Yi Shi, etc.,al. Structures and Receptor Binding of Hemagglutinins from Human-Infecting H7N9 Influenza Viruses. Science DOI: 10.1126/science.1242917
An avian-origin human-infecting influenza (H7N9) virus has recently been identified in China. Here, we have evaluated the viral hemagglutinin (HA) receptor binding properties from two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature Q226) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature L226). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas the AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (L226Q) has dual receptor binding property, indicating that other amino acid substitutions contribute to the receptor binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how the AH-H7N9 can bind human receptors, yet also retain the avian receptor binding property.
See Also:
Latest articles in those days:
- Nomenclature Updates to the Hemagglutinin Gene Clade Designations Resulting From the Continued Evolution of High Pathogenicity Avian Influenza A(H5) Virus Clades 2.3.2.1c and 2.3.4.4 12 hours ago
- Mathematical modeling of in vitro replication dynamics for multiple highly pathogenic avian influenza clade 2.3.4.4 viruses in chicken and duck cells 12 hours ago
- H5 influenza virus mRNA-lipid nanoparticle (LNP) vaccination elicits adaptive immune responses in Holstein calves 12 hours ago
- Highly pathogenic avian influenza as a systemic risk - implications for control and preparedness 2 days ago
- Multiple introductions and spread of novel reassortant highly pathogenic avian influenza A (H5N1) clade 2.3.4.4b viruses via wild birds, South Korea, 2024-2025 2 days ago
[Go Top] [Close Window]


