Abstract
Paramyxovirus-mediated membrane fusion usually requires an interaction between the viral-attachment and -fusion proteins. The mechanism by which this interaction regulates fusion differs between paramyxoviruses that bind to sialic acid-containing receptors and those that recognize specific proteins. The recently solved structure of the globular head of the measles virus hemagglutinin suggests that this difference might be related to the location of the receptor-binding sites on the attachment proteins of the two classes of paramyxoviruses.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Animals
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Binding Sites / genetics*
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HN Protein / chemistry
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HN Protein / metabolism
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Hemagglutinins, Viral / chemistry
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Hemagglutinins, Viral / metabolism
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Humans
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Measles virus / metabolism
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Measles virus / pathogenicity*
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Membrane Fusion*
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Newcastle disease virus / metabolism
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Newcastle disease virus / pathogenicity*
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Receptors, Virus / chemistry
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Receptors, Virus / metabolism*
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Viral Proteins / chemistry
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Viral Proteins / metabolism
Substances
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HN Protein
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Hemagglutinins, Viral
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Receptors, Virus
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Viral Proteins