Cholesterol modulates the fusogenic activity of a membranotropic domain of the FIV glycoprotein gp36

Lipid composition of viral envelopes is usually rich in sphingolipids and cholesterol (CHOL). These components have a stiffening effect on the membrane, thus enhancing the energetic barrier to be overcome for its fusion with the T-cell plasma membrane, a fundamental step of the infection process. In...

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Autores principales: Vitiello, G., Fragneto, G., Petruk, A.A., Falanga, A., Galdiero, S., D'Ursi, A.M., Merlino, A., D'Errico, G.
Formato: JOUR
Materias:
Cell membranes
Glycoproteins
Molecular dynamics
Molecules
Peptides
Phospholipids
T-cells
Viruses
Energetic barriers
Immunodeficiency virus
Membrane interactions
Molecular dynamics simulations
Molecular mechanism
Neutron reflectivity
Phosphatidylcholine
Strong perturbations
Cholesterol
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_1744683X_v9_n28_p6442_Vitiello
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_1744683X_v9_n28_p6442_Vitiello2023-10-03T16:31:49Z Cholesterol modulates the fusogenic activity of a membranotropic domain of the FIV glycoprotein gp36 Vitiello, G. Fragneto, G. Petruk, A.A. Falanga, A. Galdiero, S. D'Ursi, A.M. Merlino, A. D'Errico, G. Cell membranes Glycoproteins Molecular dynamics Molecules Peptides Phospholipids T-cells Viruses Energetic barriers Immunodeficiency virus Membrane interactions Molecular dynamics simulations Molecular mechanism Neutron reflectivity Phosphatidylcholine Strong perturbations Cholesterol Lipid composition of viral envelopes is usually rich in sphingolipids and cholesterol (CHOL). These components have a stiffening effect on the membrane, thus enhancing the energetic barrier to be overcome for its fusion with the T-cell plasma membrane, a fundamental step of the infection process. In this work, we demonstrate that the octapeptide (C8) corresponding to the Trp 770-Ile777 sequence of the Feline Immunodeficiency Virus gp36 is highly effective in inducing the fusion of palmitoyl oleoyl phosphatidylcholine (POPC)/sphingomyelin (SM)/CHOL membranes. We analyze the molecular mechanism of the C8-membrane interactions combining Neutron Reflectivity (NR) and Electron Spin Resonance (ESR) experiments, and molecular dynamics simulations. A strict interplay among the different lipids in the peptide-induced fusion mechanism is highlighted. Since CHOL preferentially locates close to SM, POPC molecules remain relatively free to interact with the peptide, driving its positioning at the membrane interface. Here, C8 comes in contact with CHOL-interacting SM molecules, causing a strong perturbation of acyl chain ordering, which is a necessary condition for membrane fusion. Our findings suggest that CHOL rules, by an indirect mechanism, the activity of viral fusion glycoproteins. © The Royal Society of Chemistry 2013. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_1744683X_v9_n28_p6442_Vitiello
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cell membranes
Glycoproteins
Molecular dynamics
Molecules
Peptides
Phospholipids
T-cells
Viruses
Energetic barriers
Immunodeficiency virus
Membrane interactions
Molecular dynamics simulations
Molecular mechanism
Neutron reflectivity
Phosphatidylcholine
Strong perturbations
Cholesterol
spellingShingle Cell membranes
Glycoproteins
Molecular dynamics
Molecules
Peptides
Phospholipids
T-cells
Viruses
Energetic barriers
Immunodeficiency virus
Membrane interactions
Molecular dynamics simulations
Molecular mechanism
Neutron reflectivity
Phosphatidylcholine
Strong perturbations
Cholesterol
Vitiello, G.
Fragneto, G.
Petruk, A.A.
Falanga, A.
Galdiero, S.
D'Ursi, A.M.
Merlino, A.
D'Errico, G.
Cholesterol modulates the fusogenic activity of a membranotropic domain of the FIV glycoprotein gp36
topic_facet Cell membranes
Glycoproteins
Molecular dynamics
Molecules
Peptides
Phospholipids
T-cells
Viruses
Energetic barriers
Immunodeficiency virus
Membrane interactions
Molecular dynamics simulations
Molecular mechanism
Neutron reflectivity
Phosphatidylcholine
Strong perturbations
Cholesterol
description Lipid composition of viral envelopes is usually rich in sphingolipids and cholesterol (CHOL). These components have a stiffening effect on the membrane, thus enhancing the energetic barrier to be overcome for its fusion with the T-cell plasma membrane, a fundamental step of the infection process. In this work, we demonstrate that the octapeptide (C8) corresponding to the Trp 770-Ile777 sequence of the Feline Immunodeficiency Virus gp36 is highly effective in inducing the fusion of palmitoyl oleoyl phosphatidylcholine (POPC)/sphingomyelin (SM)/CHOL membranes. We analyze the molecular mechanism of the C8-membrane interactions combining Neutron Reflectivity (NR) and Electron Spin Resonance (ESR) experiments, and molecular dynamics simulations. A strict interplay among the different lipids in the peptide-induced fusion mechanism is highlighted. Since CHOL preferentially locates close to SM, POPC molecules remain relatively free to interact with the peptide, driving its positioning at the membrane interface. Here, C8 comes in contact with CHOL-interacting SM molecules, causing a strong perturbation of acyl chain ordering, which is a necessary condition for membrane fusion. Our findings suggest that CHOL rules, by an indirect mechanism, the activity of viral fusion glycoproteins. © The Royal Society of Chemistry 2013.
format JOUR
author Vitiello, G.
Fragneto, G.
Petruk, A.A.
Falanga, A.
Galdiero, S.
D'Ursi, A.M.
Merlino, A.
D'Errico, G.
author_facet Vitiello, G.
Fragneto, G.
Petruk, A.A.
Falanga, A.
Galdiero, S.
D'Ursi, A.M.
Merlino, A.
D'Errico, G.
author_sort Vitiello, G.
title Cholesterol modulates the fusogenic activity of a membranotropic domain of the FIV glycoprotein gp36
title_short Cholesterol modulates the fusogenic activity of a membranotropic domain of the FIV glycoprotein gp36
title_full Cholesterol modulates the fusogenic activity of a membranotropic domain of the FIV glycoprotein gp36
title_fullStr Cholesterol modulates the fusogenic activity of a membranotropic domain of the FIV glycoprotein gp36
title_full_unstemmed Cholesterol modulates the fusogenic activity of a membranotropic domain of the FIV glycoprotein gp36
title_sort cholesterol modulates the fusogenic activity of a membranotropic domain of the fiv glycoprotein gp36
url http://hdl.handle.net/20.500.12110/paper_1744683X_v9_n28_p6442_Vitiello
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AT fragnetog cholesterolmodulatesthefusogenicactivityofamembranotropicdomainofthefivglycoproteingp36
AT petrukaa cholesterolmodulatesthefusogenicactivityofamembranotropicdomainofthefivglycoproteingp36
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AT derricog cholesterolmodulatesthefusogenicactivityofamembranotropicdomainofthefivglycoproteingp36
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