Oligomerization and polymerization of the filovirus matrix protein VP40.

@article{Timmins2003OligomerizationAP,
  title={Oligomerization and polymerization of the filovirus matrix protein VP40.},
  author={Joanna Timmins and Guy Schoehn and Christine F. Kohlhaas and H -D Klenk and Rob W H Ruigrok and Winfried Weissenhorn},
  journal={Virology},
  year={2003},
  volume={312 2},
  pages={359-68}
}
The matrix protein VP40 from Ebola virus plays an important role in the assembly process of virus particles by interacting with cellular factors, cellular membranes, and the ribonuclearprotein particle complex. Here we show that the N-terminal domain of VP40 folds into a mixture of two different oligomeric states in vitro, namely hexameric and octameric ringlike structures, as detected by gel filtration chromatography, chemical cross-linking, and electron microscopy. Octamer formation depends… CONTINUE READING

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