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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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
The crystal structure of N-acetylneuraminic acid methyl ester monohydrate
TL;DR: In this paper, the structure of the methyl ester of N-acetylneuraminic acid monohydrate has been determined from three-dimensional X-ray diffraction data, and the structure was solved using the tangent formula and refined by block-diagonal least-squares techniques to R=0.042.
Journal ArticleDOI
Receptor binding characteristics of strains of the influenza Hong Kong subtype, using a periodate sensitivity test.
TL;DR: The periodate sensitivity test, involving treatment of fowl erythrocytes with varying concentrations of potassium periodate, could prove to be a useful tool in identifying particular residues in the haemagglutinin molecule which influence binding to the cellular receptor.
Journal ArticleDOI
The refinement of the haemagglutinin membrane glycoprotein of influenza virus
TL;DR: The crystal structure of the haemagglutinin glycoprotein, a trimer from the membrane of influenza virus, has been refined at 3.0 A resolution to an R ≥ 20.4% as discussed by the authors.
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
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Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin
John J. Skehel,Don C. Wiley +1 more