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The flavivirus precursor membrane-envelope protein complex: structure and maturation

Long Li1, Shee-Mei Lok, I-Mei Yu

  • 1Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.

Science (New York, N.Y.)
|March 29, 2008
PubMed

Insights

Flaviviruses mature through precursor membrane protein (prM) cleavage, converting inert viruses into infectious particles. This study reveals the dengue virus prM-E heterodimer structure, explaining maturation and host cell fusion inhibition.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Viral maturation is crucial for infectivity, involving protein processing.
  • Flavivirus maturation relies on the proteolytic cleavage of the precursor membrane protein (prM).

Purpose of the Study:

  • To determine the high-resolution crystal structure of the dengue virus prM-E heterodimer.
  • To elucidate the structural basis of flavivirus maturation and host cell fusion inhibition.

Main Methods:

  • X-ray crystallography at 2.2 angstrom resolution.
  • Recombinant protein expression and purification.
  • Cryo-electron microscopy density fitting.

Main Results:

  • The crystal structure of the dengue virus prM-E heterodimer was determined.
  • The pr peptide shields the E glycoprotein's fusion loop, preventing membrane fusion.
  • The structure is consistent with immature virus cryo-EM data at neutral pH.

Conclusions:

  • The prM-E structure provides a molecular understanding of flavivirus maturation.
  • It reveals the mechanism by which the pr peptide inhibits fusion.
  • This structural insight aids in understanding pH-dependent conformational changes during viral maturation.

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