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Membrane-active peptides derived from picornavirus 2B viroporin

AutorSánchez-Martínez, Silvia; Madan, Vanesa; Carrasco Llamas, Luis ; Nieva, José Luis
Palabras clavePeptide-targeting to mitochondria
Pore-forming peptides
Peptide-lipid interactions
Enterovirus 2B
Fecha de publicación2012
EditorBentham Science Publishers
CitaciónCurrent Protein and Peptide Science 13: 632- 643 (2012)
ResumenViruses have evolved membrane-restructuring mechanisms for sustaining entry into cells, genome replication and release from host cells. Picornavirus 2B, a non-structural protein required for effective viral replication, functions as a potent intracellular pore-forming toxin by altering the permeability of cellular endomembranes. Two consecutive hydrophobic regions have been identified in 2B protein that could function as an >α-helix-turn-α-helix> hairpin membraneanchor. A peptide derived from the first transmembrane domain comprised a one-helix 2B version that possesses the intrinsic pore-forming activity required to directly and effectively permeabilize the cell plasma membrane. Moreover, this miniaturized form is capable of translocating through the plasma membrane of culture cells and to target mitochondria. These evidences suggest that viroporins constitute a new source of membrane-active sequences, worth exploring as potential leads for the development of bioactive peptides, and/or as targets for the development of antiviral compounds. © 2012 Bentham Science Publishers.
Identificadoresdoi: 10.2174/138920312804142165
issn: 1389-2037
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