Journal ArticleDOI
Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
William I. Weis,Jerry H. Brown,Stephen Cusack,Stephen Cusack,James C. Paulson,John J. Skehel,Don C. Wiley +6 more
TLDR
The three-dimensional structures of influenza virus haemagglutinins complexed with cell receptor analogues show sialic acids bound to a pocket of conserved amino acids surrounded by antibody-binding sites, suggesting that antibodies neutralize virus infectivity by preventing virus-to-cell binding.Abstract:
The three-dimensional structures of influenza virus haemagglutinins complexed with cell receptor analogues show sialic acids bound to a pocket of conserved amino acids surrounded by antibody-binding sites. Sialic acid fills the conserved pocket, demonstrating that it is the influenza virus receptor. The proximity of the antibody-binding sites suggests that antibodies neutralize virus infectivity by preventing virus-to-cell binding. The structures suggest approaches to the design of anti-viral drugs that could block attachment of viruses to cells.read more
Citations
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Journal ArticleDOI
Evolution and ecology of influenza A viruses.
TL;DR: Wild aquatic bird populations have long been considered the natural reservoir for influenza A viruses with virus transmission from these birds seeding other avian and mammalian hosts, but recent studies in bats have suggested other reservoir species may also exist.
Journal ArticleDOI
Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin
John J. Skehel,Don C. Wiley +1 more
TL;DR: Comparisons to the soluble N-ethyl-maleimide-sensitive factor attachment protein receptor (SNARE) protein complex of vesicle fusion suggests that these molecules are all in the fusion-activated conformation and that the juxtaposition of the membrane anchor and fusion peptide, a recurring feature, is involved in the fused mechanism.
Journal ArticleDOI
Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
TL;DR: Isolated variable domains may offer an alternative to monoclonal antibodies and serve as the key to building high-affinity human antibodies and the name 'single domain antibodies (dAbs)' is suggested for these antigen binding demands.
Journal ArticleDOI
1918 Influenza: the Mother of All Pandemics
TL;DR: In this paper, the authors discuss the public health implications of the Spanish influenza pandemic of 1918-1919, which caused ≈50 million deaths worldwide and remains an ominous warning to public health.
References
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Journal ArticleDOI
Amino acid sequences of haemagglutinins of influenza viruses of the H3 subtype isolated from horses.
TL;DR: The amino acid sequence of the haemagglutinin of A/equine/Miami/63 (H3N8), the prototype influenza virus of the H3 subtype from horses, is deduced from the nucleotide sequence of virus RNA.
Journal ArticleDOI
Wheat germ agglutinin dimers bind sialyloligosaccharides at four sites in solution: proton nuclear magnetic resonance temperature studies at 360 MHz.
K A Kronis,J P Carver +1 more
TL;DR: In this article, the authors reported the temperature dependence of the apparent bound shifts and apparent bound line widths of the N-acetyl, H3a, and H3e peaks.
Journal ArticleDOI
Multiple mechanisms of neutralization of animal viruses
TL;DR: It seems likely that any early function required for the establishment of infection is vulnerable to the action of antibody, and the mechanism of neutralization can be qualitatively affected by interactions between the virus, the cell receptor and the class of immunoglobulin.
Journal ArticleDOI
Evolution of the Hong Kong influenza A sub-type. Structural relationships between the haemagglutinin from A/duck/Ukraine/1/63 (Hav 7) and the Hong Kong (H3) haemagglutinins
C W Ward,T A Dopheide +1 more
TL;DR: The number of amino-acid-sequence differences suggest that the Hong Kong haemagglutinin gene did not come directly from A/duck/Ukraine/1/63 but from a virus derived from it by antigenic drift during the period 1963-1968.
Journal ArticleDOI
Relationship between mitogenic activity of influenza viruses and the receptor-binding specificity of their hemagglutinin molecules.
TL;DR: The results indicate that the receptor-binding specificity of the hemagglutinin plays a critical role in determining the mitogenic activity of influenza viruses.
Related Papers (5)
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
The Structure and Function of the Hemagglutinin Membrane Glycoprotein of Influenza Virus
Don C. Wiley,John J. Skehel +1 more
Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin
John J. Skehel,Don C. Wiley +1 more