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
Antiviral activity of acidic polysaccharides from Coccomyxa gloeobotrydiformi, a green alga, against an in vitro human influenza A virus infection.
TL;DR: The acidic polysaccharide fraction from a green alga Coccomyxa gloeobotrydiformi was isolated and the antiviral action on an in vitro infection of influenza A virus was examined, suggested to exhibit the anti-influenza virus activity through preventing the interaction of virus and host cells.
Book ChapterDOI
Influenza neuraminidase as target for antivirals.
TL;DR: This chapter describes the function of neuraminidase (NA), its structure, how inhibitors are designed, and the current state of the development of new agents against influenza.
Journal ArticleDOI
On the rôle of human salivary micelle-like globules in bacterial agglutination.
TL;DR: Results indicate that the SMGs are important in the agglutination of streptococci, and that both calcium-dependent, electrostatic and hydrophobic interactions may be involved.
Journal ArticleDOI
Versatile intermediates in the selective modification of the amino function of 2-amino-2-deoxy-D-mannopyranose and the 3-position of 2-acetamido-2-deoxy-D-mannose: potential membrane modifiers in neoplastic control.
TL;DR: The most significant preclinical therapeutic finding was the antileukemic activity found in mice for tetra-O-acetyl-2-epi-streptozotocin (the acetylated alpha-mannosamine epimer of streptozOTocin).
Journal ArticleDOI
Specificity switching in virus-receptor complexes.
TL;DR: An improved understanding of the molecular details of this specificity switching in receptor binding will help to establish links between receptor tropism, spread, and disease.
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.
Related Papers (5)
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
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