Antanasijevic A, Durst MA, Lavie A, Caffrey M. Identification of a pH Sensor in Influenza Hemagglutinin using X-ray Crystallography. J Struct Biol. 2019 Nov 2:107412
Hemagglutnin (HA) mediates entry of influenza virus through a series of conformational changes triggered by the low pH of the endosome. The residue or combination of residues acting as pH sensors has not yet been fully elucidated. In this work, we assay pH effects on the structure of H5 HA by soaking HA crystallized at pH 6.5 in a series of buffers with lower pH, mimicking the conditions of the endosome. We find that HA1-H38, which is conserved in Group 1 HA, undergoes a striking change in side chain conformation, which we attribute to its protonation and cation-cation repulsion with conserved HA1-H18. This work suggests that x-ray crystallography can be applied for studying small-scale pH-induced conformational changes providing valuable information on the location of pH sensors in HA. Importantly, the observed change in HA1-H38 conformation is further evidence that the pH-induced conformational changes of HA are the result of a series of protonation events to conserved and non-conserved pH sensors.
See Also:
Latest articles in those days:
- Epidemiological characteristics of human infections with avian influenza A(H5N6) virus, China and Laos: A multiple case descriptive analysis, February 2014-June 2023 5 hours ago
- Interim Estimates of 2023-2024 Seasonal Influenza Vaccine Effectiveness Among Adults in Korea 14 hours ago
- Abundant Intra-Subtype Reassortment Revealed in H13N8 Influenza Viruses 2 days ago
- Locations and structures of influenza A virus packaging-associated signals and other functional elements via an in silico pipeline for predicting constrained features in RNA viruses 2 days ago
- Molecular Characterization of Non-H5 and Non-H7 Avian Influenza Viruses from Non-Mallard Migratory Waterbirds of the North American Flyways, 2006~2011 2 days ago
[Go Top] [Close Window]