Science (American Association for the Advancement of Science), 2006-04, Vol.312 (5772), p.404-410
2006
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza Virus
- Ist Teil von
- Science (American Association for the Advancement of Science), 2006-04, Vol.312 (5772), p.404-410
- Ort / Verlag
- Washington, DC: American Association for the Advancement of Science
- Erscheinungsjahr
- 2006
- Quelle
- Science Online_科学在线
- Beschreibungen/Notizen
- The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other human H1 HAs than to a 1997 duck H5 HA. Glycan microarray analysis of this Viet04 HA reveals an avian [alpha]2-3 sialic acid receptor binding preference. Introduction of mutations that can convert H1 serotype HAs to human [alpha]2-6 receptor specificity only enhanced or reduced affinity for avian-type receptors. However, mutations that can convert avian H2 and H3 HAs to human receptor specificity, when inserted onto the Viet04 H5 HA framework, permitted binding to a natural human [alpha]2-6 glycan, which suggests a path for this H5N1 virus to gain a foothold in the human population.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0036-8075eISSN: 1095-9203DOI: 10.1126/science.1124513Titel-ID: cdi_proquest_miscellaneous_67883917
- Format
- –
- Schlagworte
- Amino Acid Sequence, Amino Acid Substitution, Animals, Antigenic Variation, Avian flu, binding capacity, Binding Sites, Biological and medical sciences, Birds, Carbohydrate Conformation, Cloning, Molecular, Crystallography, X-Ray, Fundamental and applied biological sciences. Psychology, Genetic mutation, Glycoproteins, Glycosylation, H5N1 subtype influenza A virus, Hemagglutinin Glycoproteins, Influenza Virus - chemistry, Hemagglutinin Glycoproteins, Influenza Virus - genetics, Hemagglutinin Glycoproteins, Influenza Virus - immunology, Hemagglutinin Glycoproteins, Influenza Virus - metabolism, hemagglutinins, Human viral diseases, Humans, Infectious diseases, Influenza A virus, Influenza A Virus, H5N1 Subtype - chemistry, Influenza A Virus, H5N1 Subtype - genetics, Influenza A Virus, H5N1 Subtype - metabolism, Influenza A Virus, H5N1 Subtype - pathogenicity, Influenza virus, Ligands, Lung - virology, Medical sciences, Microbiology, Models, Molecular, Molecular Sequence Data, Monomers, mutants, Mutation, Polysaccharides, Polysaccharides - metabolism, Protein Conformation, Protein Folding, protein structure, Protein Structure, Tertiary, protein-protein interactions, Receptors, Receptors, Virus - chemistry, Receptors, Virus - metabolism, Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains, Respiratory Mucosa - virology, serotypes, Sialic Acids - chemistry, Sialic Acids - metabolism, Species Specificity, Trimers, Viral diseases, Viral diseases of the respiratory system and ent viral diseases, Viral morphology, Virology, Virulence, Viruses