CHO KJ, Lee JH, Hong KW, Kim SH, et al.. Insight into structural diversity of influenza virus hemagglutinin. J Gen Virol. 2013
Influenza virus infects host cells through membrane fusion, a process mediated by the low pH-induced conformational change of the viral surface glycoprotein hemagglutinin (HA). We determined the structures and biochemical properties of the HA proteins from A/Korea/01/2009 (KR01), a 2009 pandemic strain, and A/Thailand/CU44/2006 (CU44), a seasonal strain. The crystal structure of KR01 HA revealed a V-shaped head-to-head arrangement, which is not seen in other HA proteins including CU44 HA. We isolated a broadly neutralizing H1-specific monoclonal antibody GC0757. The KR01 HA-Fab0757 complex structure also exhibited a head-to-head arrangement of HA. Both native and Fab complex structures reveal different spatial orientation of HA1 relative to HA2, indicating that HA is flexible and dynamic at neutral pH. Further, the KR01 HA exhibited significantly lower protein stability and increased susceptibility to proteolytic cleavage compared with other HAs. Our structures provide important insight into conformational flexibility of HA.
See Also:
Latest articles in those days:
- Spatio-temporal dynamics and drivers of highly pathogenic avian influenza H5N1 in Chile 11 hours ago
- [preprint] Avian Influenza Virus Infections in Felines: A Systematic Review of Two Decades of Literature 16 hours ago
- Exploring the effect of clinical case definitions on influenza vaccine effectiveness estimation at primary care level: Results from the end-of-season 2022-23 VEBIS multicentre study in Europe 16 hours ago
- Assessment of potential adverse events following the 2022-2023 seasonal influenza vaccines among U.S. adults aged 65 years and older 16 hours ago
- Novel Avian Influenza A(H5N6) in Wild Birds, South Korea, 2023 16 hours ago
[Go Top] [Close Window]