Abstract
The conserved influenza virus hemagglutinin (HA) stem domain elicits cross-reactive antibodies, but epitopes in the globular head typically elicit strain-specific responses because of the hypervariability of this region. We isolated human monoclonal antibody 5J8, which neutralized a broad spectrum of 20th century H1N1 viruses and the 2009 pandemic H1N1 virus. Fine mapping of the interaction unexpectedly revealed a novel epitope between the receptor-binding pocket and the Ca₂ antigenic site on HA. This antibody exposes a new mechanism underlying broad immunity against H1N1 influenza viruses and identifies a conserved epitope that might be incorporated into engineered H1 virus vaccines.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adult
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Animals
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Antibodies, Monoclonal / immunology*
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Antibodies, Monoclonal / therapeutic use
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Antibodies, Neutralizing / immunology*
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Antibodies, Neutralizing / therapeutic use
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Antibodies, Viral / immunology*
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Antibodies, Viral / therapeutic use
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Body Weight
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Cell Line
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Cross Reactions*
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Disease Models, Animal
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Epitope Mapping
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Epitopes / immunology*
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Female
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Hemagglutinin Glycoproteins, Influenza Virus / immunology*
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Humans
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Mice
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Mice, Inbred BALB C
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Molecular Sequence Data
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Orthomyxoviridae Infections / drug therapy
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Rodent Diseases / drug therapy
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Sequence Analysis, DNA
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Survival Analysis
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Treatment Outcome
Substances
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Antibodies, Monoclonal
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Antibodies, Neutralizing
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Antibodies, Viral
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Epitopes
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H1N1 virus hemagglutinin
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Hemagglutinin Glycoproteins, Influenza Virus
Associated data
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GENBANK/JF791168
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GENBANK/JF791169