SrasV1, PubMed, Checkpoint, bibRecord, 002A15

Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus.

Identifieur interne : 002A15 ( PubMed/Checkpoint ); précédent : 002A14; suivant : 002A16

Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus.

Auteurs : Paolo Ingallinella [Italie] ; Elisabetta Bianchi ; Marco Finotto ; Giovanna Cantoni ; Debra M. Eckert ; Vinit M. Supekar ; Chiara Bruckmann ; Andrea Carfi ; Antonello Pessi

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2004.

RBID : pubmed:15161975

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Binding Sites, Humans, Molecular Sequence Data, Peptide Mapping, Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Repetitive Sequences, Amino Acid, SARS Virus (chemistry), SARS Virus (genetics), Sequence Homology, Amino Acid, Viral Fusion Proteins (chemistry), Viral Fusion Proteins (genetics).
MESH :
- chemical , chemistry : Recombinant Fusion Proteins, Viral Fusion Proteins.
- chemical , genetics : Recombinant Fusion Proteins, Viral Fusion Proteins.
- chemistry : SARS Virus.
- genetics : SARS Virus.
- Amino Acid Sequence, Binding Sites, Humans, Molecular Sequence Data, Peptide Mapping, Repetitive Sequences, Amino Acid, Sequence Homology, Amino Acid.

Abstract

The causative agent of a recent outbreak of an atypical pneumonia, known as severe acute respiratory syndrome (SARS), has been identified as a coronavirus (CoV) not belonging to any of the previously identified groups. Fusion of coronaviruses with the host cell is mediated by the envelope spike protein. Two regions within the spike protein of SARS-CoV have been identified, showing a high degree of sequence conservation with the other CoV, which are characterized by the presence of heptad repeats (HR1 and HR2). By using synthetic and recombinant peptides corresponding to the HR1 and HR2 regions, we were able to characterize the fusion-active complex formed by this novel CoV by CD, native PAGE, proteolysis protection analysis, and size-exclusion chromatography. HR1 and HR2 of SARS-CoV associate into an antiparallel six-helix bundle, with structural features typical of the other known class I fusion proteins. We have also mapped the specific boundaries of the region, within the longer HR1 domain, making contact with the shorter HR2 domain. Notably, the inner HR1 coiled coil is a stable alpha-helical domain even in the absence of interaction with the HR2 region. Inhibitors binding to HR regions of fusion proteins have been shown to be efficacious against many viruses, notably HIV. Our results may help in the design of anti-SARS therapeutics.

DOI: 10.1073/pnas.0402753101
PubMed: 15161975

Affiliations:

Italie

Links toward previous steps (curation, corpus...)

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pubmed:15161975

Le document en format XML

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<front><div type="abstract" xml:lang="en">The causative agent of a recent outbreak of an atypical pneumonia, known as severe acute respiratory syndrome (SARS), has been identified as a coronavirus (CoV) not belonging to any of the previously identified groups. Fusion of coronaviruses with the host cell is mediated by the envelope spike protein. Two regions within the spike protein of SARS-CoV have been identified, showing a high degree of sequence conservation with the other CoV, which are characterized by the presence of heptad repeats (HR1 and HR2). By using synthetic and recombinant peptides corresponding to the HR1 and HR2 regions, we were able to characterize the fusion-active complex formed by this novel CoV by CD, native PAGE, proteolysis protection analysis, and size-exclusion chromatography. HR1 and HR2 of SARS-CoV associate into an antiparallel six-helix bundle, with structural features typical of the other known class I fusion proteins. We have also mapped the specific boundaries of the region, within the longer HR1 domain, making contact with the shorter HR2 domain. Notably, the inner HR1 coiled coil is a stable alpha-helical domain even in the absence of interaction with the HR2 region. Inhibitors binding to HR regions of fusion proteins have been shown to be efficacious against many viruses, notably HIV. Our results may help in the design of anti-SARS therapeutics.</div>
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<Abstract><AbstractText>The causative agent of a recent outbreak of an atypical pneumonia, known as severe acute respiratory syndrome (SARS), has been identified as a coronavirus (CoV) not belonging to any of the previously identified groups. Fusion of coronaviruses with the host cell is mediated by the envelope spike protein. Two regions within the spike protein of SARS-CoV have been identified, showing a high degree of sequence conservation with the other CoV, which are characterized by the presence of heptad repeats (HR1 and HR2). By using synthetic and recombinant peptides corresponding to the HR1 and HR2 regions, we were able to characterize the fusion-active complex formed by this novel CoV by CD, native PAGE, proteolysis protection analysis, and size-exclusion chromatography. HR1 and HR2 of SARS-CoV associate into an antiparallel six-helix bundle, with structural features typical of the other known class I fusion proteins. We have also mapped the specific boundaries of the region, within the longer HR1 domain, making contact with the shorter HR2 domain. Notably, the inner HR1 coiled coil is a stable alpha-helical domain even in the absence of interaction with the HR2 region. Inhibitors binding to HR regions of fusion proteins have been shown to be efficacious against many viruses, notably HIV. Our results may help in the design of anti-SARS therapeutics.</AbstractText>
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Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus.

Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus.

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