Interaction of Tsg101 with Marburg virus VP40 depends on the PPPY motif, but not the PT/SAP motif as in the case of Ebola virus, and Tsg101 plays a critical role in the budding of Marburg virus-like particles induced by VP40, NP, and GP

J Virol. 2007 May;81(9):4895-9. doi: 10.1128/JVI.02829-06. Epub 2007 Feb 14.

Abstract

Marburg virus (MARV) VP40 is a matrix protein that can be released from mammalian cells in the form of virus-like particles (VLPs) and contains the PPPY sequence, which is an L-domain motif. Here, we demonstrate that the PPPY motif is important for VP40-induced VLP budding and that VLP production is significantly enhanced by coexpression of NP and GP. We show that Tsg101 interacts with VP40 depending on the presence of the PPPY motif, but not the PT/SAP motif as in the case of Ebola virus, and plays an important role in VLP budding. These findings provide new insights into the mechanism of MARV budding.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs / genetics*
  • Animals
  • COS Cells
  • Capsid Proteins / metabolism
  • Chlorocebus aethiops
  • DNA-Binding Proteins / metabolism*
  • Ebolavirus / metabolism
  • Endosomal Sorting Complexes Required for Transport
  • Marburgvirus / metabolism*
  • Transcription Factors / metabolism*
  • Viral Envelope Proteins / metabolism
  • Viral Matrix Proteins / metabolism*
  • Virion / metabolism*

Substances

  • Capsid Proteins
  • DNA-Binding Proteins
  • Endosomal Sorting Complexes Required for Transport
  • Transcription Factors
  • Tsg101 protein
  • VP40 protein, virus
  • Viral Envelope Proteins
  • Viral Matrix Proteins