Serological studies with low-molecular-weight polypeptides from the Moloney strain of murine leukemia virus

Abstract

Major virion low-molecular-weight polypeptides were isolated from the Moloney strain of murine leukemia virus (type C) by agarose chromatography in 6M guanidine hydrochloride and were shown to have molecular weights of 15,000 (p15), 12,000 (p12), and 10,000 (p10) by their elution volumes and by their relative mobilities in sodium dodecyl sulfate-polyacrylamide gels. Each polypeptide could be iodinated and employed in double antibody radioimmunoassay procedures. All three polypeptides demonstrated a high degree of type-specificity in serologic immunoprecipitation analysis and in corresponding competition immunoassays. The p15 was immunologically distinct from other viron polypeptides including p12 and p10; the p12 and p10 were highly related to each other but not to other virion polypeptides and were even more type-specific than the p15 in serologic tests. Competition immunoassays with p15 and p10 indicate that the Moloney strain of MuLV is only a distant relative of the Friend-Rauscher group. The combined use of the Kirsten and Moloney low-molecular-weight polypeptide immunoassays suggest that xenotropic viruses constitute yet another group(s) of murine leukemia virus with distinct type-specific antigens, further expanding an already heterogeneous group of mouse type C viruses.