Abstract
The 1918 "Spanish" influenza pandemic represents the largest recorded outbreak of any infectious disease. The crystal structure of the uncleaved precursor of the major surface antigen of the extinct 1918 virus was determined at 3.0 angstrom resolution after reassembly of the hemagglutinin gene from viral RNA fragments preserved in 1918 formalin-fixed lung tissues. A narrow avian-like receptor-binding site, two previously unobserved histidine patches, and a less exposed surface loop at the cleavage site that activates viral membrane fusion reveal structural features primarily found in avian viruses, which may have contributed to the extraordinarily high infectivity and mortality rates observed during 1918.
Publication types
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Historical Article
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Carbohydrate Conformation
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Cloning, Molecular
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Crystallography, X-Ray
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Glycosylation
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Hemagglutinin Glycoproteins, Influenza Virus / chemistry*
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Hemagglutinin Glycoproteins, Influenza Virus / metabolism
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Histidine / chemistry
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Histidine / metabolism
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History, 20th Century
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Humans
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Hydrogen Bonding
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Influenza A virus / classification
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Influenza A virus / immunology*
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Influenza A virus / pathogenicity
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Influenza, Human / epidemiology
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Influenza, Human / history
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Influenza, Human / virology
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Molecular Sequence Data
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Protein Conformation
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Protein Structure, Quaternary
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Receptors, Virus / metabolism
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Sialic Acids / metabolism
Substances
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Hemagglutinin Glycoproteins, Influenza Virus
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Receptors, Virus
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Sialic Acids
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hemagglutinin, avian influenza A virus
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hemagglutinin, human influenza A virus
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Histidine