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
Self-assembled artificial viral capsids bearing coiled-coils at the surface
Seiya Fujita,Kazunori Matsuura +1 more
TL;DR: Dynamic light scattering measurements and transmission electron microscopy images revealed that the β-annulus-coiled-coil-B peptide self-assembled into spherical structures of about 50 nm in 10 mM Tris-HCl buffer.
Journal ArticleDOI
Cardiac glycosides decrease influenza virus replication by inhibiting cell protein translational machinery
Luciano Amarelle,Luciano Amarelle,Jeremy Katzen,Jeremy Katzen,Masahiko Shigemura,Lynn C. Welch,Hector R. Cajigas,Christin Peteranderl,Diego Celli,Susanne Herold,Susanne Herold,Emilia Lecuona,Jacob I. Sznajder +12 more
TL;DR: Evidence is provided that the inhibition of the Na-K-ATPase by CGs decreases influenza A viral replication by modulating the cell protein translational machinery and results in a modest survival benefit in mice.
Journal ArticleDOI
Viral Membrane Fusion and the Transmembrane Domain.
TL;DR: This work summarizes developments made in the past decade that have contributed to the understanding of the transmembrane region of viral fusion proteins, highlighting not only their critical role in the membrane fusion process, but further demonstrating their involvement in several aspects of the viral lifecycle.
Journal ArticleDOI
Inhibition of influenza-virus-induced cytopathy by sialylglycoconjugates.
TL;DR: The results suggest that the viral hemagglutinin recognizes exogenous sialyloligosaccharide expressed on MDCK cells, since introduction of the hydrophobic moiety to oligosACcharides might cause micelle formation.
Journal ArticleDOI
Residue Y161 of influenza virus hemagglutinin is involved in viral recognition of sialylated complexes from different hosts.
Minxiu Wang,Donna M. Tscherne,Christopher McCullough,Michael Caffrey,Adolfo García-Sastre,Lijun Rong +5 more
TL;DR: The results demonstrate that Y161 is a critical residue involved in recognition of different SA species and may play a role in determining influenza virus host tropism.
References
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Journal ArticleDOI
The thiobarbituric acid assay of sialic acids.
TL;DR: This chapter discusses the different aspects of thiobarbituric acid assay of sialic acid, which is suitable for measuring the release of bound sialoic acid by sialidase and hydrolysis of sIALic acid-containing material must be carried out for the measurement of total sialsic acids.
Journal ArticleDOI
Areas, volumes, packing and protein structure.
TL;DR: This review is concerned with the packing of groups of atoms in proteins and with the area of solvent-protein interfaces.
Journal ArticleDOI
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
TL;DR: The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-sheet is positioned on top of this stem.
Journal ArticleDOI
Aromatic-aromatic interaction: a mechanism of protein structure stabilization
TL;DR: Analysis of neighboring aromatic groups in four biphenyl peptides or peptide analogs and 34 proteins reveals a specific aromatic-aromatic interaction that helps stabilize tertiary structure, and 20 percent stabilize quaternary structure.
Journal ArticleDOI
Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
TL;DR: Four ‘antigenic sites’ on the three-dimensional structure of the influenza haemagglutinin are identified and at least one amino acid substitution in each site seems to be required for the production of new epidemic strains between 1968 and 1975.
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Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
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