tetano
Editor, Senior Moderator
J Struct Biol. 2019 Nov 2:107412. doi: 10.1016/j.jsb.2019.107412. [Epub ahead of print] [h=1]Identification of a pH Sensor in Influenza Hemagglutinin using X-ray Crystallography.[/h]
Antanasijevic A[SUP]1[/SUP], Durst MA[SUP]1[/SUP], Lavie A[SUP]1[/SUP], Caffrey M[SUP]2[/SUP].
[h=3]Author information[/h] 1 Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, 900 S Ashland Ave, 60607, Chicago, USA. 2 Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, 900 S Ashland Ave, 60607, Chicago, USA. Electronic address: caffrey@uic.edu.
[h=3]Abstract[/h] 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.
Copyright ? 2019 Elsevier Inc. All rights reserved.
PMID: 31689502 DOI: 10.1016/j.jsb.2019.107412
Antanasijevic A[SUP]1[/SUP], Durst MA[SUP]1[/SUP], Lavie A[SUP]1[/SUP], Caffrey M[SUP]2[/SUP].
[h=3]Author information[/h] 1 Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, 900 S Ashland Ave, 60607, Chicago, USA. 2 Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, 900 S Ashland Ave, 60607, Chicago, USA. Electronic address: caffrey@uic.edu.
[h=3]Abstract[/h] 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.
Copyright ? 2019 Elsevier Inc. All rights reserved.
PMID: 31689502 DOI: 10.1016/j.jsb.2019.107412