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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Antiidiotypic antibodies as probes for the Sindbis virus receptor
TL;DR: It is suggested that the alphaviruses use a number of distinguishable receptors which differ depending on the host and the tissue, and in chicken cells the 63,000 molecular weight protein may be one of them.
Journal ArticleDOI
Antiviral Polymers: Past Approaches and Future Possibilities
TL;DR: Treating a viral disease is no simple feat, with drug resistance, latent reservoirs in the body, emerging novel viruses, and a frequent lack of specific treatments all complicate antiviral therapy.
Journal ArticleDOI
Using viral vectors as gene transfer tools (Cell Biology and Toxicology Special Issue: ETCS-UK 1 day meeting on genetic manipulation of cells)
TL;DR: This review summarises some of the viral delivery systems routinely used to mediate gene transfer into cell lines, primary cell cultures and in whole animal models, and introduces the main categories of viral vectors.
Journal ArticleDOI
Multivalent glycoconjugates as vaccines and potential drug candidates
TL;DR: This review presents a concise report on the endeavors to potentially use multi- and polyvalent glycoconjugates as vaccines as well as anti-infectious and anti-inflammatory drug candidates.
Journal ArticleDOI
The flavivirus envelope protein E: isolation of a soluble form from tick-borne encephalitis virus and its crystallization.
Franz X. Heinz,Christian W. Mandl,Heidemarie Holzmann,Christian Kunz,B A Harris,Félix A. Rey,Stephen C. Harrison +6 more
TL;DR: By the use of limited trypsin digestion of purified virions, a membrane anchor-free and crystallizable form of the tick-borne encephalitis virus envelope glycoprotein E is generated and retained its reactivity with a panel of monoclonal antibodies.
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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