Human immunodeficiency virus protease expressed in Escherichia coli exhibits autoprocessing and specific maturation of the gag precursor.
The mature gag and pol proteins of human immunodeficiency virus (HIV) and all retroviruses derive from large gag and gag-pol polyprotein precursors by posttranslational cleavage. A highly specific, virally encoded protease is required for this essential proteolytic processing. In this study, the HIV protease gene product was expressed in Escherichia coli and shown to autocatalyze its maturation from a larger precursor. In addition, this bacterially produced HIV protease specifically processed an HIV p55 gag polyprotein precursor when coexpressed in E. coli. This system will allow detailed structure-function analysis of the HIV protease and provides a simple assay for the development of potential therapeutic agents directed against this critical viral enzyme.
Debouck
C
C
Department of Molecular Genetics, Smith Kline and French Laboratories, King of Prussia, PA 19406.
Gorniak
J G
JG
Strickler
J E
JE
Meek
T D
TD
Metcalf
B W
BW
Rosenberg
M
M
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D010450:Endopeptidases / Q000235:genetics*; D004926:Escherichia coli / Q000378:metabolism; D015683:Gene Products, gag; D005814:Genes, Viral; D006678:HIV / Q000201:enzymology* / Q000235:genetics; D016333:HIV Protease; D008970:Molecular Weight; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins; D012191:Retroviridae Proteins / Q000378:metabolism*
D015683:Gene Products, gag; D011994:Recombinant Proteins; D012191:Retroviridae Proteins; D010450:Endopeptidases; D016333:HIV Protease