SrasV1, Ncbi, Merge, bibRecord, 000638

Structural characterization of the SARS-coronavirus spike S fusion protein core.

Identifieur interne : 000638 ( Ncbi/Merge ); précédent : 000637; suivant : 000639

Structural characterization of the SARS-coronavirus spike S fusion protein core.

Auteurs : Brian Tripet [États-Unis] ; Megan W. Howard ; Michael Jobling ; Randall K. Holmes ; Kathryn V. Holmes ; Robert S. Hodges

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2004.

RBID : pubmed:14996844

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Base Sequence, Circular Dichroism, DNA Primers, Escherichia coli (genetics), Hemagglutinins, Viral (chemistry), Hemagglutinins, Viral (isolation & purification), Membrane Glycoproteins (chemical synthesis), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (isolation & purification), Molecular Sequence Data, Molecular Weight, Peptide Fragments (chemistry), Peptide Fragments (isolation & purification), Protein Conformation, Restriction Mapping, SARS Virus (chemistry), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemical synthesis), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (isolation & purification).
MESH :
- chemical , chemical synthesis : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , chemistry : Hemagglutinins, Viral, Membrane Glycoproteins, Peptide Fragments, Viral Envelope Proteins.
- chemical , isolation & purification : Hemagglutinins, Viral, Membrane Glycoproteins, Peptide Fragments, Viral Envelope Proteins.
- chemical : DNA Primers, Spike Glycoprotein, Coronavirus.
- chemistry : SARS Virus.
- genetics : Escherichia coli.
- Amino Acid Sequence, Base Sequence, Circular Dichroism, Molecular Sequence Data, Molecular Weight, Protein Conformation, Restriction Mapping.

Abstract

The spike (S) glycoprotein of coronaviruses mediates viral entry into host cells. It is a type 1 viral fusion protein that characteristically contains two heptad repeat regions, denoted HR-N and HR-C, that form coiled-coil structures within the ectodomain of the protein. Previous studies have shown that the two heptad repeat regions can undergo a conformational change from their native state to a 6-helix bundle (trimer of dimers), which mediates fusion of viral and host cell membranes. Here we describe the biophysical analysis of the two predicted heptad repeat regions within the severe acute respiratory syndrome coronavirus S protein. Our results show that in isolation the HR-N region forms a stable alpha-helical coiled coil that associates in a tetrameric state. The HR-C region in isolation formed a weakly stable trimeric coiled coil. When mixed together, the two peptide regions (HR-N and HR-C) associated to form a very stable alpha-helical 6-stranded structure (trimer of heterodimers). Systematic peptide mapping showed that the site of interaction between the HR-N and HR-C regions is between residues 916-950 of HR-N and residues 1151-1185 of HR-C. Additionally, interchain disulfide bridge experiments showed that the relative orientation of the HR-N and HR-C helices in the complex was antiparallel. Overall, the structure of the hetero-stranded complex is consistent with the structures observed for other type 1 viral fusion proteins in their fusion-competent state.

