Processed enzymatically active protease (p15gag) of avian retrovirus obtained in an E. coli system expressing a recombinant precursor (Pr25lac‐Δgag)

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Abstract
Processing proteases of avian and mammalian retroviruses cut the polyprotein precursors encoded by the retroviral genes into mature functional proteins. Retroviral processing proteases are still a rather poorly characterized group as to their relation to other proteases, specificity, and mechanism of enzymatic action. In avian retroviruses the generation of the processing protease itself comprises a processing cleavage event — the protease p15 gag is cut off the carboxy‐terminus of a gag polyprotein precursor, Pr76 gag . We report here that direct and efficient production of the avian retrovirus processing protease p15 gag (required for structure‐function studies and rational design of inhibitors) was obtained in an E. coli system, where massive expression of a size‐reduced, recombinant precursor (Pr25 lac‐Δgag was accompanied by its structurally accurate processing.