Membrane-Active Peptides Derived from Picornavirus 2B Viroporin

Author(s): Silvia Sanchez-Martinez, Vanesa Madan, Luis Carrasco, Jose L. Nieva

Journal Name: Current Protein & Peptide Science

Volume 13 , Issue 7 , 2012

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Viruses 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 “-helix-turn--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.

Keywords: Enterovirus 2B, viroporins, peptide-lipid interactions, pore-forming peptides, peptide-targeting to mitochondria.

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Article Details

Year: 2012
Published on: 25 November, 2012
Page: [632 - 643]
Pages: 12
DOI: 10.2174/138920312804142165
Price: $65

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