Abstract
Triggering of the Hendra virus fusion (F) protein is required to initiate the conformational changes which drive membrane fusion, but the factors which control triggering remain poorly understood. Mutation of a histidine predicted to lie near the fusion peptide to alanine greatly reduced fusion despite wild-type cell surface expression levels, while asparagine substitution resulted in a moderate restoration in fusion levels. Slowed kinetics of six-helix bundle formation, as judged by sensitivity to heptad repeat B-derived peptides, was observed for all H372 mutants. These data suggest that side chain packing beneath the fusion peptide is an important regulator of Hendra virus F triggering.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Substitution
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Animals
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Chlorocebus aethiops
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Crystallography, X-Ray
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Hendra Virus / genetics
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Hendra Virus / pathogenicity
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Hendra Virus / physiology*
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Humans
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In Vitro Techniques
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Models, Molecular
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Mutagenesis, Site-Directed
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Mutant Proteins / chemistry
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Mutant Proteins / genetics
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Mutant Proteins / physiology
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Protein Conformation
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Structural Homology, Protein
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Transfection
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Vero Cells
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Viral Fusion Proteins / chemistry*
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Viral Fusion Proteins / genetics
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Viral Fusion Proteins / physiology*
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Virus Internalization
Substances
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Mutant Proteins
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Recombinant Proteins
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Viral Fusion Proteins