Download MendeleyAn airborne transmissible avian influenza H5 hemagglutinin seen at the atomic level.
Zhang, W., Shi, Y., Lu, X., Shu, Y., Qi, J., Gao, G.F.(2013) Science 340: 1463-1467
- PubMed: 23641058
- DOI: https://doi.org/10.1126/science.1236787
- Primary Citation of Related Structures:
4K62, 4K63, 4K64, 4K65, 4K66, 4K67 - PubMed Abstract:
Recent studies have identified several mutations in the hemagglutinin (HA) protein that allow the highly pathogenic avian H5N1 influenza A virus to transmit between mammals by airborne route. Here, we determined the complex structures of wild-type and mutant HAs derived from an Indonesia H5N1 virus bound to either avian or human receptor sialic acid analogs. A cis/trans conformational change in the glycosidic linkage of the receptor analog was observed, which explains how the H5N1 virus alters its receptor-binding preference. Furthermore, the mutant HA possessed low affinities for both avian and human receptors. Our findings provide a structural and biophysical basis for the H5N1 adaptation to acquire human, but maintain avian, receptor-binding properties.
Organizational Affiliation:
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
