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Expression of Reovirus Type 3 (Dearing) 1 and s Polypeptides in Escherichia coli

¹ Department of Biochemistry
² Department of Microbiology and Molecular Genetics, Harvard Medical School
³ Department of Medicine, Division of Infectious Diseases, Brigham and Women's Hospital
⁴ Shipley Institute of Medicine, Boston, Massachusetts 02115, U.S.A.
⁵ McGill Cancer Center, McGill University, Montreal, Quebec, Canada H3G 1Y6

The revoirus S1 gene codes for two polypeptides: 1 and s. In order to characterize the structure and function of the 1 polypeptide, we have expressed the 1 protein in Escherichia coli. The S1 gene from mammalian reovirus type 3 (Dearing strain) and the variant K strain were subcloned into an expression vector containing the tac (trp-lac) promoter designed to express foreign gene products in E. coli efficiently. The hybrid plasmids, upon induction with isopropyl--D-thiogalactopyranoside, expressed two polypeptides that were detected by [³⁵S]methionine labelling. One of the induced proteins had a relative molecular mass (M_r) of approx. 46 000 and corresponded to 1, as shown by immunoprecipitation with goat anti-reovirus antibody and a monoclonal antibody against 1. The second induced protein had a M_r of approx. 12 000 and was very similar to s as judged by comparative tryptic peptide map analysis. Protein 1 produced in E. coli was shown to be functional as judged from its ability to bind to mouse L fibroblasts.

This paper is dedicated to the memory of Dr Stewart Millward.

Received 2 July 1986; accepted 9 September 1986.

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