[Expression of the Epstein-Barr virus terminal repeat protein 1 in Escherichia coli cells].
A pMAL-vector-based plasmid clone with synthetic tac-promotor effectively expressing full-length terminal repeats protein 1 (TP1) of Epstein-Barr virus (EBV) in E. coli was constructed. It is important that the N-terminal region of recombinant TP1 was represented by a maltose-binding protein. The latter can be used to separate TP1 from bacterial lysate by affinity chromatography. Moreover, after treatment with the proteolytic factor Xa, full-length TP1 can be recovered in a discrete form. On the basis of the pATH tryptophan-regulated vector, several plasmid clones expressing different fragments of N- and C-terminal regions of TP1 were also constructed. This collection of recombinant proteins could be used as an important tool for obtaining corresponding antisera and for immunological mapping of the TP1 molecule.
Afanas'eva
T A
TA
Pavlish
O A
OA
Kistoglu
Kh
Kh
Gurtsevich
V E
VE
D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics*; D004854:Herpesvirus 4, Human / Q000378:metabolism*; D010957:Plasmids; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012091:Repetitive Sequences, Nucleic Acid; D012995:Solubility; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics*
D011994:Recombinant Proteins; D014764:Viral Proteins
Ekspressiia belka terminal'nogo povtora 1 virusa Epshteĭna-Barr v kletkakh Escherichia coli.