Abstract
The SU and TM subunits of the Rous sarcoma virus glycoprotein, which are derived from a single polypeptide precursor, have been expressed independently with a simian virus 40 vector. The TM protein retains the ability to form an oligomer which resembles the TM oligomer derived from the wild-type glycoprotein complex present in virions. Oligomerization of the recombinant TM protein is more rapid than that observed for the intact glycoprotein expressed from the simian virus 40 vector and is required for its transport out of the endoplasmic reticulum. Oligomeric TM is terminally glycosylated in the Golgi complex but is less stable than the intact wild-type protein and does not accumulate at the cell surface. The SU protein, in contrast, does not form detectable oligomers but is efficiently secreted into the culture medium. These observations suggest that the oligomerization domain of the Rous sarcoma virus glycoprotein lies in the TM protein and that it can function independently of SU.