Mutant cells that abnormally process plasma membrane glycoproteins encoded by murine leukemia virus.

Wild-type normal rat kidney fibroblasts infected with the Friend strain of murine leukemia virus (MuLV) contain two virus-encoded glycoproteins on the outer surfaces of their plasma membranes: an envelope glycoprotein with an apparent molecular weight of 70,000 (gp70), and a glycoprotein that reacts with antisera to the major virion internal core proteins p30, p15, p12 and p10 and has an apparent molecular weight of 93,000 (gp93gag). To analyze the functions of these glycoproteins and to develop a model system for studying genetics of membrane synthesis, we used an immunoselection method to isolate variant cell clones defective in processing these glycoproteins into their plasma membranes. Several lines of evidence, including complementation of glycoprotein processing defects by fusion with uninfected wild-type cells, indicate that the immunoselected variants have stably inherited membrane synthesis abnormalities that are encoded by cellular rather than by viral genes. The H-4 cell line, which was selected by use of antiserum to gp70, has metabolic defects that interfere with processing of both gp70 and gp93gag into its plasma membranes. Nevertheless, this cell line releases noninfectious MuLV. Furthermore, two cell lines (2 and 5), which were selected by use of antiserum to the virion core protein p30, specifically lack detectable cell surface or intracellular gp93gag but contain cell surface gp70 and release infectious MuLV. These results suggest that MuLV particles can bud efficiently from cells that lack known virus-encoded plasma membrane constituents.