SrasV1, Main, Curation, bibRecord, 003669

Interaction of a peptide from the pre-transmembrane domain of the severe acute respiratory syndrome coronavirus spike protein with phospholipid membranes.

Identifieur interne : 003669 ( Main/Curation ); précédent : 003668; suivant : 003670

Interaction of a peptide from the pre-transmembrane domain of the severe acute respiratory syndrome coronavirus spike protein with phospholipid membranes.

Auteurs : Jaime Guillén [Espagne] ; Miguel R. Moreno ; Ana J. Pérez-Berna ; Angela Bernabeu ; José Villalaín

Source :

The journal of physical chemistry. B [ 1520-6106 ] ; 2007.

RBID : pubmed:18020324

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Chromatography, Gel, Fluorescence Polarization, Membrane Glycoproteins (chemistry), Membranes, Artificial, Molecular Sequence Data, Peptides (chemistry), Phospholipids (chemistry), Spectroscopy, Fourier Transform Infrared, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry).
MESH :
- chemical , chemistry : Membrane Glycoproteins, Peptides, Phospholipids, Viral Envelope Proteins.
- Amino Acid Sequence, Chromatography, Gel, Fluorescence Polarization, Membranes, Artificial, Molecular Sequence Data, Spectroscopy, Fourier Transform Infrared, Spike Glycoprotein, Coronavirus.

Abstract

The severe acute respiratory syndrome 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 order to gain new insight into the protein membrane alteration leading to the viral fusion mechanism, a peptide pertaining to the putative pre-transmembrane domain (PTM) of the S glycoprotein has been studied by infrared and fluorescence spectroscopies regarding its structure, its ability to induce membrane leakage, aggregation, and fusion, as well as its affinity toward specific phospholipids. We demonstrate that the SARS-CoV PTM peptide binds to and interacts with phospholipid model membranes, and, at the same time, it adopts different conformations when bound to membranes of different compositions. As it has been already suggested for other viral fusion proteins such as HIV gp41, the region of the SARS-CoV protein where the PTM peptide resides could be involved in the merging of the viral and target cell membranes working synergistically with other membrane-active regions of the SARS-CoV S glycoprotein to heighten the fusion process and therefore might be essential for the assistance and enhancement of the viral and cell fusion process.

DOI: 10.1021/jp073675y
PubMed: 18020324

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Le document en format XML

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<term>Fluorescence Polarization</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membranes, Artificial</term>
<term>Molecular Sequence Data</term>
<term>Peptides (chemistry)</term>
<term>Phospholipids (chemistry)</term>
<term>Spectroscopy, Fourier Transform Infrared</term>
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<term>Glycoprotéines membranaires ()</term>
<term>Membrane artificielle</term>
<term>Peptides ()</term>
<term>Phospholipides ()</term>
<term>Polarisation de fluorescence</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Spectroscopie infrarouge à transformée de Fourier</term>
<term>Séquence d'acides aminés</term>
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<term>Molecular Sequence Data</term>
<term>Spectroscopy, Fourier Transform Infrared</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Membrane artificielle</term>
<term>Peptides</term>
<term>Phospholipides</term>
<term>Polarisation de fluorescence</term>
<term>Protéines de l'enveloppe virale</term>
<term>Spectroscopie infrarouge à transformée de Fourier</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome 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 order to gain new insight into the protein membrane alteration leading to the viral fusion mechanism, a peptide pertaining to the putative pre-transmembrane domain (PTM) of the S glycoprotein has been studied by infrared and fluorescence spectroscopies regarding its structure, its ability to induce membrane leakage, aggregation, and fusion, as well as its affinity toward specific phospholipids. We demonstrate that the SARS-CoV PTM peptide binds to and interacts with phospholipid model membranes, and, at the same time, it adopts different conformations when bound to membranes of different compositions. As it has been already suggested for other viral fusion proteins such as HIV gp41, the region of the SARS-CoV protein where the PTM peptide resides could be involved in the merging of the viral and target cell membranes working synergistically with other membrane-active regions of the SARS-CoV S glycoprotein to heighten the fusion process and therefore might be essential for the assistance and enhancement of the viral and cell fusion process.</div>
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Interaction of a peptide from the pre-transmembrane domain of the severe acute respiratory syndrome coronavirus spike protein with phospholipid membranes.

Interaction of a peptide from the pre-transmembrane domain of the severe acute respiratory syndrome coronavirus spike protein with phospholipid membranes.

Source :

Descripteurs français

English descriptors

Abstract

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

Links to Exploration step

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