J. Chang et Yc. Sung, HUMAN FOAMY VIRUS BEL1 PROTEIN PRODUCED IN ESCHERICHIA-COLI AND INSECT CELLS IS BIOLOGICALLY FUNCTIONAL, Molecules and cells, 5(4), 1995, pp. 311-316
The Bell protein of human foamy virus (HFV) is a transcriptional trans
activator that activates gene expression directed by the homologous lo
ng terminal repeat (LTR) and human immuno-deficiency virus type 1 LTR.
Here, we overexpressed and purified the wild type and several transac
tivation-deficient mutant Bell proteins in Escherichia coli as maltose
binding protein fusion proteins, The wild type Bell protein, but not
mutant proteins, is shown to function efficiently in transactivating t
he HFV LTR-linked chloramphenicol acetyltransferase gene by protein up
take experiment. In addition, Bell is expressed as a 36 kDa protein in
insect cells by the baculovirus expression system, featuring the same
molecular weight as that of HFV-infected cells. The experiment of the
cell fusion between baculovirus-infected Sf9 cells and COS-7 cells de
monstrates that the Bell protein expressed in insect cells is capable
of activating HFV LTR-directed gene expression.