Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins.

@article{Veit1996CytoplasmicTL,
  title={Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins.},
  author={Michael Veit and H Reverey and Michael F. Schmidt},
  journal={The Biochemical journal},
  year={1996},
  volume={318 ( Pt 1)},
  pages={163-72}
}
We report remarkable differences in the fatty acid content of thioester-type acylated glycoproteins of enveloped viruses from mammalian cells. The E2 glycoprotein of Semliki Forest virus contains mainly palmitic acid like most other palmitoylated proteins analysed so far. However, the other glycoprotein (E1) of the same virus, as well as the HEF (haemagglutinin esterase fusion) glycoprotein of influenza C virus, are unique in this respect because they are acylated primarily with stearic acid… CONTINUE READING
11 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

Similar Papers

Loading similar papers…