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
Identification of functional sites on bovine leukemia virus envelope glycoproteins using structural and immunological data
TL;DR: The analysis suggests, for the first time, that the bovine leukemia virus envelope head will not adopt the typical 'jelly-roll' fold of the influenza A hemagglutinin head, but most likely folds into another type of 'Greek-key' structure corresponding to the overall topology of constant immunoglobulin domains.
Book ChapterDOI
Crystallographic and cryo EM analysis of virion-receptor interactions.
Michael G. Rossmann,N. H. Olson,Prasanna R. Kolatkar,Marcos A. Oliveira,R. H. Cheng,Jeffrey M. Greve,Alan Mcclelland,Timothy S. Baker +7 more
TL;DR: Human rhinovirus 16 complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule-1 shows that ICAM-1 binds into the 12 A deep "canyon" on the surface of the virus, consistent with the prediction that the viral receptor attachment site lies in a cavity inaccessible to the host's antibodies.
Journal ArticleDOI
ph-dependent hydrophobicity profile of hemagglutinin of influenza virus and its possible relevance in virus fusion.
TL;DR: The hydropathy profile of hemagglutinin subunits HA1 and HA2 of influenza virus X31 and A/PR 8/34 is analyzed at different pH and it is suggested that these hydrophobic stretches are important for the fusion complex, in addition to the N-terminal site of HA2.
Journal ArticleDOI
N-Acetyl-β-d-glucosaminyl-binding properties of the envelope glycoprotein of human immunodeficiency virus type1
Liliane Gattegno,Hoss Sadeghi,Line Saffar,Dominique Bladier,B Clerget-Raslain,Jean Claude Gluckman,Elmostafa Bahraoui +6 more
TL;DR: Results indicated that rgp 160 behaves as a N -acetyl-β- d -glucosaminyl-binding protein for GlcNAc residues presented at high density on a carrier, the carbohydrate-binding site of which is close to, or located on the V3 region of gp 120.
Book ChapterDOI
Viral Pathogenesis, Modulation of Immune Receptor Signaling and Treatment
TL;DR: This chapter discusses the MIRR-targeting viral strategies of immune evasion and suggests their possible mechanisms that reveal new points of antiviral intervention, and shows how two unrelated enveloped viruses use a similar mechanism to modulate the host immune response mediated by two functionally different MIRRs.
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.
The Structure and Function of the Hemagglutinin Membrane Glycoprotein of Influenza Virus
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