The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein

Mol Cell. 2002 Aug;10(2):307-16. doi: 10.1016/s1097-2765(02)00588-9.


Ebola virus encodes seven viral structural and regulatory proteins that support its high rates of replication, but little is known about nucleocapsid assembly of this virus in infected cells. We report here that three viral proteins are necessary and sufficient for formation of Ebola virus particles and that intracellular posttranslational modification regulates this process. Expression of the nucleoprotein (NP) and virion-associated proteins VP35 and VP24 led to spontaneous assembly of nucleocapsids in transfected 293T cells by transmission electron microscopy. A specific biochemical interaction of these three proteins was demonstrated, and, interestingly, O-glycosylation and sialation of NP were demonstrated and necessary for their association. This distinct mechanism of regulation for filovirus assembly suggests new approaches for viral therapies and vaccines for Ebola and related viruses.

MeSH terms

  • Amino Acid Sequence
  • Capsid / ultrastructure
  • Cell Line
  • Ebolavirus / growth & development
  • Ebolavirus / metabolism*
  • Ebolavirus / ultrastructure
  • Glycosylation
  • Humans
  • Microscopy, Electron
  • Molecular Sequence Data
  • Nucleocapsid Proteins / metabolism*
  • Nucleoproteins / chemistry
  • Nucleoproteins / metabolism*
  • Protein Processing, Post-Translational*
  • Sequence Homology, Amino Acid
  • Viral Proteins / metabolism*
  • Viral Regulatory and Accessory Proteins
  • Virion / metabolism
  • Virion / ultrastructure
  • Virus Assembly*


  • Nucleocapsid Proteins
  • Nucleoproteins
  • VP24 protein, Marburg virus
  • VP35 protein, filovirus
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins
  • nucleocapsid protein, Ebola virus