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Solution structure of the severe acute respiratory syndrome-coronavirus heptad repeat 2 domain in the prefusion state.

Identifieur interne : 002325 ( PubMed/Curation ); précédent : 002324; suivant : 002326

Solution structure of the severe acute respiratory syndrome-coronavirus heptad repeat 2 domain in the prefusion state.

Auteurs : Susanna Hakansson-Mcreynolds [États-Unis] ; Shaokai Jiang ; Lijun Rong ; Michael Caffrey

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2006.

RBID : pubmed:16507566

Descripteurs français

English descriptors

KwdEn :
- Crystallography, X-Ray, Hemagglutinins, Viral, Humans, Membrane Glycoproteins (chemical synthesis), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Models, Molecular, Protein Conformation, Repetitive Sequences, Amino Acid (genetics), SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (metabolism), Solubility, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Viral Fusion Proteins (chemical synthesis), Viral Fusion Proteins (genetics), Viral Fusion Proteins (metabolism).
MESH :
- chemical , chemical synthesis : Membrane Glycoproteins, Viral Fusion Proteins.
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical : Hemagglutinins, Viral, Spike Glycoprotein, Coronavirus.
- chemistry : SARS Virus.
- genetics : Repetitive Sequences, Amino Acid, SARS Virus.
- metabolism : SARS Virus.
- Crystallography, X-Ray, Humans, Models, Molecular, Protein Conformation, Solubility.

Abstract

The envelope glycoprotein, termed the spike protein, of severe acute respiratory syndrome coronavirus (SARS-CoV) is known to mediate viral entry. Similar to other class 1 viral fusion proteins, the heptad repeat regions of SARS-CoV spike are thought to undergo conformational changes from a prefusion form to a subsequent post-fusion form that enables fusion of the viral and host membranes. Recently, the structure of a post-fusion form of SARS-CoV spike, which consists of isolated domains of heptad repeats 1 and 2 (HR1 and HR2), has been determined by x-ray crystallography. To date there is no structural information for the prefusion conformations of SARS-CoV HR1 and HR2. In this work we present the NMR structure of the HR2 domain (residues 1141-1193) from SARS-CoV (termed S2-HR2) in the presence of the co-solvent trifluoroethanol. We find that in the absence of HR1, S2-HR2 forms a coiled coil symmetric trimer with a complex molecular mass of 18 kDa. The S2-HR2 structure, which is the first example of the prefusion form of coronavirus envelope, supports the current model of viral membrane fusion and gives insight into the design of structure-based antagonists of SARS.

DOI: 10.1074/jbc.M601174200
PubMed: 16507566

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Le document en format XML

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<affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607, USA.</nlm:affiliation>
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<term>Membrane Glycoproteins (chemistry)</term>
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<term>Viral Envelope Proteins (genetics)</term>
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<term>Protéines de fusion virale (métabolisme)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Fusion Proteins</term>
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<term>Séquences répétées d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">The envelope glycoprotein, termed the spike protein, of severe acute respiratory syndrome coronavirus (SARS-CoV) is known to mediate viral entry. Similar to other class 1 viral fusion proteins, the heptad repeat regions of SARS-CoV spike are thought to undergo conformational changes from a prefusion form to a subsequent post-fusion form that enables fusion of the viral and host membranes. Recently, the structure of a post-fusion form of SARS-CoV spike, which consists of isolated domains of heptad repeats 1 and 2 (HR1 and HR2), has been determined by x-ray crystallography. To date there is no structural information for the prefusion conformations of SARS-CoV HR1 and HR2. In this work we present the NMR structure of the HR2 domain (residues 1141-1193) from SARS-CoV (termed S2-HR2) in the presence of the co-solvent trifluoroethanol. We find that in the absence of HR1, S2-HR2 forms a coiled coil symmetric trimer with a complex molecular mass of 18 kDa. The S2-HR2 structure, which is the first example of the prefusion form of coronavirus envelope, supports the current model of viral membrane fusion and gives insight into the design of structure-based antagonists of SARS.</div>
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<Abstract><AbstractText>The envelope glycoprotein, termed the spike protein, of severe acute respiratory syndrome coronavirus (SARS-CoV) is known to mediate viral entry. Similar to other class 1 viral fusion proteins, the heptad repeat regions of SARS-CoV spike are thought to undergo conformational changes from a prefusion form to a subsequent post-fusion form that enables fusion of the viral and host membranes. Recently, the structure of a post-fusion form of SARS-CoV spike, which consists of isolated domains of heptad repeats 1 and 2 (HR1 and HR2), has been determined by x-ray crystallography. To date there is no structural information for the prefusion conformations of SARS-CoV HR1 and HR2. In this work we present the NMR structure of the HR2 domain (residues 1141-1193) from SARS-CoV (termed S2-HR2) in the presence of the co-solvent trifluoroethanol. We find that in the absence of HR1, S2-HR2 forms a coiled coil symmetric trimer with a complex molecular mass of 18 kDa. The S2-HR2 structure, which is the first example of the prefusion form of coronavirus envelope, supports the current model of viral membrane fusion and gives insight into the design of structure-based antagonists of SARS.</AbstractText>
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Solution structure of the severe acute respiratory syndrome-coronavirus heptad repeat 2 domain in the prefusion state.

Solution structure of the severe acute respiratory syndrome-coronavirus heptad repeat 2 domain in the prefusion state.

Source :

Descripteurs français

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Abstract

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