Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers.

@article{Roche2002CharacterizationOT,
  title={Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers.},
  author={St{\'e}phane P Roche and Yves Gaudin},
  journal={Virology},
  year={2002},
  volume={297 1},
  pages={128-35}
}
Rabies virus-induced membrane fusion is triggered at low pH and is mediated by the trimeric viral glycoprotein (G). G assumes three conformations: the native state (N) detected above pH 7; the activated state (A), which initiates the fusion process; and the fusion-inactive conformation (I) observed after prolonged incubation at low pH. Differently from other viral fusogenic glycoproteins, G in the I state recovers its native conformation when reincubated above pH 7. Here, we demonstrate that… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 39 extracted citations

Similar Papers

Loading similar papers…