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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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Citations
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Journal ArticleDOI

An H1‐H3 chimeric influenza virosome confers complete protection against lethal challenge with PR8 (H1N1) and X47 (H3N2) viruses in mice

TL;DR: The chimeric virosomes can be used as an innovative vaccine formulation to confer protection against a broad range of influenza viruses and has shown an excellent tolerability profile due to its biocompatibility and purity.
Journal ArticleDOI

In Vitro and In Vivo Antiviral Activity of Nylidrin by Targeting the Hemagglutinin 2-Mediated Membrane Fusion of Influenza A Virus.

TL;DR: It is discovered that nylidrin targets hemagglutinin 2 (HA2)-mediated membrane fusion by blocking conformational change of HA at acidic pH, and could provide a core chemical skeleton for the development of a direct-acting inhibitor of influenza A virus entry.
Journal ArticleDOI

Synthesis of methyl α-sialosides N-substituted with large alkanoyl groups, and investigation of their inhibition of agglutination of erythrocytes by influenza A virus

TL;DR: There appears to be a correlation between increased chain length and increased inhibition of virus-induced agglutination of erythrocytes, and these derivatives did not, however, show increased binding to BHA, a soluble form of the lectin hemagglutinin that is responsible for the attachment of virus to cell.
Patent

Canine influenza virus and related compositions and methods of use

TL;DR: In this article, the authors presented an isolated canine influenza virus of subtype H3N8 comprising an HA having SEQ ID NO: 4 or an amino acid sequence that is greater than 99% identical to Seq ID No: 4, with the proviso that the amino acids at positions 94 and 233 are identical to SEQ No. 4.
Book ChapterDOI

Membrane Proximity and Internal Binding in the Microbial Recognition of Host Cell Glycolipids: A Conceptual Discussion

TL;DR: The distinct development during the last few years of assay, separation and structural techniques for glycoconjugates, in combination with improved information in microbial molecular biology, is at present contributing with information on receptor characteristics that holds promise also for drug design.
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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