Calnexin acts as a molecular chaperone during the folding of glycoprotein B of human cytomegalovirus.

@article{Yamashita1996CalnexinAA,
  title={Calnexin acts as a molecular chaperone during the folding of glycoprotein B of human cytomegalovirus.},
  author={Yasuyuki Yamashita and Kaoru Shimokata and Satoshi Mizuno and Tohru Daikoku and Tatsuya Tsurumi and Yukihiro Nishiyama},
  journal={Journal of virology},
  year={1996},
  volume={70 4},
  pages={2237-46}
}
Human cytomegalovirus glycoprotein B (gB) is synthesized as a 105-kDa nonglycosylated polypeptide and cotranslationally modified by addition of N-linked oligosaccharides to a 160-kDa precursor in the endoplasmic reticulum (ER). It is then transported to the Golgi complex, where it is endoproteolytically cleaved to form the disulfide-linked mature gp55-116 complex. Pulse-chase experiments demonstrate that the 160-kDa gB precursor was transiently associated with calnexin, a membrane-bound… CONTINUE READING