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
X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme.
Judith A. Kelly,Judith A. Kelly,Anita R. Sielecki,Brian D. Sykes,Michael N.G. James,David Phillips +5 more
TL;DR: The X-ray structure of the non-hydrolysed13 trisaccharide NAM-NAG-NAM bound in subsites B, C, D is presented and it is shown that the interpretation of the 2.5-Å resolution difference map does not involve distortion of this residue in site D.
Journal ArticleDOI
Role of Gangliosides in Reception of Influenza Virus
Lev D. Bergelson,Alla G. Bukrinskaya,Nina V. Prokazova,Galina I. Shaposhnikova,Sergey L. Kocharov,Valeriy P. Shevchenko,Galina V. Kornilaeva,Elena V. Fomina-Ageeva +7 more
TL;DR: It is suggested that GT1b gangliosides react specifically with the virus protein responsible for membrane fusion and thus are involved in virus penetration and delivery of the virus genome to the nuclei.
Journal ArticleDOI
Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units
TL;DR: A general mechanism in which the isolated charges on the various buried, desolvated ionic groups are stabilized by the polarized peptide units is proposed, which has broad application to processes requiring binding of uncompensated ions and charged ligands and stabilization of enzyme reaction charged intermediates, as well as activation of catalytic residues.
Journal ArticleDOI
Selection of influenza A virus adsorptive mutants by growth in the presence of a mixture of monoclonal antihemagglutinin antibodies.
TL;DR: Findings are consistent with the idea that the variants of influenza virus A/PR/8/34 were initially selected by virtue of their increased avidity for host cell receptors after they emerged under conditions of partial neutralization.
Journal ArticleDOI
Recognition of monovalent sialosides by influenza virus H3 hemagglutinin.
TL;DR: The results provide evidence that the previously reported specificity of the A/Memphis/102/72 hemagglutinin for the NeuAc alpha 2,6Gal sequence on cell surface receptors was due to differential affinity of the receptor binding pocket for sialoside sequences, apart from contributions due to the protein or lipid portions of the cell surface receptor.
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