Ebolavirus Glycoprotein Directs Fusion through NPC1+ Endolysosomes

J Virol. 2015 Oct 14;90(1):605-10. doi: 10.1128/JVI.01828-15. Print 2016 Jan 1.

Abstract

Ebolavirus, a deadly hemorrhagic fever virus, was thought to enter cells through endolysosomes harboring its glycoprotein receptor, Niemann-Pick C1. However, an alternate model was recently proposed in which ebolavirus enters through a later NPC1-negative endosome that contains two-pore Ca(2+) channel 2 (TPC2), a newly identified ebolavirus entry factor. Here, using live cell imaging, we obtained evidence that in contrast to the new model, ebolavirus enters cells through endolysosomes that contain both NPC1 and TPC2.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Calcium Channels / metabolism*
  • Carrier Proteins / metabolism*
  • Cell Line
  • Chlorocebus aethiops
  • Ebolavirus / physiology*
  • Endosomes / virology*
  • Host-Pathogen Interactions
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins / metabolism*
  • Microscopy
  • Models, Biological
  • Niemann-Pick C1 Protein
  • Viral Envelope Proteins / metabolism*
  • Virus Internalization*

Substances

  • Calcium Channels
  • Carrier Proteins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins
  • NPC1 protein, human
  • Niemann-Pick C1 Protein
  • TPCN2 protein, human
  • Viral Envelope Proteins
  • envelope glycoprotein, Ebola virus