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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Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens
TL;DR: Bacteria did not bind to Leb antigen substituted with a terminal GalNAc alpha 1-3 residue (blood group A determinant), suggesting that the availability of H. pylori receptors might be reduced in individuals of blood group A and B phenotypes, as compared with blood group O individuals.
Journal ArticleDOI
The major human rhinovirus receptor is ICAM-1.
Jeffrey M. Greve,Gary Davis,Ann M. Meyer,Carla P. Forte,Susan Connolly Yost,Christopher W. Marlor,Michael E. Kamarck,Alan Mcclelland +7 more
TL;DR: The major human rhinovirus receptor has been identified with monoclonal antibodies that inhibit rhInovirus infection and protein sequence from the 95 kd protein showed an identity with that of intercellular adhesion molecule-1 (ICAM-1).
Journal ArticleDOI
Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily.
TL;DR: Northern hybridization analysis indicates that poliov virus receptor transcripts are expressed in a wide range of human tissues, in contrast to the limited expression of virus binding sites, which suggests that additional factors or modifications of the receptor protein are required to permit poliovirus attachment.
Journal ArticleDOI
Molecular Basis for the Generation in Pigs of Influenza A Viruses with Pandemic Potential
Toshihiro Ito,J. Nelson S. S. Couceiro,Sørge Kelm,Linda G. Baum,Scott Krauss,Maria R. Castrucci,Isabella Donatelli,Hiroshi Kida,James C. Paulson,Robert G. Webster,Robert G. Webster,Yoshihiro Kawaoka,Yoshihiro Kawaoka +12 more
TL;DR: A structural basis for the hypothesis that pigs may serve as “mixing vessels” for the generation of human-avian influenza A virus reassortants, similar to those responsible for the 1957 and 1968 pandemics is demonstrated.
Journal ArticleDOI
Recognition of haemagglutinins on virus-infected cells by NKp46 activates lysis by human NK cells
Ofer Mandelboim,Niva Lieberman,Marianna Lev,Lada Paul,Tal I. Arnon,Yuri Bushkin,Daniel M. Davis,Jack L. Strominger,Jonathan W. Yewdell,Angel Porgador +9 more
TL;DR: Findings indicate how NKp46-expressing NK cells may recognize target cells infected by influenza or parainfluenza without the decreased expression of target-cell MHC class I protein.
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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