English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/113889
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


Membrane-active peptides derived from picornavirus 2B viroporin

AuthorsSánchez-Martínez, Silvia; Madan, Vanesa; Carrasco Llamas, Luis ; Nieva, José Luis
KeywordsPeptide-targeting to mitochondria
Pore-forming peptides
Peptide-lipid interactions
Enterovirus 2B
Issue Date2012
PublisherBentham Science Publishers
CitationCurrent Protein and Peptide Science 13: 632- 643 (2012)
AbstractViruses 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.
Identifiersdoi: 10.2174/138920312804142165
issn: 1389-2037
Appears in Collections:(CBM) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.