Purification and composition of the proteins from Sindbis virus grown in chick and BHK cells

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Abstract
Procedures are described for the purification of the Sindbis virus structural proteins. The amino acid and carbohydrate compositions of the purified proteins are presented for virus grown in BHK[baby hamster kidney]-21/13 and chicken embryo cells. Glycoprotein E1 from virus grown in BHK cells is deficient in a mannose-rich glycopeptide found on that glycoprotein when virus is grown in chicken embryo cells. The complex galactose-containing glycopeptides appear similar for virus grown in both hosts. When virus is grown in BHK cells, both glycoproteins are enriched in those glycopeptides containing more sialic acid. Since the 2 viral glycoproteins are difficult to separate cleanly during purification, it is suggested that there may be strong, but noncovalent, interactions between glycoproteins E1 and E2. There may be an interaction between glycoprotein E2 and a component of the nucleocapsid.