Efficient in vivo and in vitro assembly of retroviral capsids from Gag precursor proteins expressed in bacteria.
The capsid precursor protein (Gag) of Mason-Pfizer monkey virus, the prototype type D retrovirus, has been expressed to high levels in bacteria under the control of the phage T7 promoter. Electron microscopic studies of induced cells revealed the assembly of capsid-like structures within inclusion bodies that formed at the poles of the cells 6 h after induction with isopropyl-beta-D-thiogalactopyranoside (IPTG). The inclusion bodies and enclosed capsid-like structures were solubilized completely in 8 M urea, but following renaturation, we observed assembly in vitro of capsid-like structures that demonstrated apparent icosahedral symmetry. These results demonstrate for the first time that retroviral capsid precursors have the propensity to self-assemble in vitro and point to new approaches for the analysis of retroviral assembly and structure.[1]References
- Efficient in vivo and in vitro assembly of retroviral capsids from Gag precursor proteins expressed in bacteria. Klikova, M., Rhee, S.S., Hunter, E., Ruml, T. J. Virol. (1995) [Pubmed]
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