Abstract
Treatment of murine leukemia virus (MuLV) with nonionic detergents in Tris-buffered saline resulted in solubilization of the membrane and degradation of the core. An appreciable fraction of the core survived as a stable particle whose physical and chemical properties are consistent with published values for MuLV core only if phosphate was present in the medium. The stability of the core in phosphate-buffered detergent indicates that protein-protein interactions other than simple hydrophobic aggregation are primarily responsible for the structural integrity of the viral core. The stabilizing effect of phosphate was found to be much stronger in phosphate esterified to peptide. This suggests a possible role for the phosphorylation of the gag gene-coded polyprotein, Pr65 gag.
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