Expression and Purification of Herpes Simplex Virus Type 1 Protease.
- Author:
Pan Kee BAE
1
;
Jin Wook PAENG
;
Jee Hyun KIM
;
Hae Soo KIM
;
Sang Gi PAIK
;
In Kwon CHUNG
Author Information
1. Pharmaceutical Screening Center, Korea Research Institute of Chemical Technology, Taejon 305-600, Korea.
- Publication Type:Original Article
- Keywords:
Herpes simplex virus type1;
Protease gene;
Nucleotide sequence analysis;
HPLC
- MeSH:
Amino Acid Sequence;
Base Sequence;
Catalytic Domain;
Chromatography, High Pressure Liquid;
Chromatography, Liquid;
Clone Cells;
DNA Packaging;
Drug Therapy;
Herpes Simplex*;
Herpesvirus 1, Human*;
Simplexvirus*
- From:Journal of the Korean Society of Virology
1999;29(3):175-182
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
An attractive target for anti-herpes chemotherapy is the herpes simplex virus 1 (HSV-1) protease encoded by the UL26 gene. HSV-1 protease is essential for DNA packaging and virus maturation. To perform high throughput for potent inhibitors, the efficient production of larger amounts of highly purified enzyme and protease activity assay method must be established. In this report, expression in E. coli and purification of the protease gene of HSV-1 strain F was investigated. The protease gene was cloned pET28, and the nucleotide sequence of protease catalytic domain of HSV-1 compared strain F with other strains (KOS and CL101). In these results the F strain was different in base sequence. However, the amino acid sequence was identifical. The HSV-1 protease was purified with His-tagged affinity column. The analysis of HSV-1 protease activity Was performed by high performance liquid chromatography.
