Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein.
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.
Kienzle
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Department of Microbiology, University of Tennessee, Knoxville 37996-0845.
Abraham
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Hogue
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Brian
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001692:Biological Transport; D002417:Cattle; D003332:Coronaviridae / Q000201:enzymology / Q000235:genetics*; D015870:Gene Expression; D005814:Genes, Viral; D006023:Glycoproteins / Q000235:genetics* / Q000378:metabolism; D006389:Hemagglutinins, Viral / Q000235:genetics* / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational / Q000235:genetics; D014760:Viral Fusion Proteins; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism
D006023:Glycoproteins; D006389:Hemagglutinins, Viral; D014760:Viral Fusion Proteins; D014764:Viral Proteins; C060814:hemagglutinin esterase