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J. Virol., Feb 1995, 1093-1098, Vol 69, No. 2
Copyright © 1995, American Society for Microbiology

Efficient in vivo and in vitro assembly of retroviral capsids from Gag precursor proteins expressed in bacteria

M Klikova, SS Rhee, E Hunter and T Ruml
Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague, Czech Republic.

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.


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