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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/57892
Title: Membrane-transferring regions of gp41 as targets for HIV-1 fusion inhibition and viral neutralization
Authors: Huarte, Nerea; Lorizate, Maier; Pérez-Payá, Enrique ; Nieva, José L.
Issue Date: 1-Dec-2011
Publisher: Bentham Science Publishers
Citation: Current Topics in Medicinal Chemistry 11(24): 2985-96 (2011)
Abstract: The fusogenic function of HIV-1 gp41 transmembrane Env subunit relies on two different kinds of structural elements: i) a collapsible ectodomain structure (the hairpin or six-helix bundle) that opens and closes, and ii) two membrane- transferring regions (MTRs), the fusion peptide (FP) and the membrane-proximal external region (MPER), which ensure coupling of hairpin closure to apposition and fusion of cell and viral membranes. The isolation of naturally produced short peptides and neutralizing IgG-s, that interact with FP and MPER, respectively, and block viral infection, suggests that these conserved regions might represent useful targets for clinical intervention. Furthermore, MTR-derived peptides have been shown to be membrane-active. Here, it is discussed the potential use of these molecules and how the analysis of their membrane activity in vitro could contribute to the development of HIV fusion inhibitors and effective immunogens
Description: 12 páginas, 4 figuras
Publisher version (URL): http://www.benthamdirect.org/pages/content.php?CTMC/2011/00000011/00000024/0004R
URI: http://hdl.handle.net/10261/57892
ISSN: 1568-0266
E-ISSN: 1873-4294
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