated in cell membrane permeabilization during the late phases of infection. Here, we have approached the molecular mechanism of this process by assessing the pore-forming activity of an overlapping peptide library that spanned the complete 2B sequence. At non-cytopathic concentrations, only the P3 peptide, spanning 2B residues 35–55, effectively assembled hydrophilic pores that allowed diffusion of low molecular mass solutes across the cell plasma membrane (IC50 ≈ 4 × 10−7 M) and boundary liposome bilayers (starting at peptide to lipid molar ratios > 1:104). Circular dichroism data were consistent with its capacity to fold as a helix in a membrane-like environment. Furthermore, addition of this peptide to a sealed plasma-membrane model, consisting of retinal rod outer segments patch-clamped in a whole-cell configuration, induced ion channel activity within seconds at concentrations as low as 10−8 M. Thus, we have established a “one-helix” 2B version that possesses the intrinsic pore-forming activity required to directly and effectively permeabilize the cell plasma membrane. We conclude that 2B viroporin can be classified as a genuine pore-forming toxin of viral origin, which is produced intracellularly at certain times post infection
Versión del editorhttp://dx.doi.org/10.1016/j.jmb.2007.09.058
URIhttp://hdl.handle.net/10261/5045
DOI10.1016/j.jmb.2007.09.058
ISSN0022-2836 (Print)
1089-8638 (Online)
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