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Polarized budding of measles virus is not determined by viral surface glycoproteins

A Maisner1, H Klenk, G Herrler

  • 1Institut für Virologie, Philipps-Universität Marburg, 35037 Marburg, Germany.

Journal of Virology
|May 30, 1998
PubMed

Insights

Measles virus releases from the apical surface of polarized epithelial cells. This differs from other budding viruses, as its glycoproteins are not exclusively targeted to the apical domain.

Area of Science:

  • Virology
  • Cell Biology
  • Epithelial Cell Biology

Background:

  • Budding viruses typically release from polarized epithelial cells at the membrane domain where their envelope glycoproteins are targeted.
  • Viral glycoproteins are key determinants of the site of virus release in many enveloped viruses.

Purpose of the Study:

  • To investigate the release mechanism of measles virus from polarized epithelial cells.
  • To determine if measles virus follows the conventional budding virus release strategy.

Main Methods:

  • Utilized polarized epithelial cell cultures.
  • Tracked the transport and localization of measles virus (MeV) surface glycoproteins (H and F).
  • Determined the site of measles virus release.

Main Results:

  • Measles virus was released from the apical membrane domain of polarized epithelial cells.
  • Unlike other budding viruses, measles virus surface glycoproteins H and F showed nonpolarized transport.
  • Glycoprotein F was specifically found in the basolateral membrane domain.

Conclusions:

  • Measles virus employs a distinct maturation and release strategy compared to other budding viruses.
  • The release site of measles virus is not solely dictated by the polarized transport of its envelope glycoproteins.
  • This finding reveals a unique mechanism for viral morphogenesis in polarized epithelial cells.

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