Role of endocytosis and cathepsin-mediated activation in Nipah virus entry

Virology. 2008 Jun 5;375(2):391-400. doi: 10.1016/j.virol.2008.02.019. Epub 2008 Mar 14.

Abstract

The recent discovery that the Nipah virus (NiV) fusion protein (F) is activated by endosomal cathepsin L raised the question if NiV utilize pH- and protease-dependent mechanisms of entry. We show here that the NiV receptor ephrin B2, virus-like particles and infectious NiV are internalized from the cell surface. However, endocytosis, acidic pH and cathepsin-mediated cleavage are not necessary for the initiation of infection of new host cells. Our data clearly demonstrate that proteolytic activation of the NiV F protein is required before incorporation into budding virions but not after virus entry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cathepsin B / metabolism*
  • Cell Line
  • Cell Membrane / metabolism
  • Cell Membrane / virology
  • Endocytosis / physiology
  • Ephrin-B2 / metabolism*
  • Henipavirus Infections / virology*
  • Humans
  • Nipah Virus / physiology*
  • Receptors, Virus / physiology
  • Viral Envelope Proteins / metabolism
  • Virus Internalization

Substances

  • Ephrin-B2
  • F protein, Nipah virus
  • Receptors, Virus
  • Viral Envelope Proteins
  • Cathepsin B