Specific TonB-ExbB-ExbD energy transduction systems required for ferric enterobactin acquisition in Campylobacter
文献类型: 外文期刊
作者: Zeng, Ximin 1 ; Xu, Fuzhou 1 ; Lin, Jun 1 ;
作者机构: 1.Univ Tennessee, Dept Anim Sci, Knoxville, TN 37996 USA
2.Beijing Acad Agr & Forestry Sci, Inst Anim Sci & Vet Med, Beijing, Peoples R China
关键词: iron uptake;molecular mechanism;siderophore
期刊名称:FEMS MICROBIOLOGY LETTERS ( 影响因子:2.742; 五年影响因子:2.856 )
ISSN: 0378-1097
年卷期: 2013 年 347 卷 1 期
页码:
收录情况: SCI
摘要: Ferric enterobactin (FeEnt) acquisition plays a critical role in the pathophysiology of Campylobacter, the leading bacterial cause of human gastroenteritis in industrialized countries. In Campylobacter, the surface-exposed receptor, CfrA or CfrB, functions as a gatekeeper' for initial binding of FeEnt. Subsequent transport across the outer membrane is energized by TonB-ExbB-ExbD energy transduction systems. Although there are up to three TonB-ExbB-ExbD systems in Campylobacter, the cognate components of TonB-ExbB-ExbD for FeEnt acquisition are still largely unknown. In this study, we addressed this issue using complementary molecular approaches: comparative genomic analysis, random transposon mutagenesis and site-directed mutagenesis in two representative C.jejuni strains, NCTC 11168 and 81-176. We demonstrated that CfrB could interact with either TonB2 or TonB3 for efficient Ent-mediated iron acquisition. However, TonB3 is a dominant player in the CfrA-dependent pathway. The ExbB2 and ExbD2 components were essential for both CfrA- and CfrB-dependent FeEnt acquisition. Sequences analysis identified potential TonB boxes in CfrA and CfrB, and the corresponding binding sites in TonB. In conclusion, these findings identify specific TonB-ExbB-ExbD energy transduction components required for FeEnt acquisition, and provide insights into the complex molecular interactions of FeEnt acquisition systems in Campylobacter.
- 相关文献
作者其他论文 更多>>
-
Identification of Host-Protein Interaction Network of Canine Parvovirus Capsid Protein VP2 in F81 Cells
作者:Zhou, Hongzhuan;Zhang, Huanhuan;Su, Xia;Xu, Fuzhou;Xiao, Bing;Zhang, Jin;Qi, Qi;Lin, Lulu;Cui, Kaidi;Li, Qinqin;Li, Songping;Yang, Bing;Zhang, Huanhuan;Cui, Kaidi;Li, Qinqin;Li, Songping
关键词:CPV; VP2; protein interaction network; FHL2
-
Zinc methionine mitigates intestinal mucosal injury of broilers challenged with Salmonella by modulating mucus secretion, tight junction and microbial composition
作者:Shao, Yuxin;Wang, Zheng;Sun, Huiling;Cui, Yifang;Guo, Fangfang;Xu, Fuzhou;Suo, Yanrui;Lin, Dongmei;Ma, Tenghe
关键词:Zinc methionine; Salmonella; Mucus; Intestinal microbiota; Zinc methionine; Salmonella; Mucus; Intestinal microbiota
-
Transcriptional Differential Analysis of Nitazoxanide-Mediated Anticanine Parvovirus Effect in F81 Cells
作者:Su, Xia;Zhou, Hongzhuan;Han, Ziwei;Xu, Fuzhou;Xiao, Bing;Zhang, Jin;Qi, Qi;Lin, Lulu;Zhang, Huanhuan;Li, Songping;Yang, Bing;Han, Ziwei;Zhang, Huanhuan;Li, Songping
关键词:canine parvovirus; nitazoxanide; RNA-seq; cell cycle
-
Chaperonin TRiC/CCT subunit CCT7 is involved in the replication of canine parvovirus in F81 cells
作者:Su, Xia;Zhou, Hongzhuan;Xu, Fuzhou;Zhang, Jin;Xiao, Bing;Qi, Qi;Lin, Lulu;Yang, Bing
关键词:canine parvovirus; CCT7; VP2; replication; stability
-
Assessment of probiotic Bacillus velezensis supplementation to reduce Campylobacter jejuni colonization in chickens
作者:Cui, Yifang;Li, Pengxiang;Guo, Fangfang;Yang, Bing;Su, Xia;Zhou, Hongzhuan;Xu, Fuzhou;Zhu, Jiajia;Zhu, Kui
关键词:probiotic; Bacillus velezensis; antimicrobial activity; Campylobacter jejuni; chicken
-
Effects of OxyR regulator on oxidative stress, Apx toxin secretion and virulence of Actinobacillus pleuropneumoniae
作者:Guo, Fangfang;Quan, Rong;Cui, Yifang;Cao, Xiaoya;Xu, Fuzhou;Wen, Tong
关键词:Actinobacillus pleuropneumoniae; oxyR gene; Apx toxins; oxidative stress; virulence
-
The absence of luxS reduces the invasion of Avibacterium paragallinarum but is not essential for virulence
作者:Li, Donghai;Qiao, Jian;Li, Donghai;Huo, Caiyun;Li, Guiping;Zhu, Menghan;Xu, Fuzhou;Sun, Huiling
关键词:quorum sensing; LuxS; autoinducer-2; Avibacterium paragallinarum; virulence



