Opacity proteins of neisseria gonorrhoeae in lipooligosaccharide mutants lost ability to interact with neutrophil-restricted CEACAM3 (CD66d).
10.1007/s11596-016-1589-4
- Author:
Song ZHANG
1
;
Ya-Ting TU
1
;
Hua-Hua CAI
2
;
Hong-Hui DING
2
;
Qiao LI
2
;
Ying-Xia HE
2
;
Xin-Xin LIU
1
;
Xin WANG
1
;
Feng HU
3
;
Tie CHEN
4
;
Hong-Xiang CHEN
5
Author Information
1. Department of Dermatology, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430022, China.
2. Division of Clinical Immunology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430030, China.
3. Department of Dermatology, Wuhan First Hospital, Wuhan, 430022, China.
4. Division of Clinical Immunology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430030, China. chentie@hust.edu.cn.
5. Department of Dermatology, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430022, China. hongxiangchen@hotmail.com.
- Publication Type:Journal Article
- Keywords:
Neisseria gonorrhoeae;
alpha-oligosaccharide;
chemiluminescence;
opacity proteins
- MeSH:
Antigens, Bacterial;
chemistry;
genetics;
immunology;
metabolism;
Carbohydrate Sequence;
Carcinoembryonic Antigen;
genetics;
immunology;
Gene Expression Regulation;
HeLa Cells;
Host-Pathogen Interactions;
Humans;
Lipopolysaccharides;
chemistry;
immunology;
Luminescent Measurements;
Mutation;
Neisseria gonorrhoeae;
genetics;
metabolism;
pathogenicity;
Neutrophils;
immunology;
microbiology;
Phagocytosis
- From:
Journal of Huazhong University of Science and Technology (Medical Sciences)
2016;36(3):344-349
- CountryChina
- Language:English
-
Abstract:
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 (lgtF mutant) significantly impairs invasion of GC into epithelial cell lines. GC opacity (Opa) proteins, such as OpaI, 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 OpaI-expressing lgtF mutant on phagocytosis by HeLa-CEACAM3 cells and chemiluminescence responses in neutrophils. The results showed that lgtF mutant even expressing OpaI completely lost the ability to promote either phagocytosis mediated by CEACAM3 interaction in HeLa cells or chemiluminescence responses in neutrophils. These data indicated that Opa proteins in the lgtF mutant, which might result from the conformational change, cannot be functional.
