Studies on antibacterial activity and endotoxin neutralization of murine BPI N-terminal functional fragment(muBPI_(25) protein)in vitro
10.3969/j.issn.1000-484X.2010.04.002
- VernacularTitle:小鼠BPI N端功能片段(muBPI_(25)蛋白)体外杀菌和中和内毒素作用研究
- Author:
Zhe Lü
;
Wei WANG
;
Yiqiang FAN
;
Zhenlong LIU
;
Qingli KONG
;
Mingjie WEN
;
Jun LONG
;
Chen LI
;
Qing XU
;
Yunqing AN
- Publication Type:Journal Article
- Keywords:
Bactericidal/permeability-increasing protein;
RAW264.7 cell line;
Intracelltdar bacterial parasite;
Endotoxin
- From:
Chinese Journal of Immunology
2010;26(4):294-297,303
- CountryChina
- Language:Chinese
-
Abstract:
Objective:To establish an experimental model for intracellular antibacteria and endotoxin neutralization in vitro to detect the antibacterial and endotoxin neutralization activity of the muBPI_(25) protein.Methods: RAW264.7 cells were transfected with pcDNA3.1(+)muBPI_(36-259), and then were infected with intracellular bacterial of either G ~+/G~-to establish the experimental model of intracellalar antibacteria.The RAW264.7 cells were co-transfected with the pSecTag2B-muBPI_(36-259) and dual-luciferase reporter gene plasmids for establishment of the experimental model of endotoxin neutralization.Results:The experimental model of intracellular antibacteria confirmed that the muBPI_(25) protein could inhibit/kill Salmonella typhi.The experimental model of endotoxin neutralization indicated that the muBPI_(25) protein could neutralize endotoxin.Conelusion: We firstly demonstrate that murine BPI N-terminal functional fragment(muBPI_(25) protein)can inhibit/kill Salmonella typhi,and can neutralize, its lysating product, endotoxin.
