Oligomerization-dependent folding of the membrane fusion protein of Semliki Forest virus.

@article{Andersson1997OligomerizationdependentFO,
  title={Oligomerization-dependent folding of the membrane fusion protein of Semliki Forest virus.},
  author={Helena Andersson and Bettina Barth and Maria Ekstr{\"o}m and Henrik Garoff},
  journal={Journal of virology},
  year={1997},
  volume={71 12},
  pages={9654-63}
}
The spikes of alphaviruses are composed of three copies of an E2-E1 heterodimer. The E1 protein possesses membrane fusion activity, and the E2 protein, or its precursor form, p62 (sometimes called PE2), controls this function. Both proteins are, together with the viral capsid protein, translated from a common C-p62-E1 coding unit. In an earlier study, we showed that the p62 protein of Semliki Forest virus (SFV) dimerizes rapidly and efficiently in the endoplasmic reticulum (ER) with the E1… CONTINUE READING

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