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/Exploration ); précédent : 003668; suivant : 003670Interaction 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 VillalaínSource :
- The journal of physical chemistry. B [ 1520-6106 ] ; 2007.
Descripteurs français
- KwdFr :
- Chromatographie sur gel, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Membrane artificielle, Peptides (), Phospholipides (), Polarisation de fluorescence, Protéines de l'enveloppe virale (), Spectroscopie infrarouge à transformée de Fourier, Séquence d'acides aminés.
- MESH :
- Chromatographie sur gel, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Membrane artificielle, Peptides, Phospholipides, Polarisation de fluorescence, Protéines de l'enveloppe virale, Spectroscopie infrarouge à transformée de Fourier, Séquence d'acides aminés.
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 :
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
Affiliations:
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Le document en format XML
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<term>Phospholipides ()</term>
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<term>Peptides</term>
<term>Phospholipides</term>
<term>Polarisation de fluorescence</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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