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Structure of the immature dengue virus at low pH primes proteolytic maturation

Science, ISSN: 0036-8075, Vol: 319, Issue: 5871, Page: 1834-1837
2008
  • 516
    Citations
  • 0
    Usage
  • 576
    Captures
  • 3
    Mentions
  • 0
    Social Media
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Metrics Details

  • Citations
    516
  • Captures
    576
  • Mentions
    3
    • References
      2
      • Wikipedia
        2
    • News Mentions
      1
      • News
        1

Most Recent News

Anticuerpos contra el virus del dengue en pacientes con dislipidemias /Antibodies against dengue virus in patients with dislipidemias.

Introducción Los virus son agentes patógenos intracelulares obligados que dependen del metabolismo de la célula huésped para su replicación; interactúan con las membranas y los

Article Description

Intracellular cleavage of immature flaviviruses is a critical step in assembly that generates the membrane fusion potential of the E glycoprotein. With cryo-electron microscopy we show that the immature dengue particles undergo a reversible conformational change at low pH that renders them accessible to furin cleavage. At a pH of 6.0, the E proteins are arranged in a herringbone pattern with the pr peptides docked onto the fusion loops, a configuration similar to that of the mature virion. After cleavage, the dissociation of pr is pH-dependent, suggesting that in the acidic environment of the trans-Golgi network pr is retained on the virion to prevent membrane fusion. These results suggest a mechanism by which flaviviruses are processed and stabilized in the host cell secretory pathway.

Bibliographic Details

Yu, I-Mei; Zhang, Wei; Holdaway, Heather A; Li, Long; Kostyuchenko, Victor A; Chipman, Paul R; Kuhn, Richard J; Rossmann, Michael G; Chen, Jue

American Association for the Advancement of Science (AAAS)

Multidisciplinary

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