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Open Access item 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-ISSNmetadata.dc.identifier.doi = DOI:1873-4294
Appears in Collections:(UBF) Artículos
(IBV) Artículos

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