Retention by the endoplasmic reticulum of rotavirus VP7 is controlled by three adjacent amino-terminal residues.

@article{Maa1994RetentionBT,
  title={Retention by the endoplasmic reticulum of rotavirus VP7 is controlled by three adjacent amino-terminal residues.},
  author={Dieter Maa\ss and Paul H Atkinson},
  journal={Journal of virology},
  year={1994},
  volume={68 1},
  pages={366-78}
}
The rotavirus outer capsid glycoprotein, VP7, is an endoplasmic reticulum (ER) membrane-associated glycoprotein in both infected and transfected cells. It was previously demonstrated in this laboratory and by others that both the cleaved signal sequence (H2) and the first NH2-terminal 61 amino acids of VP7 are sufficient and necessary for ER retention of this molecule. Using site-specific mutagenesis and transfection techniques, we show that residues Ile-9, Thr-10, and Gly-11 were specifically… CONTINUE READING