Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein.

@article{Kienzle1990StructureAO,
  title={Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein.},
  author={Thomas E. Kienzle and Sonny Abraham and Brenda G Hogue and David A. Brian},
  journal={Journal of virology},
  year={1990},
  volume={64 4},
  pages={1834-8}
}
The sequence of the hemagglutinin-esterase (HE) gene for the Mebus strain of bovine coronavirus was obtained from cDNA clones, and its deduced product is a 47,700-kilodalton apoprotein of 424 amino acids. Expression of the HE protein in vitro in the presence of microsomes revealed N-terminal signal peptide cleavage and C-terminal anchorage but not disulfide-linked dimerization. Dimerization was observed only after expression in vivo, during which HE was also transported to the cell surface. 

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