Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza Virus.
Stevens, James 1*; Blixt, Ola 1,2; Tumpey, Terrence M. 4; Taubenberger, Jeffery K. 5; Paulson, James C. 1,2; Wilson, Ian A. 1,3*
[Article] Science. Influenza. 312(5772):404-410, April 21, 2006.

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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.

Copyright (C) 2006 by the American Association for the Advancement of Science