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
Functional and structural analysis of the sialic acid-binding domain of rotaviruses.
TL;DR: Alanine substitutions for tyrosines 155 and 188 and for serine 190 are suggested to play an essential role in the SA-binding activity of the protein, presumably by interacting directly with the SA molecule.
Book ChapterDOI
Receptor structure, binding, and cell entry of arenaviruses.
TL;DR: In order for a virus to infect and replicate within the cells of its host, it must first gain entry into them by the attachment of virus particles to the host cell surface and subsequent transfer of viral nucleic acids and associated proteins into the cell cytoplasm.
Journal ArticleDOI
Hemagglutinin specificity and neuraminidase coding capacity of neuraminidase-deficient influenza viruses.
TL;DR: It appears that the role of NA in influenza infection is to remove sialic acid from the HA rather than to destroy receptors on cells, in contrast to the ease of selection of NA-deficient mutants from the H1N9 virus.
Journal ArticleDOI
Use of sialic acid analogues to define functional groups involved in binding to the influenza virus hemagglutinin
Sørge Kelm,James C. Paulson,Ursula Rose,Reinhard Brossmer,Walther Schmid,Babasaheb P. Bandgar,Erwin Schreiner,Michael Hartmann,Erich Zbiral +8 more
TL;DR: The functional groups of the nine-carbon sialic acid molecule which interact with the hemagglutinin and contribute to the affinity of this sugar to the protein are elucidated to help develop novel compounds which bind more avidly to the influenza virus hemag GLUTinin.
Journal ArticleDOI
Targeting B cell responses in universal influenza vaccine design.
TL;DR: New strategies to design the influenza vaccine rely on selectively inducing broadly neutralizing antibodies that are specific for highly conserved viral epitopes, taking us away from the limited range of protection provided by current seasonal influenza vaccines and towards a future with a pan-influenza vaccine capable of providing universal strain coverage.
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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