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Article
Avian and human receptor binding by hemagglutinins of influenza A viruses
An understanding of the structural determinants and molecular mechanisms involved in influenza A virus binding to human cell receptors is central to the identification of viruses that pose a pandemic threat. T...
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Chapter
Aspects of the Fusogenic Activity of Influenza Hemagglutinin Peptides by Molecular Dynamics Simulations
The interactions of the fusion domain of influenza hemagglutinin (HA) (N-terminal 20 residues, the fusion peptide) with a POPC lipid bilayer have been studied by molecular dynamics (MD) simulations. This domai...
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Article
Atomic structure of the ectodomain from HIV-1 gp41
Fusion of viral and cellular membranes by the envelope glyco-protein gp120/gp41 effects entry of HIV-1 into the cell. The precursor, gp160, is cleaved post-translationally into gp120 and gp41 (refs 1,2), which...
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Article
Antigenic and genetic characterization of current influenza strains
Annually the influenza centre receives more than 1000 virus isolates from around the world to monitor the changing pattern of viruses causing influenza throughout the year. These are characterized antigenicall...
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Article
Amantadine blocks the channel
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Article
Influenza A virus enhances IgE-mediated histamine release from human basophil leukocytes. Examination of the effect of viral neuraminidase and haemagglutinin
Histamine release caused by anti-IgE was examined in leukocyte suspensions from 10 healthy individuals. Influenza A virus was found to enhance the histamine release but did not release histamineper se. When monoc...
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Chapter
Structure, Function, and Antigenicity of the Hemagglutinin of Influenza Virus
The major surface glycoprotein of influenza virus is hemagglutinin (HA). This chapter reviews the two major functions of HA: (1) its involvement in binding to receptors on cells before their infection, and (2)...
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Article
Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
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. Sia...
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Chapter and Conference Paper
Antigenicity of the Influenza Haemagglutinin Membrane Glycoprotein
Antibodies which neutralize the infectivity of influenza viruses specifically react with the hemagglutinin membrane glycooroteins. These molecules, of which there are about 500 on each virus surface, serve to ...
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Article
Immunology: Are peptides good antigens?
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Article
Three-dimensional structure of an antigenic mutant of the influenza virus haemagglutinin
Antigenic variation in the haemagglutinin (HA) glycoprotein of influenza virus is associated with recurrent epidemics of respiratory disease in man (for review see ref. 1). We have examined the size of structu...
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Chapter
Targets for the Design of Antiviral Agents: Targets in Orthomyxoviruses
To initiate replication influenza viruses bind to sialic acid residues of membrane glycoconjugates and are taken into intracellular vesicles by endocytosis. Fusion of virus membranes and endosomal membranes oc...
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Chapter
Studies on the Structure and Activities of Influenza Virus Haemagglutinin
The initial events in infection by influenza virus involve binding of virus to sialic acid residues of glycosylated membrane receptors, endocytosis, and fusion of the membranes of virus and endosome. Virus ads...
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Article
Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity
The haemagglutinin (HA) glycoproteins of influenza virus membranes are responsible for binding viruses to cells by interacting with membrane receptor molecules which contain sialic acid (for review see ref. 1)...
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Article
Influenza A specific cytotoxic T-cell clones that do not recognize viral glycoproteins
Since the demonstration that murine cytotoxic T cells generated during a secondary immune response to influenza A viruses were composed of cross-reactive and subtype-specific populations1–5, it has become of inte...
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Article
Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
Four ‘antigenic sites’ on the three-dimensional structure of the influenza haemagglutinin are identified. At least one amino acid substitution in each site seems to be required for the production of new epidem...
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Article
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
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 a...
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Chapter
Structural Studies of the Hemagglutinin of the Asian Influenza Virus Japan/305/57 — Bellamy/42 (H2N1).Cyanogen Bromide Cleavage of the Larger Polypeptide Chain HA1
A structural study of the hemagglutinin from the influenza virus variant Japan/305 /57 - Bellamy/42 (H2N1) is described. The two disulfide bonded glycopolypeptide chains (BHA1 and BHA2 were separated from the hem...
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Chapter
Preliminary Studies of the Membrane-Associated Portion of the Hemagglutinin
Like other ‘intrinsic’ membrane proteins the hemagglutinin is amphipathic. The results of comparative analyses of intact hemagglutinin molecules and preparations which lack the membrane associated hydrophobic ...
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Chapter
The Structure of the Small Polypeptide Chain of the Hemagglutinin of an Asian Influenza Virus Japan 305/57 — Bellamy/42 (H2N1)
The hemagglutinin of the influenza virus variant A/Japan/305/57 — A/Bellamy/42 (H2N1) was isolated from virus particles following digestion with Bromelain (EC 3.4.22.4) and purified by sucrose density gradient...
