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Abstract:

A wealth of evidence indicates that lipid rafts are involved in the fusion of the viral lipid envelope with the target cell membrane. However, the interplay between these sterol- and sphingolipid-enriched ordered domains and viral fusion glycoproteins has not yet been clarified. In this work we investigate the molecular mechanism by which a membranotropic fragment of the glycoprotein gH of the Herpes Simplex Virus (HSV) type I (gH625) drives fusion of lipid bilayers formed by palmitoyl oleoyl phosphatidylcholine (POPC)-sphingomyelin (SM)-cholesterol (CHOL) (1:1:1 wt/wt/wt), focusing on the role played by each component. The comparative analysis of the liposome fusion assays, Dynamic Light Scattering (DLS), spectrofluorimetry, Neutron Reflectivity (NR) and Electron Spin Resonance (ESR) experiments, and Molecular Dynamics (MD) simulations shows that CHOL is fundamental for liposome fusion to occur. In detail, CHOL stabilizes the gH625-bilayer association by specific interactions with the peptide Trp residue. The interaction with gH625 causes an increased order of the lipid acyl chains, whose local rotational motion is significantly hampered. SM plays only a minor role in the process, favoring the propagation of lipid perturbation to the bilayer inner core. The stiffening of the peptide-interacting bilayer leaflet results in an asymmetric perturbation of the membrane, which is locally destabilized thus favoring fusion events. Our results show that viral fusion glycoproteins are optimally suited to exert a high fusogenic activity on lipid rafts and support the relevance of cholesterol as a key player of membrane-related processes. © The Royal Society of Chemistry.2015.

Registro:

Documento: Artículo
Título:Fusion of raft-like lipid bilayers operated by a membranotropic domain of the HSV-type i glycoprotein gH occurs through a cholesterol-dependent mechanism
Autor:Vitiello, G.; Falanga, A.; Petruk, A.A.; Merlino, A.; Fragneto, G.; Paduano, L.; Galdiero, S.; D'Errico, G.
Filiación:Department of Chemical, Materials and Production Engineering, University of Naples federico II, Piazzale Tecchio 80, Naples, 80125, Italy
CSGI, Consorzio Interuniversitario per Lo Sviluppo Dei Sistemi A Grande Interfase, via della Lastruccia 3, SestoFiorentino,Florence, 50019, Italy
Department of Pharmacy, DFM Scarl and Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples federico II, Via Mezzocannone 16, Naples, 80134, Italy
Departamento de Quimica Inorganica, Analitica y Quimica Fisica/INQUIMAE-CONICET, University of Buenos Aires, Buenos Aires, Argentina
Department of Chemical Sciences, University of Naples federico II Monte sant'Angelo, Naples, 80126, Italy
Istituto di Biostrutture e Bioimmagini-CNR, Via Mezzocannone 16, Naples, 80134, Italy
Institut Laue-Langevin, BP 156, Grenoble, 38042, France
Palabras clave:Association reactions; Cell membranes; Cholesterol; Cytology; Dynamic light scattering; Electron spin resonance spectroscopy; Glycoproteins; Light scattering; Magnetic moments; Molecular dynamics; Peptides; Phospholipids; Spin dynamics; Viruses; Asymmetric perturbations; Comparative analysis; Herpes simplex virus; Molecular dynamics simulations; Molecular mechanism; Neutron reflectivity; Phosphatidylcholine; Specific interaction; Lipid bilayers; Simplexvirus; 1-palmitoyl-2-oleoylphosphatidylcholine; cholesterol; gH625 peptide, Herpes simplex virus type I; glycoprotein; lipid bilayer; peptide; phosphatidylcholine; sphingomyelin; virus envelope protein; virus protein; chemistry; lipid bilayer; molecular dynamics; protein tertiary structure; Cholesterol; Glycoproteins; Lipid Bilayers; Molecular Dynamics Simulation; Peptides; Phosphatidylcholines; Protein Structure, Tertiary; Sphingomyelins; Viral Envelope Proteins; Viral Proteins
Año:2015
Volumen:11
Número:15
Página de inicio:3003
Página de fin:3016
DOI: http://dx.doi.org/10.1039/c4sm02769h
Título revista:Soft Matter
Título revista abreviado:Soft Matter
ISSN:1744683X
CODEN:SMOAB
CAS:cholesterol, 57-88-5; phosphatidylcholine, 55128-59-1, 8002-43-5; sphingomyelin, 85187-10-6; 1-palmitoyl-2-oleoylphosphatidylcholine; Cholesterol; gH625 peptide, Herpes simplex virus type I; Glycoproteins; Lipid Bilayers; Peptides; Phosphatidylcholines; Sphingomyelins; Viral Envelope Proteins; Viral Proteins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1744683X_v11_n15_p3003_Vitiello

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Citas:

---------- APA ----------
Vitiello, G., Falanga, A., Petruk, A.A., Merlino, A., Fragneto, G., Paduano, L., Galdiero, S.,..., D'Errico, G. (2015) . Fusion of raft-like lipid bilayers operated by a membranotropic domain of the HSV-type i glycoprotein gH occurs through a cholesterol-dependent mechanism. Soft Matter, 11(15), 3003-3016.
http://dx.doi.org/10.1039/c4sm02769h
---------- CHICAGO ----------
Vitiello, G., Falanga, A., Petruk, A.A., Merlino, A., Fragneto, G., Paduano, L., et al. "Fusion of raft-like lipid bilayers operated by a membranotropic domain of the HSV-type i glycoprotein gH occurs through a cholesterol-dependent mechanism" . Soft Matter 11, no. 15 (2015) : 3003-3016.
http://dx.doi.org/10.1039/c4sm02769h
---------- MLA ----------
Vitiello, G., Falanga, A., Petruk, A.A., Merlino, A., Fragneto, G., Paduano, L., et al. "Fusion of raft-like lipid bilayers operated by a membranotropic domain of the HSV-type i glycoprotein gH occurs through a cholesterol-dependent mechanism" . Soft Matter, vol. 11, no. 15, 2015, pp. 3003-3016.
http://dx.doi.org/10.1039/c4sm02769h
---------- VANCOUVER ----------
Vitiello, G., Falanga, A., Petruk, A.A., Merlino, A., Fragneto, G., Paduano, L., et al. Fusion of raft-like lipid bilayers operated by a membranotropic domain of the HSV-type i glycoprotein gH occurs through a cholesterol-dependent mechanism. Soft Matter. 2015;11(15):3003-3016.
http://dx.doi.org/10.1039/c4sm02769h