DOI: 10.1074/jbc.M400759200
PubMed: 14996844

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Le document en format XML

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<term>Circular Dichroism</term>
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<term>Escherichia coli (genetics)</term>
<term>Hemagglutinins, Viral (chemistry)</term>
<term>Hemagglutinins, Viral (isolation & purification)</term>
<term>Membrane Glycoproteins (chemical synthesis)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (isolation & purification)</term>
<term>Molecular Sequence Data</term>
<term>Molecular Weight</term>
<term>Peptide Fragments (chemistry)</term>
<term>Peptide Fragments (isolation & purification)</term>
<term>Protein Conformation</term>
<term>Restriction Mapping</term>
<term>SARS Virus (chemistry)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (chemical synthesis)</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (isolation & purification)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN</term>
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<term>Données de séquences moléculaires</term>
<term>Escherichia coli (génétique)</term>
<term>Fragments peptidiques ()</term>
<term>Fragments peptidiques (isolement et purification)</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (isolement et purification)</term>
<term>Glycoprotéines membranaires (synthèse chimique)</term>
<term>Hémagglutinines virales ()</term>
<term>Hémagglutinines virales (isolement et purification)</term>
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<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Virus du SRAS ()</term>
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<term>Membrane Glycoproteins</term>
<term>Peptide Fragments</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Hemagglutinins, Viral</term>
<term>Membrane Glycoproteins</term>
<term>Peptide Fragments</term>
<term>Viral Envelope Proteins</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>DNA Primers</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Fragments peptidiques</term>
<term>Glycoprotéines membranaires</term>
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<term>Protéines de l'enveloppe virale</term>
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<term>Base Sequence</term>
<term>Circular Dichroism</term>
<term>Molecular Sequence Data</term>
<term>Molecular Weight</term>
<term>Protein Conformation</term>
<term>Restriction Mapping</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term>
<term>Cartographie de restriction</term>
<term>Conformation des protéines</term>
<term>Dichroïsme circulaire</term>
<term>Données de séquences moléculaires</term>
<term>Fragments peptidiques</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Hémagglutinines virales</term>
<term>Masse moléculaire</term>
<term>Protéines de l'enveloppe virale</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
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<front><div type="abstract" xml:lang="en">The spike (S) glycoprotein of coronaviruses mediates viral entry into host cells. It is a type 1 viral fusion protein that characteristically contains two heptad repeat regions, denoted HR-N and HR-C, that form coiled-coil structures within the ectodomain of the protein. Previous studies have shown that the two heptad repeat regions can undergo a conformational change from their native state to a 6-helix bundle (trimer of dimers), which mediates fusion of viral and host cell membranes. Here we describe the biophysical analysis of the two predicted heptad repeat regions within the severe acute respiratory syndrome coronavirus S protein. Our results show that in isolation the HR-N region forms a stable alpha-helical coiled coil that associates in a tetrameric state. The HR-C region in isolation formed a weakly stable trimeric coiled coil. When mixed together, the two peptide regions (HR-N and HR-C) associated to form a very stable alpha-helical 6-stranded structure (trimer of heterodimers). Systematic peptide mapping showed that the site of interaction between the HR-N and HR-C regions is between residues 916-950 of HR-N and residues 1151-1185 of HR-C. Additionally, interchain disulfide bridge experiments showed that the relative orientation of the HR-N and HR-C helices in the complex was antiparallel. Overall, the structure of the hetero-stranded complex is consistent with the structures observed for other type 1 viral fusion proteins in their fusion-competent state.</div>
</front>
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<Abstract><AbstractText>The spike (S) glycoprotein of coronaviruses mediates viral entry into host cells. It is a type 1 viral fusion protein that characteristically contains two heptad repeat regions, denoted HR-N and HR-C, that form coiled-coil structures within the ectodomain of the protein. Previous studies have shown that the two heptad repeat regions can undergo a conformational change from their native state to a 6-helix bundle (trimer of dimers), which mediates fusion of viral and host cell membranes. Here we describe the biophysical analysis of the two predicted heptad repeat regions within the severe acute respiratory syndrome coronavirus S protein. Our results show that in isolation the HR-N region forms a stable alpha-helical coiled coil that associates in a tetrameric state. The HR-C region in isolation formed a weakly stable trimeric coiled coil. When mixed together, the two peptide regions (HR-N and HR-C) associated to form a very stable alpha-helical 6-stranded structure (trimer of heterodimers). Systematic peptide mapping showed that the site of interaction between the HR-N and HR-C regions is between residues 916-950 of HR-N and residues 1151-1185 of HR-C. Additionally, interchain disulfide bridge experiments showed that the relative orientation of the HR-N and HR-C helices in the complex was antiparallel. Overall, the structure of the hetero-stranded complex is consistent with the structures observed for other type 1 viral fusion proteins in their fusion-competent state.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tripet</LastName>
<ForeName>Brian</ForeName>
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<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, CO 80262, USA.</Affiliation>
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<ForeName>Megan W</ForeName>
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<name sortKey="Holmes, Kathryn V" sort="Holmes, Kathryn V" uniqKey="Holmes K" first="Kathryn V" last="Holmes">Kathryn V. Holmes</name>
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Structural characterization of the SARS-coronavirus spike S fusion protein core.

Structural characterization of the SARS-coronavirus spike S fusion protein core.

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Abstract

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