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Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch.

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Viral fusion proteins use a pH-sensitive histidine switch to initiate membrane fusion. This discovery in GP64 offers new strategies for antiviral therapies and vaccines against enveloped viruses.

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Area of Science:

  • Structural biology
  • Virology
  • Biochemistry

Background:

  • Enveloped viruses fuse with host cells via viral fusion proteins.
  • The pH-dependent conformational changes of these proteins are crucial for fusion, but the precise mechanisms remain unclear.

Purpose of the Study:

  • To elucidate the structural intermediates and pH-sensing mechanisms of viral membrane fusion.
  • To investigate the role of pH-sensitive switches in viral fusion proteins.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine structures of GP64 in prefusion and intermediate states.
  • Cell-cell syncytium formation assays and dual dye-labeling to validate pH sensing.

Main Results:

  • Cryo-EM structures revealed early intermediate states of the class III fusion protein GP64.
  • A pH-sensitive switch involving histidine residues (H23, H245, H304) was identified as the trigger for membrane fusion.
  • Experimental assays confirmed the role of this multi-histidine switch in pH sensing and fusion activation.

Conclusions:

  • A coordinated multi-histidine switch acts as a pH sensor and activator in viral fusion.
  • Understanding this mechanism can inform the development of novel antiviral therapies and vaccines targeting viral fusion.
  • The findings are relevant to human-infecting thogotoviruses and other enveloped viruses.