Identification of the Membrane-Active Regions of the Severe Acute Respiratory Syndrome Coronavirus Spike Membrane Glycoprotein Using a 16/18-Mer Peptide Scan: Implications for the Viral Fusion Mechanism
Identifieur interne : 000D25 ( Ncbi/Curation ); précédent : 000D24; suivant : 000D26Identification of the Membrane-Active Regions of the Severe Acute Respiratory Syndrome Coronavirus Spike Membrane Glycoprotein Using a 16/18-Mer Peptide Scan: Implications for the Viral Fusion Mechanism
Auteurs : Jaime Guillén [Espagne] ; Ana J. Pérez-Berná [Espagne] ; Miguel R. Moreno [Espagne] ; José Villalaín [Espagne]Source :
- Journal of Virology [ 0022-538X ] ; 2005.
Descripteurs français
- KwdFr :
- Animaux, Banque de peptides, Données de séquences moléculaires, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (métabolisme), Humains, Membrane cellulaire (métabolisme), Peptides (), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme), Relation structure-activité, Suidae, Séquence d'acides aminés, Virus du SRAS (pathogénicité).
- MESH :
- métabolisme : Glycoprotéines membranaires, Membrane cellulaire, Protéines de l'enveloppe virale.
- pathogénicité : Virus du SRAS.
- Animaux, Banque de peptides, Données de séquences moléculaires, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Peptides, Protéines de l'enveloppe virale, Relation structure-activité, Suidae, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cell Membrane (metabolism), Humans, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Peptide Library, Peptides (chemistry), SARS Virus (pathogenicity), Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Swine, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- metabolism : Cell Membrane, Membrane Glycoproteins, Viral Envelope Proteins.
- pathogenicity : SARS Virus.
- Amino Acid Sequence, Animals, Humans, Membrane Fusion, Molecular Sequence Data, Peptide Library, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Swine.
Abstract
We have identified the membrane-active regions of the severe acute respiratory syndrome coronavirus (SARS CoV) spike glycoprotein by determining the effect on model membrane integrity of a 16/18-mer SARS CoV spike glycoprotein peptide library. By monitoring the effect of this peptide library on membrane leakage in model membranes, we have identified three regions on the SARS CoV spike glycoprotein with membrane-interacting capabilities: region 1, located immediately upstream of heptad repeat 1 (HR1) and suggested to be the fusion peptide; region 2, located between HR1 and HR2, which would be analogous to the loop domain of human immunodeficiency virus type 1; and region 3, which would correspond to the pretransmembrane region. The identification of these membrane-active regions, which are capable of modifying the biophysical properties of phospholipid membranes, supports their direct role in SARS CoV-mediated membrane fusion, as well as facilitating the future development of SARS CoV entry inhibitors.
Url:
DOI: 10.1128/JVI.79.3.1743-1752.2005
PubMed: 15650199
PubMed Central: 544113
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PMC:544113Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Identification of the Membrane-Active Regions of the Severe Acute Respiratory Syndrome Coronavirus Spike Membrane Glycoprotein Using a 16/18-Mer Peptide Scan: Implications for the Viral Fusion Mechanism</title>
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<term>Membrane Glycoproteins (metabolism)</term>
<term>Molecular Sequence Data</term>
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<term>Données de séquences moléculaires</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
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<term>Peptides ()</term>
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<term>Suidae</term>
<term>Séquence d'acides aminés</term>
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<term>Peptides</term>
<term>Viral Envelope Proteins</term>
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<term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Membrane cellulaire</term>
<term>Protéines de l'enveloppe virale</term>
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<term>Animals</term>
<term>Humans</term>
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<term>Molecular Sequence Data</term>
<term>Peptide Library</term>
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<term>Structure-Activity Relationship</term>
<term>Swine</term>
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<term>Banque de peptides</term>
<term>Données de séquences moléculaires</term>
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<front><div type="abstract" xml:lang="en"><p>We have identified the membrane-active regions of the severe acute respiratory syndrome coronavirus (SARS CoV) spike glycoprotein by determining the effect on model membrane integrity of a 16/18-mer SARS CoV spike glycoprotein peptide library. By monitoring the effect of this peptide library on membrane leakage in model membranes, we have identified three regions on the SARS CoV spike glycoprotein with membrane-interacting capabilities: region 1, located immediately upstream of heptad repeat 1 (HR1) and suggested to be the fusion peptide; region 2, located between HR1 and HR2, which would be analogous to the loop domain of human immunodeficiency virus type 1; and region 3, which would correspond to the pretransmembrane region. The identification of these membrane-active regions, which are capable of modifying the biophysical properties of phospholipid membranes, supports their direct role in SARS CoV-mediated membrane fusion, as well as facilitating the future development of SARS CoV entry inhibitors.</p>
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