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J Virol. 1979 July; 31(1): 1-7

Glycopeptides of Murine Leukemia Viruses I. Comparison of Two Ecotropic Viruses

Department of Microbiology, University of Alabama Medical Center, Birmingham, Alabama 35294

ABSTRACT

The glycopeptides obtained by pronase digestion of two ecotropic strains of murine leukemia virus (MuLV) were compared by gel filtration. Four different glycopeptide size classes, designated G₁, G₂, G₃, and G₄, with molecular weights of approximately 5,100, 2,900, 2,200, and 1,500, respectively, were shown to be associated with Rauscher MuLV virions grown in JLS-V9 cells. Various sugar precursors, including glucosamine, galactose, fucose, and mannose were incorporated into G₁ and G₂, suggesting that these are complex (type I) glycopeptides. The two smaller glycopeptide size classes, G₃ and G₄, were shown to be mannoserich (type II) glycopeptides. G₄ was more sensitive to digestion with endo-ß-N-acetylglucosaminidase H than G₃, suggesting that the core of G₃ may contain fewer mannose residues. Glycopeptides of the same size class as G₁ and G₂ were associated with both Rauscher MuLV and AKR-MuLV grown in III6A (mouse embryo) cells. Previous studies have shown that gp52, a proteolytic cleavage product of gp70, possessed primarily G₁ glycopeptides and that gp52 was more highly sulfated than gp70. We observed that G₁ is approximately twofold more highly sulfated than G₂, explaining the observed difference in sulfation of gp52. The unusually large size of G₁ suggested that infection with MuLV may alter the host cell glycosylation pattern. To test this possibility, glycopeptides from Sindbis virions grown in uninfected and Rauscher MuLV-infected JLS-V9 cells were compared, and no differences were observed. G₁ was not detected in Sindbis virions, indicating that acquisition of G₁ depends on properties of the virus-coded polypeptide backbone of the gp70 molecule.