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. 1990 Apr;64(4):1834–1838. doi: 10.1128/jvi.64.4.1834-1838.1990

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

T E Kienzle 1, S Abraham 1, B G Hogue 1, D A Brian 1
PMCID: PMC249325  PMID: 2319653

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.

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Selected References

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