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We followed maturation of the glycosylated envelope polyprotein Pr80env of a murine retrovirus by using antisera specific to subregions of the protein, including an antiserum directed against a synthetic peptide corresponding to the COOH-terminus of Pr80env. Shortly after synthesis and glycosylation, Pr80env is cleaved into two species, gp70 and Pr15E, that are found associated, perhaps through disulfide bonds, in infected cells. Pr15E is further cleaved at the time of virus maturation to form virus protein p15E. NH2-Terminal protein sequence analysis showed that Pr15E had an NH2 terminus in common with p15E. Pr15E, but not p15E, is precipitated by antibody against the COOH-terminal peptide; hence, p15E is missing a peptide at the COOH-terminus. Our data indicate that Pr15E is the predominant species in cells and p15E is the major species in virus.

Sequence-specific antibodies show that maturation of Moloney leukemia virus envelope polyprotein involves removal of a COOH-terminal peptide.