Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1834-1838 |
| Number of pages | 5 |
| Journal | Journal of virology |
| Volume | 64 |
| Issue number | 4 |
| State | Published - 1990 |
| Externally published | Yes |
ASJC Scopus subject areas
- Microbiology
- Immunology
- Insect Science
- Virology