Structural highlights
Publication Abstract from PubMed
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.
An Airborne Transmissible Avian Influenza H5 Hemagglutinin Seen at the Atomic Level.,Zhang W, Shi Y, Lu X, Shu Y, Qi J, Gao GF Science. 2013 May 2. PMID:23641058[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang W, Shi Y, Lu X, Shu Y, Qi J, Gao GF. An Airborne Transmissible Avian Influenza H5 Hemagglutinin Seen at the Atomic Level. Science. 2013 May 2. PMID:23641058 doi:10.1126/science.1236787
