Opacity Proteins of Neisseria Gonorrhoeae in Lipooligosaccharide Mutants Lost Ability to Interact with Neutrophil-restricted CEACAM3(CD66d)  

作　　者：张颂 涂亚庭 蔡华华 丁红辉 李俏 何应霞 刘欣欣 王新 胡枫 陈铁 陈宏翔 

机构地区：[1]Department of Dermatology,Union Hospital,Tongji Medical College,Huazhong University of Science and Technology [2]Division of Clinical Immunology,Tongji Hospital,Tongji Medical College,Huazhong University of Science and Technology [3]Department of Dermatology,Wuhan First Hospital

出　　处：《Journal of Huazhong University of Science and Technology(Medical Sciences)》2016年第3期344-349,共6页华中科技大学学报（医学英德文版）

基　　金：partly supported by grants from National Natural Science Foundation of China(No.81171495 and No.81271780);the Youth Chenguang Project of Science and Technology of Wuhan City of China(No.2015071704011621)

摘　　要：Lipooligosacharide（LOS） of Neisseria gonorrhoeae（gonococci, GC） is involved in the interaction of GC with host cells. Deletion of the alpha-oligosaccharide（alpha-OS） moiety of LOS（lgt F mutant） significantly impairs invasion of GC into epithelial cell lines. GC opacity（Opa） proteins, such as Opa I, mediate phagocytosis and stimulate chemiluminescence responses in neutrophils in part through interaction with members of the carcinoembryonic antigen（CEA） family, which includes CEACAM3（CD66d）, a human neutrophil specific receptor for phagocytosis of bacteria. In the present work, we examined the effects of Opa I-expressing lgt F mutant on phagocytosis by He La-CEACAM3 cells and chemiluminescence responses in neutrophils. The results showed that lgt F mutant even expressing Opa I completely lost the ability to promote either phagocytosis mediated by CEACAM3 interaction in He La cells or chemiluminescence responses in neutrophils. These data indicated that Opa proteins in the lgt F mutant, which might result from the conformational change, cannot be functional.Lipooligosacharide（LOS） of Neisseria gonorrhoeae（gonococci, GC） is involved in the interaction of GC with host cells. Deletion of the alpha-oligosaccharide（alpha-OS） moiety of LOS（lgt F mutant） significantly impairs invasion of GC into epithelial cell lines. GC opacity（Opa） proteins, such as Opa I, mediate phagocytosis and stimulate chemiluminescence responses in neutrophils in part through interaction with members of the carcinoembryonic antigen（CEA） family, which includes CEACAM3（CD66d）, a human neutrophil specific receptor for phagocytosis of bacteria. In the present work, we examined the effects of Opa I-expressing lgt F mutant on phagocytosis by He La-CEACAM3 cells and chemiluminescence responses in neutrophils. The results showed that lgt F mutant even expressing Opa I completely lost the ability to promote either phagocytosis mediated by CEACAM3 interaction in He La cells or chemiluminescence responses in neutrophils. These data indicated that Opa proteins in the lgt F mutant, which might result from the conformational change, cannot be functional.

关 键 词：Neisseria gonorrhoeae chemiluminescence alpha-oligosaccharide opacity proteins 

分 类 号：R759.2[医药卫生—皮肤病学与性病学]