Biochemical and immunological characterization of the major envelope glycoprotein gp69/71 and degradation fragments from Rauscher leukemia virus.
Analysis of the proteins of Rauscher murine oncornavirus by immunoprecipitation showed that antiserum to the purified envelope glycoprotein of approximately 69,000 and 71,000 daltons (gp69/71) reacted as well with a number of other components of several murine oncornaviruses of approximately 45,000, 32,000, and 15,000 daltons. Polypeptides of similar size were also produced by limited proteolysis of purified gp69/71; these degradation fragments were shown to contain carbohydrate by the incorporation of (3)H from sodium boro[(3)H]hydride after neuraminidase and galactose oxidase treatment. Each of these glycoproteins was isolated by preparative polyacrylamide gel electrophoresis and was analyzed by tryptic peptide mapping. The major virion components of 69,000 and 71,000 daltons were nearly identical, as were the primary degradation fragments. Analysis of the immunological properties of the glycoproteins showed that the 71,000-, 69,000-, and 32,000-dalton glycoproteins behaved similarly with respect to type and group-specific antigenic determinants. In contrast, the 45,000-dalton glycoprotein lacked detectable interspecies and some of the group-specific reactivity. Components of about 45,000 and 32,000 daltons isolated directly from virions were also identified as constituents of the major envelope glycoprotein by immune precipitation and tryptic peptide mapping. These results indicate that all of the examined virion glycoproteins of approximately 71,000, 69,000, 45,000, and 32,000 daltons are derived from the same viral gene and that these lower-molecular-weight glycoproteins can readily be produced from the major envelope glycoprotein.