Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza Virus
Abstract
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 α2-3 sialic acid receptor binding preference. Introduction of mutations that can convert H1 serotype HAs to human α2-6 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 α2-6 glycan, which suggests a path for this H5N1 virus to gain a foothold in the human population.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Apr 21, 2006
- Source ID
- 10.1126/science.1124513
Entities
People
- Ian A Wilson
- James C. Paulson
- James D. Stevens
- Jeffery Taubenberger
- Ola Blixt
- Terrence M. Tumpey
Organizations
- Armed Forces Institute of Pathology
- Centers for Disease Control and Prevention
- Consortium for Functional Glycomics
- Scripps Research