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:
- The evolution, complexity, and diversity of swine influenza viruses in China: A hidden public health threat 1 days ago
- MHC class II proteins mediate sialic acid independent entry of human and avian H2N2 influenza A viruses 1 days ago
- Histopathologic Features and Viral Antigen Distribution of H5N1 Highly Pathogenic Avian Influenza Virus Clade 2.3.4.4b from the 2022–2023 Outbreak in Iowa Wild Birds 1 days ago
- Detection and characterization of H5N1 HPAIV in environmental samples from a dairy farm 1 days ago
- Genomic Characterization of Highly Pathogenic Avian Influenza A H5N1 Virus Newly Emerged in Dairy Cattle 1 days ago
[Go Top] [Close Window]