SrasV1, Main, Exploration, bibRecordById, pubmed:18489147

Structural and dynamic characterization of the interaction of the putative fusion peptide of the S2 SARS-CoV virus protein with lipid membranes.

Identifieur interne : 003008 ( Main/Exploration ); précédent : 003007; suivant : 003009

Structural and dynamic characterization of the interaction of the putative fusion peptide of the S2 SARS-CoV virus protein with lipid membranes.

Auteurs : Jaime Guillén [Espagne] ; Rodrigo F M. De Almeida ; Manuel Prieto ; José Villalaín

Source :

The journal of physical chemistry. B [ 1520-6106 ] ; 2008.

RBID : pubmed:18489147

Descripteurs français

English descriptors

KwdEn :
- Kinetics, Lipids (chemistry), Membrane Fusion, Membrane Glycoproteins (chemistry), Protein Conformation, Spectrometry, Fluorescence, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry).
MESH :
- chemical , chemistry : Lipids, Membrane Glycoproteins, Viral Envelope Proteins.
- Kinetics, Membrane Fusion, Protein Conformation, Spectrometry, Fluorescence, Spike Glycoprotein, Coronavirus.

Abstract

The SARS coronavirus (SARS-CoV) envelope spike (S) glycoprotein, a Class I viral fusion protein, is responsible for the fusion between the membranes of the virus and the target cell. In the present work, we report a study of the binding and interaction with model membranes of a peptide pertaining to the putative fusion domain of SARS-CoV, SARS FP, as well as the structural changes that take place in both the phospholipid and the peptide molecules upon this interaction. From fluorescence and infrared spectroscopies, the peptide ability to induce membrane leakage, aggregation and fusion, as well as its affinity toward specific phospholipids, was assessed. We demonstrate that SARS FP strongly partitions into phospholipid membranes, more specifically with those containing negatively charged phospholipids, increasing the water penetration depth and displaying membrane-activity modulated by the lipid composition of the membrane. Interestingly, peptide organization is different depending if SARS FP is in water or bound to the membrane. These data suggest that SARS FP could be involved in the merging of the viral and target cell membranes by perturbing the membrane outer leaflet phospholipids and specifically interacting with negatively charged phospholipids located in the inner leaflet.

DOI: 10.1021/jp7118229
PubMed: 18489147

Affiliations:

Espagne

Le document en format XML

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<term>Glycoprotéines membranaires ()</term>
<term>Lipides ()</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Spectrométrie de fluorescence</term>
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<front><div type="abstract" xml:lang="en">The SARS coronavirus (SARS-CoV) envelope spike (S) glycoprotein, a Class I viral fusion protein, is responsible for the fusion between the membranes of the virus and the target cell. In the present work, we report a study of the binding and interaction with model membranes of a peptide pertaining to the putative fusion domain of SARS-CoV, SARS FP, as well as the structural changes that take place in both the phospholipid and the peptide molecules upon this interaction. From fluorescence and infrared spectroscopies, the peptide ability to induce membrane leakage, aggregation and fusion, as well as its affinity toward specific phospholipids, was assessed. We demonstrate that SARS FP strongly partitions into phospholipid membranes, more specifically with those containing negatively charged phospholipids, increasing the water penetration depth and displaying membrane-activity modulated by the lipid composition of the membrane. Interestingly, peptide organization is different depending if SARS FP is in water or bound to the membrane. These data suggest that SARS FP could be involved in the merging of the viral and target cell membranes by perturbing the membrane outer leaflet phospholipids and specifically interacting with negatively charged phospholipids located in the inner leaflet.</div>
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Structural and dynamic characterization of the interaction of the putative fusion peptide of the S2 SARS-CoV virus protein with lipid membranes.

Structural and dynamic characterization of the interaction of the putative fusion peptide of the S2 SARS-CoV virus protein with lipid membranes.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

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