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Herpes Simplex Virus Type 1 마우스 뇌염모델에서의 조직내 바이러스 증식 및 재활성에 미치는 Acyclovir의 약효
이종교(Jong Gyo Lee),김지현(Ji Hyun Kim),배판기(Pan Gee Bae),피미경(Mi Gyung Pi),김해수(Hae Soo Kim) 대한바이러스학회 1999 Journal of Bacteriology and Virology Vol.29 No.3
To investigate viral pathogenesis and in vivo efficacy of acyclovir (ACV) in mouse HSV-1 encephalitis models, female BALB/c mice aged 5 weeks were inoculated with strain F either intranasally (IN) or intracerebrally (IC). ACV-treatment by intraperitorneal injection with 0, 5, 10 and 25 mg/kg b.i.d. for 6 days was commenced 1 h after infection. Body weight and signs of clinical disease were noted daily up to 2 weeks. ED50 of ACV in IN infection was <5 mg/kg and 14.1 mg/kg in IC infection. Tissues of central nervous system were collected from 2 mice per group everyday up to 5 day p.i. and the virus titers were measured. In IN infection model, high titers in eyes and trigeminal nerves were observed. ACV-treatment showed significant reduction of the titers in all the isolated. In IC infection model, cerebrum, cerebellum and brain stem showed high virus titers. ACV-treatment showed less significant reduction of virus titers than that in IN infection model. Reactivation of explanted trigeminal nerves from mice 30 day p.i. was monitored. In all of ACV treated mice reactivation was observed, i.e. even the highest dose of ACV did not inhibit the establishment of viral latency.
Herpes Simplex Virus Type 1 Protease의 발현 및 분리 정제
배판기(Pan Gee Bae),팽진욱(Jin Wook Paeng),김지현(Ji Hyun Kim),김해수(Hae Soo Kim),백상기(Sang Gee Baek),정인권(In Gwon Jung),이종교(Jong Gyo Lee) 대한바이러스학회 1999 Journal of Bacteriology and Virology Vol.29 No.3
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.