An Avian Influenza H5N1 Virus That Binds to a Human-Type Receptor
- 15 September 2007
- journal article
- research article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 81 (18) , 9950-9955
- https://doi.org/10.1128/jvi.00468-07
Abstract
Avian influenza viruses preferentially recognize sialosugar chains terminating in sialic acid-α2,3-galactose (SAα2,3Gal), whereas human influenza viruses preferentially recognize SAα2,6Gal. A conversion to SAα2,6Gal specificity is believed to be ...Keywords
This publication has 22 references indexed in Scilit:
- Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptorsNature, 2006
- Computational studies of H5N1 hemagglutinin binding with SA-α-2, 3-Gal and SA-α-2, 6-GalBiochemical and Biophysical Research Communications, 2006
- Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza VirusScience, 2006
- Glycan Microarray Analysis of the Hemagglutinins from Modern and Pandemic Influenza Viruses Reveals Different Receptor SpecificitiesJournal of Molecular Biology, 2005
- SWISS-MODEL: an automated protein homology-modeling serverNucleic Acids Research, 2003
- Chemoenzymatic synthesis and application of glycopolymers containing multivalent sialyloligosaccharides with a poly(L-glutamic acid) backbone for inhibition of infection by influenza virusesGlycobiology, 2002
- Receptor Binding and Membrane Fusion in Virus Entry: The Influenza HemagglutininAnnual Review of Biochemistry, 2000
- A DNA transfection system for generation of influenza A virus from eight plasmidsProceedings of the National Academy of Sciences, 2000
- VMD: Visual molecular dynamicsJournal of Molecular Graphics, 1996
- The solution conformation of sialyl-α(2→6)-lactose studied by modern NMR techniques and Monte Carlo simulationsJournal of Biomolecular NMR, 1992