Abstract
Measles virus (MV) entry requires at least 2 viral proteins, the hemagglutinin (H) and fusion (F) proteins. We describe the rescue and characterization of a measles virus with a specific mutation in the stalk region of H (I98A) that is able to bind normally to cells but infects at a lower rate than the wild type due to a reduction in fusion triggering. The mutant H protein binds to F more avidly than the parent H protein does, and the corresponding virus is more sensitive to inhibition by fusion-inhibitory peptide. We show that after binding of MV to its receptor, H-F dissociation is required for productive infection.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Substitution
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Animals
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Cell Line
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Chlorocebus aethiops
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Giant Cells / virology
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Hemagglutinins, Viral / chemistry
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Hemagglutinins, Viral / genetics*
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Hemagglutinins, Viral / physiology
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Humans
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Measles virus / genetics*
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Measles virus / pathogenicity*
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Measles virus / physiology
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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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Mutation, Missense*
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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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Hemagglutinins, Viral
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Mutant Proteins
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Viral Fusion Proteins
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hemagglutinin protein G, measles virus