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Zika virus M protein latches and locks the E protein from transitioning to an immature state after prM cleavage

Sydney A Majowicz1, Anoop Narayanan2, Ibrahim M Moustafa2

  • 1The Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA, 16802, USA.

Npj Viruses
|April 28, 2025
PubMed

Insights

Flavivirus maturation involves structural changes in prM/E proteins. M protein residues Arg38 and Trp19 lock the E protein into a stable, mature conformation, preventing premature fusion.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Flavivirus maturation involves critical low pH-mediated conformational changes of structural proteins.
  • The transition from spiky trimeric to smooth dimeric prM/E heterodimers is essential for infectivity.
  • Mechanisms stabilizing the mature E protein conformation after prM cleavage remain unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms stabilizing the mature E protein structure in flaviviruses.
  • To identify key interactions responsible for the irreversible conformational change of the E protein.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) of immature Zika virus.
  • Structure-based mutagenesis of Zika virus M and E proteins.

Main Results:

  • Identified two critical "latching and locking" interactions involving M protein residues Arg38 and Trp19.
  • These interactions stabilize the E protein in its smooth, mature dimeric conformation.
  • Demonstrated that M protein prevents premature fusion by locking the E protein structure.

Conclusions:

  • M protein plays a crucial role in irreversibly stabilizing the mature E protein structure via specific residues.
  • These findings provide mechanistic insights into flavivirus maturation and infectivity.

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