SrasV1, PubMed, Checkpoint, bibRecord, 001B77

Characterization of the prefusion and transition states of severe acute respiratory syndrome coronavirus S2-HR2.

Identifieur interne : 001B77 ( PubMed/Checkpoint ); précédent : 001B76; suivant : 001B78

Characterization of the prefusion and transition states of severe acute respiratory syndrome coronavirus S2-HR2.

Auteurs : Susanna Mcreynolds [États-Unis] ; Shaokai Jiang ; Ying Guo ; Jessica Celigoy ; Christine Schar ; Lijun Rong ; Michael Caffrey

Source :

Biochemistry [ 1520-4995 ] ; 2008.

RBID : pubmed:18540634

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Circular Dichroism, Glycoproteins (chemistry), Glycoproteins (genetics), Glycoproteins (metabolism), Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Structure, Quaternary, SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (metabolism), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism), Virus Internalization.
MESH :
- chemical , chemistry : Glycoproteins, Viral Proteins.
- chemical , genetics : Glycoproteins, Viral Proteins.
- chemical , metabolism : Glycoproteins, Viral Proteins.
- chemistry : SARS Virus.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- Amino Acid Sequence, Circular Dichroism, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Structure, Quaternary, Virus Internalization.

Abstract

The envelope glycoproteins of the class I family, which include human immunodeficiency virus (HIV), influenza, and severe acute respiratory syndrome coronavirus (SARS-CoV), mediate viral entry by first binding to their cellular receptors and subsequently inducing fusion of the viral and cellular membranes. In the case of SARS-CoV, heptad repeat domains of the envelope glycoprotein, termed S2-HR1 and S2-HR2, are thought to undergo structural changes from a prefusion state, in which S2-HR1 and S2-HR2 do not interact, to a postfusion state in which S2-HR1 and S2-HR2 associate to form a six-helix bundle. In the present work, the structural and dynamic properties of S2-HR2 have been characterized. Evidence is presented for an equilibrium between a structured trimer thought to represent a prefusion state and an ensemble of unstructured monomers thought to represent a novel transition state. A model for viral entry is presented in which S2-HR2 is in a dynamic equilibrium between an ensemble of unstructured monomers in the transition state and a structured trimer in the prefusion state. Conversion from the prefusion state to the postfusion state requires passage through the transition state, a state that may give insight into the design of structure-based antagonists of SARS-CoV in particular, as well as other enveloped viruses in general.

DOI: 10.1021/bi800622t
PubMed: 18540634

Affiliations:

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pubmed:18540634

Le document en format XML

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<front><div type="abstract" xml:lang="en">The envelope glycoproteins of the class I family, which include human immunodeficiency virus (HIV), influenza, and severe acute respiratory syndrome coronavirus (SARS-CoV), mediate viral entry by first binding to their cellular receptors and subsequently inducing fusion of the viral and cellular membranes. In the case of SARS-CoV, heptad repeat domains of the envelope glycoprotein, termed S2-HR1 and S2-HR2, are thought to undergo structural changes from a prefusion state, in which S2-HR1 and S2-HR2 do not interact, to a postfusion state in which S2-HR1 and S2-HR2 associate to form a six-helix bundle. In the present work, the structural and dynamic properties of S2-HR2 have been characterized. Evidence is presented for an equilibrium between a structured trimer thought to represent a prefusion state and an ensemble of unstructured monomers thought to represent a novel transition state. A model for viral entry is presented in which S2-HR2 is in a dynamic equilibrium between an ensemble of unstructured monomers in the transition state and a structured trimer in the prefusion state. Conversion from the prefusion state to the postfusion state requires passage through the transition state, a state that may give insight into the design of structure-based antagonists of SARS-CoV in particular, as well as other enveloped viruses in general.</div>
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Characterization of the prefusion and transition states of severe acute respiratory syndrome coronavirus S2-HR2.

Characterization of the prefusion and transition states of severe acute respiratory syndrome coronavirus S2-HR2.

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Descripteurs français

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Abstract

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