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Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein
T E Kienzle1, S Abraham, B G Hogue
1Department of Microbiology, University of Tennessee, Knoxville 37996-0845.
Journal of Virology
|April 1, 1990
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.