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Journal ArticleDOI

Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid

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.

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Book ChapterDOI

Sialylation of the Gram-Negative Bacterial Cell Surface

TL;DR: This chapter discusses the biological effects of sialylation, which mediate antiphagocytosis, anticomplement activity, and protection against bactericidal killing, and the potential to act with sialic acid binding immunoglobulinlike lectins on the surface of hematopoietic and immune system cells.

Role of Bovine Ileal Sub-epithelial Myofibroblasts and Epithelial Cells in Innate Immunity

Tirth Uprety
TL;DR: It is suggested that within the next few weeks, the water quality in this part of the world will improve significantly, and the quality of the water in this area will improve as well.
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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