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MPMV precursor polypeptide Pr78 Gag  orchestrates assembly and packaging of genomic RNA (gRNA) into virus particles. Therefore, we have expressed recombinant full-length Pr78 Gag  either with or without His 6 -tag in bacterial as well as eukaryotic cultures and purified the recombinant protein from soluble fractions of the bacterial cultures. The recombinant Pr78 Gag  protein has the intrinsic ability to assemble  in vitro  to form virus like particles (VLPs). Consistent with this observation, the recombinant protein could form VLPs in both prokaryotes and eukaryotes. VLPs formed in eukaryotic cells by recombinant Pr78 Gag  with or without His 6 -tag can encapsidate MPMV transfer vector RNA, suggesting that the inclusion of the His 6 -tag to the full-length Pr78 Gag  did not interfere with its expression or biological function. This study demonstrates the expression and purification of a biologically active, recombinant Pr78 Gag , which should pave the way to study RNA-protein interactions involved in the MPMV gRNA packaging process.

Expression, purification, and characterization of biologically active full-length Mason-Pfizer monkey virus (MPMV) Pr78Gag