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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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Practical synthesis of d-[1-13C]mannose, l-[1-13C] and l-[6-13C]fucose

TL;DR: In this paper, a new method for the synthesis of [1-13 C]-labeled compounds via the corresponding olefin compounds, which are in turn derived from d -mannitol or l -arabinose by efficient introduction of 13 C, by the Wittig reaction using Ph 3 P 13 CH 3 I and n -BuLi.
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Antigenic variations of human influenza virus in Shiraz, Iran

TL;DR: The H3N2 subtype strains prevalent during the 2005/7 influenza outbreak in southern Iran demonstrated a drastic antigenic variation and differed from A/California/7/2004 vaccine strain.
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The therapeutic potential of sialylated Fc domains of human IgG.

TL;DR: In this article, the authors describe the development of molecular scaffolds based on the crystallizable fragment (Fc) region of immunoglobulin (Ig) G that deliver high-avidity binding to innate immune receptors, including sialic acid-dependent receptors.

Alternative approaches in the preparation and growth of influenza B vaccine viruses

TL;DR: A large number of influenza B antigens are present in all human vaccines, and increases in yields have been observed with increasing levels of influenza A viruses.
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.
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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.
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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.
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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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