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Low pH deforms the influenza virus envelope

R W Ruigrok1, E A Hewat, R H Wade

  • 1EMBL Grenoble Outstation, France.

Insights

Low pH causes irreversible changes in influenza virus haemagglutinin (HA), extruding its fusion peptide. This destabilizes the virus membrane, a process reversible by returning to neutral pH.

Area of Science:

  • Virology
  • Structural Biology
  • Membrane Biophysics

Background:

  • Influenza virus entry into host cells relies on membrane fusion.
  • This fusion process is triggered by the viral haemagglutinin (HA) protein.
  • Low pH conditions in endosomes initiate conformational changes in HA.

Purpose of the Study:

  • To investigate the structural changes in influenza virus at low pH.
  • To visualize the effect of low pH on the viral membrane and HA.
  • To understand the mechanism of virus-endosome membrane fusion.

Main Methods:

  • Negative staining electron microscopy of low pH-treated influenza virus.
  • Cryo-electron microscopy of influenza virus in a frozen hydrated state.
  • Observation of structural alterations induced by pH changes.

Main Results:

  • Low pH induces significant destabilization of the influenza virus membrane.
  • Conformational changes in haemagglutinin (HA) lead to fusion peptide extrusion.
  • The observed membrane destabilization is reversible upon return to neutral pH.

Conclusions:

  • Low pH is critical for initiating irreversible conformational changes in HA, essential for viral fusion.
  • The study provides direct visualization of virus membrane destabilization at low pH.
  • Understanding these pH-dependent structural dynamics is key to viral entry mechanisms.

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