Abstract
Nipah virus (NiV) and Hendra virus (HeV) are novel zoonotic members of the Paramyxoviridae family and are the prototypes for a newly designated genus, Genus Henipavirus. Recent studies have shown that paramyxovirus might adopt a similar mechanism of virus fusion-entry. Under this mechanism, the two highly conserved heptad repeat (HR) regions, HR1 and HR2, in the fusion (F) protein, seem to show characteristic structure in the fusion core: the formation of a 6-helix coiled-coil bundle. The three HR1s form the alpha-helix coiled-coil surrounded by three HR2s. In this study, the two HR regions of NiV or HeV were expressed in an Escherichia coli system as a single chain and the results do show that HR1 and HR2 interact with each other in both NiV and HeV and form typical 6-helix coiled-coil bundles. This provides the molecular basis of HR2 inhibition to NiV and HeV fusion as observed in an earlier report.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Chromatography, Gel
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Circular Dichroism
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Cross-Linking Reagents / chemistry
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DNA Primers / genetics
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Drug Stability
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Hendra Virus / genetics
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Hendra Virus / metabolism*
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Hot Temperature
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Membrane Fusion / physiology*
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Models, Molecular
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Molecular Sequence Data
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Molecular Weight
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Nipah Virus / genetics
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Nipah Virus / metabolism*
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Protein Structure, Secondary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Repetitive Sequences, Amino Acid
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Viral Fusion Proteins / chemistry
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Viral Fusion Proteins / genetics*
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Viral Fusion Proteins / isolation & purification
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Viral Fusion Proteins / metabolism*
Substances
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Cross-Linking Reagents
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DNA Primers
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Recombinant Proteins
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Viral Fusion Proteins