An analysis of type-C retrovirus polypeptides and their associations in the virion.

The polypeptide compositions of ³H]leucine-labeled Prague-Rous sarcoma virus-subgroup C (Pr-RSV-C) and Friend murine leukemia virus (FLV) were investigated using guanidine hydrochloride gel filtration and a high-resolution SDS-polyacrylamide-gel system. These techniques resolved seven major structural components in Pr-RSV-C (gp85, gp35, p27, p19, p12, p15, and p10), as reported previously for other avian leukosis-sarcoma viruses. However, in the case of FLV two previously unresolved proteins (p15E and p12E) were clearly demonstrated in addition to gp71, p30, p15C, p12, and p10. FLV p15E, p12E, and gp71 were removed when intact virions were digested with bromelain, whereas the remaining components were not affected. These and other studies support the notion that gp71, p15E, and p12E are situated on the surface of the virion. The linkages (covalent and noncovalent) between viral polypeptides were also examined. The results of these studies indicate that more than 90% of avian gp85 and gp35 are disulfide linked as a viral glycoprotein complex (VGP). The data also suggests that p19 exists as a network of disulfide-linked molecules, some of which may be further linked to VGP. In contrast to the avian system, only about 10–15% of FLV gp71 is disulfide linked to p15E in the VGP complex; the remaining gp71 is apparently loosely attached to the virus, perhaps by a noncovalent interaction with p12E. The implications of these associations to virus structure and assembly are discussed.